Lipocalin 2: An Emerging Player in Iron Homeostasis and Inflammation

Xiao, Xia; Yeoh, Beng San; Vijay-Kumar, Matam

doi:10.1146/annurev-nutr-071816-064559

Cited by 426Iron Metabolism and DisordersFerroptosis and cancer prognosisHemoglobin structure and function

The DOI matches its Crossref record; 204 of the 204 references it cites were found in a registry or an index.

Lipocalin 2: An Emerging Player in Iron Homeostasis and Inflammation

Open access

Xiao, Xia, Yeoh, Beng San, Vijay-Kumar, Matam·2017·Annual Review of Nutrition

DOI 10.1146/annurev-nutr-071816-064559

Open this paper in CoChat — free account Open PDF

Abstract

Lipocalin 2 (Lcn2), an innate immune protein, has emerged as a critical iron regulatory protein during physiological and inflammatory conditions. As a bacteriostatic factor, Lcn2 obstructs the siderophore iron-acquiring strategy of bacteria and thus inhibits bacterial growth. As part of host nutritional immunity, Lcn2 facilitates systemic, cellular, and mucosal hypoferremia during inflammation, in addition to stabilizing the siderophore-bound labile iron pool. In this review, we summarize recent advances in understanding the interaction between Lcn2 and iron, and its effects in various inflammatory diseases. Lcn2 exerts mostly a protective role in infectious and inflammatory bowel diseases, whereas both beneficial and detrimental functions have been documented in neurodegenerative diseases, metabolic syndrome, renal disorders, skin disorders, and cancer. Further animal and clinical studies are necessary to unveil the multifaceted roles of Lcn2 in iron dysregulation during inflammation and to explore its therapeutic potential for treating inflammatory diseases.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1146/annurev-nutr-071816-064559

Cites

204 of 204 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Lipocalin-2 sequesters high-affinity metal-binding siderophores released by pathogenic bacteria, preventing their uptake.
“Lipocalin-2 sequesters the high affinity metal binding siderophore molecules released by pathogenic bacteria to prevent uptake (Xiao et al., 2017).”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Xiao et al., 2017
Infiltrating neutrophils and macrophages block bacterial iron acquisition in part by releasing lipocalin-2.
“Infiltrating neutrophils and macrophages block bacterial iron acquisition in part by releasing the protein lipocalin-2 (Xiao et al., 2017).”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Xiao et al., 2017

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Epithelial–mesenchymal transitions in tumour progression
Thiery, J. P. (2002) · Nature reviews. Cancer · doi:10.1038/nrc822 · Cited by 6,767
Metabolic Syndrome and Altered Gut Microbiota in Mice Lacking Toll-Like Receptor 5
Vijay-Kumar, M., Aitken, J. D., Carvalho, F. A., Cullender, T. C., Mwangi, S., Srinivasan, S., Sitaraman, S. V., Knight, R., Ley, R. E., & Gewirtz, A. T. (2010) · Science · doi:10.1126/science.1179721 · Cited by 2,068
Self-citation
The epidemiology of global micronutrient deficiencies
Bailey, R. L., West Jr., K. P., & Black, R. E. (2015) · Annals of Nutrition and Metabolism · doi:10.1159/000371618 · Cited by 2,035
Matrix metalloproteinases and tumor metastasis
Deryugina, E. I., & Quigley, J. P. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-7886-9 · Cited by 1,974
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819
Chemistry and biology of siderophores
Hider, R. C., & Kong, X. (2010) · Natural Product Reports · doi:10.1039/b906679a · Cited by 1,722
Iron and cancer: more ore to be mined
Torti, S. V., & Torti, F. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3495 · Cited by 1,621
The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition
Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Inflammation in neurodegenerative diseases
Amor, S., Puentes, F., Baker, D., & Van Der Valk, P. (2010) · Immunology · doi:10.1111/j.1365-2567.2009.03225.x · Cited by 1,355
Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
Kjeldsen, L., Johnsen, A., Sengeløv, H., & Borregaard, N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82217-7 · Cited by 1,286
Hepcidin and iron homeostasis
Ganz, T., & Nemeth, E. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.014 · Cited by 1,282
Iron metabolism and toxicity
Papanikolaou, G., & Pantopoulos, K. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.06.021 · Cited by 1,070
Increased nigral iron content in postmortem parkinsonian brain
Dexter, D. T., Wells, F. R., Agid, F., Agid, Y., Lees, A. J., Jenner, P., & Marsden, C. D. (1987) · The Lancet · doi:10.1016/s0140-6736(87)91361-4 · Cited by 963
Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury
Mori, K., Lee, H. T., Rapoport, D., Drexler, I. R., Foster, K., Yang, J., Schmidt-Ott, K. M., Chen, X., Li, J. Y., Weiss, S., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23056 · Cited by 954
The lipocalin protein family: structural and sequence overview
Flower, D. R., North, A. C. T., & Sansom, C. E. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00148-5 · Cited by 868
The transferrin receptor and the targeted delivery of therapeutic agents against cancer
Daniels, T. R., Bernabeu, E., Rodríguez, J. A., Patel, S., Kozman, M., Chiappetta, D. A., Holler, E., Ljubimova, J. Y., Helguera, G., & Penichet, M. L. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.016 · Cited by 807
Dual Action of Neutrophil Gelatinase–Associated Lipocalin
Schmidt-Ott, K. M., Mori, K., Li, J. Y., Kalandadze, A., Cohen, D. J., Devarajan, P., & Barasch, J. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080882 · Cited by 772
Altered Brain Metabolism of Iron as a Cause of Neurodegenerative Diseases?
Gerlach, M., Ben‐Shachar, D., Riederer, P. F., & Youdim, M. B. H. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030793.x · Cited by 704
Iron and Its Relation to Immunity and Infectious Disease
Oppenheimer, S. J. (2001) · The Journal of Nutrition · doi:10.1093/jn/131.2.616s · Cited by 695
The High Molecular Weight Urinary Matrix Metalloproteinase (MMP) Activity Is a Complex of Gelatinase B/MMP-9 and Neutrophil Gelatinase-associated Lipocalin (NGAL)
Li, Y., Borregaard, N., Kjeldsen, L., & Moses, M. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106089200 · Cited by 678
A Cell-Surface Receptor for Lipocalin 24p3 Selectively Mediates Apoptosis and Iron Uptake
Devireddy, L. R., Gazin, C., Zhu, X., & Green, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.10.027 · Cited by 672
An Iron Delivery Pathway Mediated by a Lipocalin
Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651
Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo
Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620
Fecal Lipocalin 2, a Sensitive and Broadly Dynamic Non-Invasive Biomarker for Intestinal Inflammation
Chassaing, B., Srinivasan, G., Delgado, M. A., Young, A. N., Gewirtz, A. T., & Vijay–Kumar, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044328 · Cited by 584
Lipocalin-2 Is an Inflammatory Marker Closely Associated with Obesity, Insulin Resistance, and Hyperglycemia in Humans
Wang, Y., Lam, K. S. L., Kraegen, E. W., Sweeney, G., Zhang, J., Tso, A. W., Chow, W.-S., Wat, N. M., Xu, J. Y., Hoo, R. L., et al. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2006.075614 · Cited by 578
Body Iron Stores and the Risk of Cancer
Stevens, R. G., Jones, D. Y., Micozzi, M. S., & Taylor, P. R. (1988) · New England Journal of Medicine · doi:10.1056/nejm198810203191603 · Cited by 575
Probiotic Bacteria Reduce Salmonella Typhimurium Intestinal Colonization by Competing for Iron
Deriu, E., Liu, J. Z., Pezeshki, M., Edwards, R. A., Ochoa, R. J., Contreras, H., Libby, S. J., Fang, F. C., & Raffatellu, M. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.007 · Cited by 550
Microcins mediate competition among Enterobacteriaceae in the inflamed gut
Sassone-Corsi, M., Nuccio, S.-P., Liu, H., Hernandez, D., Vu, C. T., Takahashi, A. A., Edwards, R. A., & Raffatellu, M. (2016) · Nature · doi:10.1038/nature20557 · Cited by 549
Lack of a role for iron in the Lyme disease pathogen
Posey, J. E., & Gherardini, F. C. (2000) · Science · doi:10.1126/science.288.5471.1651 · Cited by 538
Amelioration of Ischemic Acute Renal Injury by Neutrophil Gelatinase-Associated Lipocalin
Mishra, J., Mori, K., Ma, Q., Kelly, C. N., Yang, J., Mitsnefes, M. M., Barasch, J. M., & Devarajan, P. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000145013.44578.45 · Cited by 536
Lipocalin-2 Resistance Confers an Advantage to Salmonella enterica Serotype Typhimurium for Growth and Survival in the Inflamed Intestine
Raffatellu, M., George, M. D., Akiyama, Y., Hornsby, M. J., Nuccio, S.-P., Paixao, T. A., Butler, B. P., Chu, H., Santos, R. L., Berger, T., et al. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.03.011 · Cited by 525
The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer
Chakraborty, S., Kaur, S., Guha, S., & Batra, S. K. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.03.008 · Cited by 503
Iron metabolism in the CNS: implications for neurodegenerative diseases
Rouault, T. A. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3453 · Cited by 496
The Adipokine Lipocalin 2 Is Regulated by Obesity and Promotes Insulin Resistance
Yan, Q.-W., Yang, Q., Mody, N., Graham, T. E., Hsu, C.-H., Xu, Z., Houstis, N. E., Kahn, B. B., & Rosen, E. D. (2007) · Diabetes · doi:10.2337/db07-0007 · Cited by 483
Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury
Berger, T., Togawa, A., Duncan, G. S., Elia, A. J., You-Ten, A., Wakeham, A., Fong, H. E. H., Cheung, C. C., & Mak, T. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510847103 · Cited by 460
Ferroportin and Iron Regulation in Breast Cancer Progression and Prognosis
Pinnix, Z. K., Miller, L. D., Wang, W., D’Agostino, R., Kute, T., Willingham, M. C., Hatcher, H., Tesfay, L., Sui, G., Di, X., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001127 · Cited by 448
Induction of NGAL synthesis in epithelial cells of human colorectal neoplasia and inflammatory bowel diseases.
Nielsen, B. S., Borregaard, N., Bundgaard, J. R., Timshel, S., Sehested, M., & Kjeldsen, L. (1996) · Gut · doi:10.1136/gut.38.3.414 · Cited by 422
Deletion of TLR5 results in spontaneous colitis in mice
Vijay–Kumar, M., Sanders, C. J., Taylor, R. T., Kumar, A., Aitken, J. D., Sitaraman, S. V., Neish, A. S., Uematsu, S., Akira, S., Williams, I. R., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci33084 · Cited by 420
Lipocalin 2 is essential for chronic kidney disease progression in mice and humans
Viau, A., Karoui, K. E., Laouari, D., Burtin, M., Nguyen, C., Mori, K., Pillebout, É., Berger, T., Mak, T. W., Knebelmann, B., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42004 · Cited by 393
Induction of Apoptosis by a Secreted Lipocalin That is Transcriptionally Regulated by IL-3 Deprivation
Devireddy, L. R., Teodoro, J. G., Richard, F. A., & Green, M. R. (2001) · Science · doi:10.1126/science.1061075 · Cited by 380
“Blooming” in the gut: how dysbiosis might contribute to pathogen evolution.
Stecher, B., Maier, L., & Hardt, W.-D. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro2989 · Cited by 378
Lipocalin 2 protects from inflammation and Tumorigenesis associated with gut microbiota alterations
Moschen, A. R., Gerner, R. R., Wang, J., Klepsch, V., Adolph, T. E., Reider, S. J., Hackl, H., Pfister, A., Schilling, J., Moser, P. L., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.03.007 · Cited by 375
Wound Healing and Expression of Antimicrobial Peptides/Polypeptides in Human Keratinocytes, a Consequence of Common Growth Factors
Sørensen, O. E., Cowland, J. B., Theilgaard‐Mönch, K., Liu, L., Ganz, T., & Borregaard, N. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.11.5583 · Cited by 373
Reactive astrocytes secrete lcn2 to promote neuron death
Bi, F., Huang, C., Tong, J., Qiu, G., Huang, B., Wu, Q., Li, F., Xu, Z., Bowser, R., Xia, X.-G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218497110 · Cited by 371
Iron and Cancer Risk—A Systematic Review and Meta-analysis of the Epidemiological Evidence
Fonseca‐Nunes, A., Jakszyn, P. G., & Agudo, A. (2013) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-13-0733 · Cited by 357
Lipocalin 2 promotes breast cancer progression
Yang, J., Bielenberg, D. R., Rodig, S. J., Doiron, R., Clifton, M. C., Kung, A. L., Strong, R. K., Zurakowski, D., & Moses, M. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810617106 · Cited by 356
Neutrophil Gelatinase-Associated Lipocalin Is Up-Regulated in Human Epithelial Cells by IL-1β, but Not by TNF-α
Cowland, J. B., Sørensen, O. E., Sehested, M., & Borregaard, N. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.12.6630 · Cited by 354
The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake
Hvidberg, V., Jacobsen, C. B., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.031 · Cited by 351
Mesenchymal stem cells enhance survival and bacterial clearance in murineEscherichia colipneumonia
Gupta, N., Krasnodembskaya, A. D., Kapetanaki, M. G., Mouded, M., Tan, X., Serikov, V. B., & Matthay, M. A. (2012) · Thorax · doi:10.1136/thoraxjnl-2011-201176 · Cited by 331
Obesity as an emerging risk factor for iron deficiency
Aigner, E., Feldman, A., & Datz, C. (2014) · Nutrients · doi:10.3390/nu6093587 · Cited by 328
How pathogenic bacteria evade mammalian sabotage in the battle for iron
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2006) · Nature Chemical Biology · doi:10.1038/nchembio771 · Cited by 321
Solution equilibria of enterobactin and metal-enterobactin complexes
Loomis, L. D., & Raymond, K. N. (1991) · Inorganic Chemistry · doi:10.1021/ic00005a008 · Cited by 321
The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2
Fischbach, M. A., Lin, H., Zhou, L., Yu, Y., Abergel, R. J., Liu, D. R., Raymond, K. N., Wanner, B. L., Strong, R. K., Walsh, C. T., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604636103 · Cited by 319
Clinical use of E. coli Nissle 1917 in inflammatory bowel disease
Schultz, M. (2008) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20377 · Cited by 310
Klebsiella pneumoniae Yersiniabactin Promotes Respiratory Tract Infection through Evasion of Lipocalin 2
Bachman, M. A., Oyler, J. E., Burns, S. H., Caza, M., Lepine, F. L., Dozois, C. M., & Weiser, J. N. (2011) · Infection and Immunity · doi:10.1128/iai.05114-11 · Cited by 308
Iron traffics in circulation bound to a siderocalin (Ngal)–catechol complex
Bao, G., Clifton, M., Hoette, T. M., Mori, K., Deng, S.-X., Qiu, A., Viltard, M., Williams, D., Paragas, N., Leete, T., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.402 · Cited by 307
The Role of Lipocalin 2 in the Regulation of Inflammation in Adipocytes and Macrophages
Zhang, J., Wu, Y., Zhang, Y., LeRoith, D., Bernlohr, D., & Chen, X. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0420 · Cited by 302
The Origin of Multiple Molecular Forms in Urine of HNL/NGAL
Cai, L., Rubin, J., Han, W., Venge, P., & Xu, S. (2010) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.00980110 · Cited by 300
The potential of lipocalin-2/NGAL as biomarker for inflammatory and metabolic diseases
Abella, V., Scotece, M., Conde, J., Gómez, R., Lois, A., Pino, J., Gómez-Reino, J. J., Lago, F., Mobasheri, A., & Gualillo, O. (2015) · Biomarkers · doi:10.3109/1354750x.2015.1123354 · Cited by 288
Lipocalin-2 Is an Autocrine Mediator of Reactive Astrocytosis
Lee, S., Park, J., Lee, W., Kim, H., Park, H., Mori, K., & Suk, K. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5273-08.2009 · Cited by 286
Lipocalin-2 Deficiency Attenuates Insulin Resistance Associated With Aging and Obesity
Law, I. K. M., Xu, A., Lam, K. S. L., Berger, T., Mak, T. W., Vanhoutte, P. M., Liu, J. T. C., Sweeney, G., Zhou, M., Yang, B., et al. (2010) · Diabetes · doi:10.2337/db09-1541 · Cited by 285
Moderate elevation of body iron level and increased risk of cancer occurrence and death
Stevens, R. G., Graubard, B. I., Micozzi, M. S., Neriishi, K., & Blumberg, B. S. (1994) · International Journal of Cancer · doi:10.1002/ijc.2910560312 · Cited by 276
Review of Oxidative Stress in Brain and Spinal Cord Injury: Suggestions for Pharmacological and Nutritional Management Strategies
Juurlink, B. H. J., & Paterson, P. G. (1998) · Journal of Spinal Cord Medicine · doi:10.1080/10790268.1998.11719540 · Cited by 274
Cancer cell iron metabolism and the development of potent iron chelators as anti-tumour agents
Richardson, D. R., Kalinowski, D. S., Lau, S. L., Jansson, P. J., & Lovejoy, D. B. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.04.003 · Cited by 260
Identification of a New Acute Phase Protein
Liu, Q., & Nilsen‐Hamilton, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.38.22565 · Cited by 251
Siderocalin (Lcn 2) Also Binds Carboxymycobactins, Potentially Defending against Mycobacterial Infections through Iron Sequestration
Holmes, M. A., Paulsene, W., Jide, X., Ratledge, C., & Strong, R. K. (2005) · Structure · doi:10.1016/j.str.2004.10.009 · Cited by 246
A 25 kDa α2‐microglobulin‐related protein is a component of the 125 kDa form of human gelatinase
Triebel, S., Bläser, J., Reinke, H., & Tschesche, H. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81511-j · Cited by 229
Prevalence of Body Iron Excess in the Metabolic Syndrome
Bozzini, C., Girelli, D., Olivieri, O., Martinelli, N., Bassi, A., De Matteis, G., Tenuti, I., Lotto, V., Friso, S., Pizzolo, F., et al. (2005) · Diabetes Care · doi:10.2337/diacare.28.8.2061 · Cited by 224
STAT3-dependent reactive astrogliosis in the spinal dorsal horn underlies chronic itch
Shiratori‐Hayashi, M., Koga, K., Tozaki‐Saitoh, H., Kohro, Y., Toyonaga, H., Chiharu, Y., Hasegawa, A., Nakahara, T., Hachisuka, J., Akira, S., et al. (2015) · Nature Medicine · doi:10.1038/nm.3912 · Cited by 218
Lipocalin-2 Deficiency Impairs Thermogenesis and Potentiates Diet-Induced Insulin Resistance in Mice
Guo, H., Jin, D., Zhang, Y., Wright, W. S., Bazuine, M., Brockman, D. A., Bernlohr, D., & Chen, X. (2010) · Diabetes · doi:10.2337/db09-1735 · Cited by 214
Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses
Lögdberg, L., & Wester, L. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00164-3 · Cited by 202
Increased adipose tissue expression of lipocalin-2 in obesity is related to inflammation and matrix metalloproteinase-2 and metalloproteinase-9 activities in humans
Catalán, V., Gómez‐Ambrosi, J., Rodrı́guez, A., Ramírez, B., Silva, C., Rotellar, F., Gil, M. J. C., Cienfuegos, J. A., Salvador, J., & Frühbeck, G. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0486-8 · Cited by 190
Neutrophil gelatinase-associated lipocalin as a survival factor
Tong, Z., Wu, X., Ovcharenko, D., Zhu, J., Chen, C., & Kehrer, J. P. (2005) · Biochemical Journal · doi:10.1042/bj20051020 · Cited by 187
Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin
Bachman, M. A., Miller, V. L., & Weiser, J. N. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000622 · Cited by 186
The Lactobacillus Anomaly: Total Iron Abstinence
Weinberg, E. D. (1997) · Perspectives in Biology and Medicine · doi:10.1353/pbm.1997.0072 · Cited by 176
A novel inflammatory pathway mediating rapid hepcidin-independent hypoferremia
Guida, C., Altamura, S., Klein, F. A., Galy, B., Boutros, M., Ulmer, A. J., Hentze, M. W., & Muckenthaler, M. U. (2015) · Blood · doi:10.1182/blood-2014-08-595256 · Cited by 173
Iron metabolism in the pathogenesis of iron-induced kidney injury
Martines, A.-C. M. F., Masereeuw, R., Tjalsma, H., Hoenderop, J. G. J., Wetzels, J. F. M., & Swinkels, D. W. (2013) · Nature Reviews Nephrology · doi:10.1038/nrneph.2013.98 · Cited by 169
Interaction of lipocalin 2, transferrin, and siderophores determines the replicative niche of Klebsiella pneumoniae during pneumonia
Bachman, M. A., Lenio, S., Schmidt, L., Oyler, J. E., & Weiser, J. N. (2012) · mBio · doi:10.1128/mbio.00224-11 · Cited by 168
Purification and characterization of a human neutrophil lipocalin (HNL) from the secondary granules of human neutrophils
Xu, S., Carlson, M., Engström, Å., Garcia, R. C., Peterson, C. G. B., & Venge, P. (1994) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365519409088436 · Cited by 167
Neuronal Production of Lipocalin-2 as a Help-Me Signal for Glial Activation
Xing, C., Wang, X., Cheng, C., Montaner, J., Mandeville, E. T., Leung, W., van Leyen, K., Lok, J. M., Wang, X., & Lo, E. H. (2014) · Stroke · doi:10.1161/strokeaha.114.005733 · Cited by 162
Lipocalin-2 protects the brain during inflammatory conditions
Kang, S. S., Ren, Y., Liu, C.-C., Kurti, A., Baker, K. E., Bu, G., Asmann, Y., & Fryer, J. D. (2018) · Molecular Psychiatry · doi:10.1038/mp.2016.243 · Cited by 162
Mitochondrial iron homeostasis and its dysfunctions in neurodegenerative disorders
Mena, N. P., Urrutia, P. J., Lourido, F., Carrasco, C. M., & Núñez, M. T. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.02.001 · Cited by 154
SV40-induced expression of mouse gene 24p3 involves a post-transcriptional mechanism.
Hraba-Renevey, S., Türler, H., Kress, M., Salomon, C., & Weil, R. (1989) · PubMed · Cited by 151
Lipocalin 2 deactivates macrophages and worsens pneumococcal pneumonia outcomes
Warszawska, J. M., Gawish, R., Sharif, O., Sigel, S., Doninger, B., Lakovits, K., Mesteri, I., Nairz, M., Boon, L., Spiel, A., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67911 · Cited by 148
Absence of functional Hfe protects mice from invasive Salmonella enterica Serovar Typhimurium infection via induction of lipocalin-2
Nairz, M., Theurl, I., Schroll, A., Theurl, M., Fritsche, G., Lindner, E., Seifert, M., Crouch, M.-L. V., Hantke, K., Akira, S., et al. (2009) · Blood · doi:10.1182/blood-2009-05-223354 · Cited by 146
Cancer risk following primary hemochromatosis: A population‐based cohort study in Denmark
Hsing, A. W., McLaughlin, J. K., Olsen, J. H., Mellemkjar, L., Wacholder, S., & Fraumeni, J. F. (1995) · International Journal of Cancer · doi:10.1002/ijc.2910600204 · Cited by 145
Increased Lipocalin-2 Contributes to the Pathogenesis of Psoriasis by Modulating Neutrophil Chemotaxis and Cytokine Secretion
Shao, S., Cao, T., Jin, L., Li, B., Fang, H., Zhang, J., Zhang, Y., Jin-hong, H., & Wang, G. (2016) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2016.03.002 · Cited by 145
Lipocalin 2 Deficiency Dysregulates Iron Homeostasis and Exacerbates Endotoxin-Induced Sepsis
Srinivasan, G., Aitken, J. D., Zhang, B., Carvalho, F. A., Chassaing, B., Shashidharamurthy, R., Borregaard, N., Jones, D. P., Gewirtz, A. T., & Vijay–Kumar, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200892 · Cited by 143
Activation of toll-like receptor 3 protects against DSS-induced acute colitis
Vijay–Kumar, M., Wu, H., Aitken, J., Kolachala, V. L., Neish, A. S., Sitaraman, S. V., & Gewirtz, A. T. (2007) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20142 · Cited by 139
Lipocalin-2 Protein Deficiency Ameliorates Experimental Autoimmune Encephalomyelitis
Nam, Y., Kim, J.-H., Seo, M., Kim, J., Jin, M., Jeon, S., Seo, J.-W., Lee, W., Bing, S. J., Jee, Y., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.542282 · Cited by 137
Lipocalin 2 is a novel immune mediator of experimental autoimmune encephalomyelitis pathogenesis and is modulated in multiple sclerosis
Berard, J. L., Zarruk, J. G., Arbour, N., Prat, A., Yong, V. W., Jacques, F. H., Akira, S., & David, S. (2012) · Glia · doi:10.1002/glia.22342 · Cited by 136
Lipocalin-2 ameliorates granulocyte functionality
Schroll, A., Eller, K., Feistritzer, C., Nairz, M., Sonnweber, T., Moser, P. A., Rosenkranz, A. R., Theurl, I., & Weiss, G. (2012) · European Journal of Immunology · doi:10.1002/eji.201142351 · Cited by 135
Lipocalin 2-Dependent Inhibition of Mycobacterial Growth in Alveolar Epithelium
Saiga, H., Nishimura, J., Kuwata, H., Okuyama, M., Matsumoto, S., Sato, S., Matsumoto, M., Akira, S., Yoshikai, Y., Honda, K., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.12.8521 · Cited by 133
Causes and Significance of Markedly Elevated Serum Ferritin Levels in an Academic Medical Center
Moore, C., Ormseth, M. J., & Fuchs, H. A. (2013) · JCR Journal of Clinical Rheumatology · doi:10.1097/rhu.0b013e31829ce01f · Cited by 132
Studies of the release and turnover of a human neutrophil lipocalin
Axelsson, L., Bergenfeldt, M., & OHLSSON, K. (1995) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365519509110257 · Cited by 132
Parkinson's Disease Iron Deposition Caused by Nitric Oxide-Induced Loss of β-Amyloid Precursor Protein
Ayton, S., Lei, P., Hare, D. J., Duce, J. A., George, J. L., Adlard, P. A., McLean, C., Rogers, J. T., Cherny, R. A., Finkelstein, D. I., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3439-14.2015 · Cited by 131
Influenza A Virus Exacerbates Staphylococcus aureus Pneumonia in Mice by Attenuating Antimicrobial Peptide Production
Robinson, K. M., McHugh, K. J., Mandalapu, S., Clay, M. E., Lee, B., Scheller, E. V., Enelow, R. I., Chan, Y. R., Kolls, J. K., & Alcorn, J. F. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit527 · Cited by 131
Evolution of the acute phase response: iron release by echinoderm (Asterias forbesi) coelomocytes, and cloning of an echinoderm ferritin molecule
Beck, G., Ellis, T. W., Habicht, G. S., Schluter, S. F., & Marchalonis, J. J. (2002) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(01)00051-9 · Cited by 129
Endoplasmic reticulum stress drives proteinuria-induced kidney lesions via Lipocalin 2
Karoui, K. E., Viau, A., Dellis, O., Bagattin, A., Nguyen, C., Baron, W., Burtin, M., Broueilh, M., Heidet, L., Mollet, G., et al. (2016) · Nature Communications · doi:10.1038/ncomms10330 · Cited by 126
Lipocalin 2 Plays an Immunomodulatory Role and Has Detrimental Effects after Spinal Cord Injury
Rathore, K. I., Berard, J. L., Redensek, A., Chierzi, S., López‐Vales, R., Santos, M. M., Akira, S., & David, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0116-11.2011 · Cited by 125
Lipocalin 2 in cancer: When good immunity goes bad
Rodvold, J. J., Mahadevan, N. R., & Zanetti, M. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.11.002 · Cited by 124
Myoglobin toxicity in proximal human kidney cells: Roles of Fe, Ca2+, H2O2, and terminal mitochondrial electron transport
Zager, R. A., & Burkhart, K. M. (1997) · Kidney International · doi:10.1038/ki.1997.104 · Cited by 123
Flagellin Suppresses Epithelial Apoptosis and Limits Disease during Enteric Infection
Vijay–Kumar, M., Wu, H., Jones, R. M., Grant, G., Babbin, B. A., King, T. P., Kelly, D., Gewirtz, A. T., & Neish, A. S. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060345 · Cited by 122
Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut
Singh, V., Yeoh, B. S., Xiao, X., Kumar, M., Bachman, M. A., Borregaard, N., Joe, B., & Vijay–Kumar, M. (2015) · Nature Communications · doi:10.1038/ncomms8113 · Cited by 119
NGAL (Lcn2) monomer is associated with tubulointerstitial damage in chronic kidney disease
Nickolas, T. L., Forster, C. S., Sise, M. E., Barasch, N., Valle, D. S.-D., Viltard, M., Buchen, C., Kupferman, S., Carnevali, M. L., BENNETT, M. R., et al. (2012) · Kidney International · doi:10.1038/ki.2012.195 · Cited by 118
Pathogenic Upregulation of Glial Lipocalin-2 in the Parkinsonian Dopaminergic System
Kim, B.-W., Jeong, K. H., Kim, J., Jin, M., Kim, J., Lee, M., Choi, D., Won, S.-Y., McLean, C., Jeon, M., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4261-15.2016 · Cited by 118
Microbiota-Inducible Innate Immune Siderophore Binding Protein Lipocalin 2 Is Critical for Intestinal Homeostasis
Singh, V., Yeoh, B. S., Chassaing, B., Zhang, B., Saha, P., Xiao, X., Awasthi, D., Shashidharamurthy, R., Dikshit, M., Gewirtz, A., et al. (2016) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2016.03.007 · Cited by 117
Self-citation
Mammalian Siderophores, Siderophore-binding Lipocalins, and the Labile Iron Pool
Correnti, C., & Strong, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.311829 · Cited by 115
Lipocalin 2 in the central nervous system host response to systemic lipopolysaccharide administration
Ip, J. P. K., Noçon, A. L., Hofer, M. J., Lim, S. L., Müller, M., & Campbell, I. L. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-124 · Cited by 115
Mouse oncogene protein 24p3 is a member of the Lipocalin protein family
Flower, D. R., North, A. C. T., & Attwood, T. K. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81256-2 · Cited by 114
NGAL decreases E-cadherin-mediated cell–cell adhesion and increases cell motility and invasion through Rac1 in colon carcinoma cells
Hu, L., Hittelman, W. N., Lu, T., Ji, P., Arlinghaus, R. B., Ilya Shmulevich, C., Hamilton, S. R., & Zhang, W. (2009) · Laboratory Investigation · doi:10.1038/labinvest.2009.17 · Cited by 114
Effects of Mouse and Human Lipocalin Homologues 24p3/lcn2 and Neutrophil Gelatinase–Associated Lipocalin on Gastrointestinal Mucosal Integrity and Repair
Playford, R. J., Belo, A., Poulsom, R., Fitzgerald, A. J., Harris, K. M., Pawluczyk, I., Ryon, J., Darby, T., Nilsen‐Hamilton, M., Ghosh, S. K., et al. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.05.051 · Cited by 105
Reduction of circulating redox-active iron by apotransferrin protects against renal ischemia-reperfusion injury1
de Vries, B., Walter, S. J., von Bonsdorff, L., Wolfs, T. G. A. M., van Heurn, E. L. W., Parkkinen, J., & Buurman, W. A. (2004) · Transplantation · doi:10.1097/01.tp.0000115002.28575.e7 · Cited by 105
Anticalins
Gebauer, M., & Skerra, A. (2012) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-396962-0.00007-0 · Cited by 104
Fecal neutrophil gelatinase‐associated lipocalin as a biomarker for inflammatory bowel disease
Thorsvik, S., Damås, J. K., Granlund, A. V. B., Flo, T. H., Bergh, K., Østvik, A. E., & Sandvik, A. K. (2016) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.13598 · Cited by 102
Infusion of IL-10–expressing cells protects against renal ischemia through induction of lipocalin-2
Jung, M., Solà, A., Hughes, J., Kluth, D., Vinuesa, E., Viñas, J. L., Pérez-Ladaga, A., & Hotter, G. (2012) · Kidney International · doi:10.1038/ki.2011.446 · Cited by 100
Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore
Zawadzka, A. M., Kim, Y., Maltseva, N., Nichiporuk, R. V., Fan, Y., Joachimiak, A., & Raymond, K. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904793106 · Cited by 99
Immunoassays distinguishing between HNL/NGAL released in urine from kidney epithelial cells and neutrophils
Mårtensson, J., Xu, S., Bell, M., Martling, C., & Venge, P. (2012) · Clinica Chimica Acta · doi:10.1016/j.cca.2012.05.010 · Cited by 97
Disruption of the Lcn2 gene in mice suppresses primary mammary tumor formation but does not decrease lung metastasis
Berger, T., Cheung, C. C., Elia, A. J., & Mak, T. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000101107 · Cited by 96
Lipocalin 2 is a Choroid Plexus Acute-Phase Protein
Marques, F., Rodrigues, A. J., Sousa, J. C., Coppola, G., Geschwind, D. H., Sousa, N., Correia‐Neves, M., & Palha, J. A. (2007) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600557 · Cited by 95
Regulation by lipocalin‐2 of neuronal cell death, migration, and morphology
Lee, S., Lee, W., Lee, M., Mori, K., & Suk, K. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22779 · Cited by 92
Management of Iron-Deficiency Anemia in Inflammatory Bowel Disease
Nielsen, O. H., Ainsworth, M. A., Coskun, M., & Weiß, G. (2015) · Medicine · doi:10.1097/md.0000000000000963 · Cited by 92
Role of Hepcidin in the Setting of Hypoferremia during Acute Inflammation
Deschemin, J.-C., & Vaulont, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061050 · Cited by 89
Lipocalin 2 is present in the EAE brain and is modulated by natalizumab
Marques, F., Mesquita, S. D., Sousa, J. C., Coppola, G., Gao, F., Geschwind, D. H., Cabezas, S. C., Aloisi, F., Degn, M., Cerqueira, J., et al. (2012) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2012.00033 · Cited by 85
Lipocalin 2 is protective against E. coli pneumonia
Wu, H., Santoni-Rugiu, E., Ralfkiaer, E., Porse, B. T., Moser, C., Høiby, N., Borregaard, N., & Cowland, J. B. (2010) · Respiratory Research · doi:10.1186/1465-9921-11-96 · Cited by 82
Variation in Siderophore Biosynthetic Gene Distribution and Production across Environmental and Faecal Populations of Escherichia coli
Searle, L. J., Méric, G., Porcelli, I., Sheppard, S. K., & Lucchini, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117906 · Cited by 80
Effect of iron on renal tubular epithelial cells
Sponsel, H. T., Alfrey, A. C., Hammond, W. S., Dürr, J. A., Ray, C. J., & Anderson, R. J. (1996) · Kidney International · doi:10.1038/ki.1996.334 · Cited by 79
Role of iron in brain lipocalin 2 upregulation after intracerebral hemorrhage in rats
Dong, M., Xi, G., Keep, R. F., & Hua, Y. (2013) · Brain Research · doi:10.1016/j.brainres.2013.02.008 · Cited by 77
Lipocalin 2 Imparts Selective Pressure on Bacterial Growth in the Bladder and Is Elevated in Women with Urinary Tract Infection
Steigedal, M., Marstad, A., Haug, M., Damås, J. K., Strong, R. K., Roberts, P. L., Himpsl, S. D., Stapleton, A. E., Hooton, T. M., Mobley, H. L. T., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401528 · Cited by 75
Lipocalin 2 prevents intestinal inflammation by enhancing phagocytic bacterial clearance in macrophages
Toyonaga, T., Matsuura, M., Mori, K., Honzawa, Y., Minami, N., Yamada, S., Kobayashi, T., Hibi, T., & Nakase, H. (2016) · Scientific Reports · doi:10.1038/srep35014 · Cited by 75
Tcf3 promotes cell migration and wound repair through regulation of lipocalin 2
Miao, Q., Ku, A., Nishino, Y., Howard, J. M., Rao, A., Shaver, T., Garcia, G. E., Le, D., Karlin, K. L., Westbrook, T. F., et al. (2014) · Nature Communications · doi:10.1038/ncomms5088 · Cited by 74
Role of Lipocalin-2 in Brain Injury after Intracerebral Hemorrhage
Ni, W., Zheng, M., Xi, G., Keep, R. F., & Hua, Y. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.52 · Cited by 74
Neutrophil Gelatinase-Associated Lipocalin Expresses Antimicrobial Activity by Interfering with l-Norepinephrine-Mediated Bacterial Iron Acquisition
Miethke, M., & Skerra, A. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01158-09 · Cited by 74
Knockdown of lipocalin‐2 suppresses the growth and invasion of prostate cancer cells
Tung, M., Hsieh, S., Yang, S., Cheng, C., Tsai, R., Wang, S., Huang, M., & Hsieh, Y. (2013) · The Prostate · doi:10.1002/pros.22670 · Cited by 74
Combinatorial Design of an Anticalin Directed against the Extra-Domain B for the Specific Targeting of Oncofetal Fibronectin
Gebauer, M., Schiefner, A., Matschiner, G., & Skerra, A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.12.004 · Cited by 71
Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant — a so-called ‘anticalin’ — using a molecular random approach
Schlehuber, S., & Skerra, A. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00026-1 · Cited by 70
Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
Liu, Z., Reba, S., Chen, W.-D., Porwal, S. K., Boom, W. H., Petersen, R. B., Rojas, R., Viswanathan, R., & Devireddy, L. (2014) · Journal of Experimental Medicine · doi:10.1084/jem.20132629 · Cited by 70
Lipocalin 2 Regulates Inflammation during Pulmonary Mycobacterial Infections
Guglani, L., Gopal, R., Rangel-Moreno, J., Junecko, B. F., Lin, Y., Berger, T., Mak, T. W., Alcorn, J. F., Randall, T. D., Reinhart, T. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050052 · Cited by 68
Lipocalin‐2 ensures host defense against Salmonella Typhimurium by controlling macrophage iron homeostasis and immune response
Nairz, M., Schroll, A., Haschka, D., Dichtl, S., Sonnweber, T., Theurl, I., Theurl, M., Lindner, E., Demetz, E., Aßhoff, M., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545569 · Cited by 67
Circulating levels of lipocalin-2 and retinol-binding protein-4 are increased in psoriatic patients and correlated with baseline PASI
Romaní, J., Caixàs, A., Ceperuelo‐Mallafré, V., Carrascosa, J. M., Ribera, M., Rigla, M., Vendrell, J. J., & Luelmo, J. (2012) · Archives of Dermatological Research · doi:10.1007/s00403-012-1306-5 · Cited by 66
Siderocalin-mediated recognition, sensitization, and cellular uptake of actinides
Allred, B. E., Rupert, P. B., Gauny, S. S., An, D. D., Ralston, C. Y., Sturzbecher‐Hoehne, M., Strong, R. K., & Abergel, R. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1508902112 · Cited by 66
Lipocalin 2 Bolsters Innate and Adaptive Immune Responses to Blood-Stage Malaria Infection by Reinforcing Host Iron Metabolism
Zhao, H., Konishi, A., Fujita, Y., Yagi, M., Ohata, K., Aoshi, T., Itagaki, S., Sato, S., Narita, H., Abdelgelil, N. H., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.10.010 · Cited by 65
Low dietary iron intake restrains the intestinal inflammatory response and pathology of enteric infection by food‐borne bacterial pathogens
Kortman, G. A. M., Mulder, M. L. M., Richters, T. J. W., Shanmugam, N. K. N., Trebicka, E., Boekhorst, J., Timmerman, H. M., Roelofs, R., Wiegerinck, E. T., Laarakkers, C. M., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545642 · Cited by 65
Impaired Neutrophil Function in 24p3 Null Mice Contributes to Enhanced Susceptibility to Bacterial Infections
Liu, Z., Petersen, R., & Devireddy, L. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202411 · Cited by 64
Ageing neuroinflammation and neurodegeneration
Ward, R. J. (2015) · Frontiers in Bioscience-Scholar · doi:10.2741/s433 · Cited by 64
A minor role for lipocalin 2 in high-fat diet-induced glucose intolerance
Jun, L. S., Siddall, P., & Rosen, E. D. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00147.2011 · Cited by 62
Neutrophils and keratinocytes in innate immunity—cooperative actions to provide antimicrobial defense at the right time and place
Borregaard, N., Theilgaard‐Mönch, K., Cowland, J. B., Ståhle, M., & Sørensen, O. E. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0704381 · Cited by 61
Lipocalin‐2 exacerbates psoriasiform skin inflammation by augmenting T‐helper 17 response
Hau, C. S., Kanda, N., Tada, Y., Shibata, S., Uozaki, H., Fukusato, T., Sato, S., & Watanabe, S. (2015) · The Journal of Dermatology · doi:10.1111/1346-8138.13227 · Cited by 60
Lipocalin‐2 enhances angiogenesis in rat brain endothelial cells via reactive oxygen species and iron‐dependent mechanisms
Wu, L., Du, Y., Lok, J. M., Lo, E. H., & Xing, C. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.13023 · Cited by 59
Serum lipocalin-2 levels are increased in patients with psoriasis
Kamata, M., Tada, Y., Tatsuta, A., Kawashima, T., Shibata, S., Mitsui, H., Asano, Y., Sugaya, M., Kadono, T., Kanda, N., et al. (2012) · Clinical and Experimental Dermatology · doi:10.1111/j.1365-2230.2011.04265.x · Cited by 58
Expression and localization of the iron–siderophore binding protein lipocalin 2 in the normal rat brain and after kainate-induced excitotoxicity
Chia, W.-J., Dawe, G. S., & Ong, W. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.04.007 · Cited by 58
Hemeoxygenase-1 and Renal Ischaemia-Reperfusion Injury
Ferenbach, D. A., Kluth, D., & Hughes, J. (2010) · Nephron Experimental Nephrology · doi:10.1159/000313828 · Cited by 57
Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17
Martinez, A.-I. C., Weinhäupl, K., Lee, W., Wolff, N. A., Storch, B., Żerko, S., Konrat, R., Koźmiński, W., Breuker, K., Thévenod, F., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.685644 · Cited by 56
Inhibition of the proliferation and invasion of hepatocellular carcinoma cells by lipocalin 2 through blockade of JNK and PI3K/Akt signaling
Kim (2010) · International Journal of Oncology · doi:10.3892/ijo.2010.854 · Cited by 54
A novel alternative spliced variant of neutrophil gelatinase-associated lipocalin receptor in oesophageal carcinoma cells
Fang, W., Xu, L., Lu, X., Liao, L., Cai, W., Shen, Z., & Li, E. (2007) · Biochemical Journal · doi:10.1042/bj20060836 · Cited by 54
Interactions between neutrophil gelatinase-associated lipocalin and natural lipophilic ligands
Bratt, T., Ohlson, S., & Borregaard, N. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00131-2 · Cited by 52
Siderocalin/Lcn2/NGAL/24p3 Does Not Drive Apoptosis Through Gentisic Acid Mediated Iron Withdrawal in Hematopoietic Cell Lines
Correnti, C., Richardson, V., Sia, A. K., Bandaranayake, A. D., Ruiz, M., Rahmanto, Y. S., Kovačević, Ž., Clifton, M. C., Holmes, M. A., Kaiser, B. K., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043696 · Cited by 52
Lipocalin-2 inhibits autophagy and induces insulin resistance in H9c2 cells
Chan, Y. K., Sung, H. K., Jahng, J. W. S., Kim, G. H. E., Han, M., & Sweeney, G. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.04.006 · Cited by 51
Neutrophil gelatinase–associated lipocalin is instrumental in the pathogenesis of antibody‐mediated nephritis in mice
Pawar, R. D., Pitashny, M., Gindea, S., Tieng, A. T., Levine, B., Goilav, B., Campbell, S. R., Xia, Y., Qing, X., Thomas, D. B., et al. (2011) · Arthritis & Rheumatism · doi:10.1002/art.33485 · Cited by 50
Neutrophil gelatinase-associated lipocalin (NGAL/Lcn2) is upregulated in gastric mucosa infected with Helicobacter pylori
Alpízar‐Alpízar, W., Lærum, O. D., Illemann, M., Ramírez, J. A., Arias, A., Malespín-Bendaña, W., Ramírez, V., Lund, L. R., Borregaard, N., & Nielsen, B. S. (2009) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-009-0825-8 · Cited by 50
Epigallocatechin-3-Gallate Inhibition of Myeloperoxidase and Its Counter-Regulation by Dietary Iron and Lipocalin 2 in Murine Model of Gut Inflammation
Yeoh, B. S., Olvera, R. A., Singh, V., Xiao, X., Kennett, M. J., Joe, B., Lambert, J. D., & Vijay–Kumar, M. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.12.004 · Cited by 49
Lipophilic siderophores of Mycobacterium tuberculosis prevent cardiac reperfusion injury
Horwitz, L. D., Sherman, N. A., Kong, Y., Pike, A. W., Gobin, J., Fennessey, P. V., & Horwitz, M. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5263 · Cited by 48
Increased expression of the lipocalin 24p3 as an apoptotic mechanism for MK886
Tong, Z., Wu, X., & Kehrer, J. P. (2003) · Biochemical Journal · doi:10.1042/bj20021696 · Cited by 48
The Molecular Mechanisms that Promote Edema After Intracerebral Hemorrhage
Bodmer, D., Vaughan, K. A., Zacharia, B. E., Hickman, Z. L., & Connolly, E. S. (2012) · Translational Stroke Research · doi:10.1007/s12975-012-0162-0 · Cited by 46
Hepcidin resistance in dysmetabolic iron overload
Rametta, R., Dongiovanni, P., Pelusi, S., Francione, P., Iuculano, F., Borroni, V. N., Fatta, E., Castagna, A., Girelli, D., Fargion, S. R., et al. (2016) · Liver International · doi:10.1111/liv.13124 · Cited by 46
Lipocalin 2 produces insulin resistance and can be upregulated by glucocorticoids in human adipose tissue
Kamble, P. G., Pereira, M. J., Sidibeh, C. O., Amini, S., Sundbom, M., Lau, J., & Eriksson, J. W. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.03.011 · Cited by 45
Engineered Recognition of Tetravalent Zirconium and Thorium by Chelator–Protein Systems: Toward Flexible Radiotherapy and Imaging Platforms
Captain, I., Deblonde, G. J. ‐., Rupert, P. B., An, D. D., Illy, M., Rostan, E., Ralston, C. Y., Strong, R. K., & Abergel, R. J. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b02041 · Cited by 45
Disposal of iron by a mutant form of lipocalin 2
Barasch, J. M., Hollmén, M., Deng, R., Hod, E. A., Rupert, P. B., Abergel, R. J., Allred, B. E., Xu, K. H., Darrah, S. F., Tekabe, Y., et al. (2016) · Nature Communications · doi:10.1038/ncomms12973 · Cited by 44
Neutrophil gelatinase-associated lipocalin and interleukin-10 regulate intramacrophage Chlamydia pneumoniae replication by modulating intracellular iron homeostasis
Bellmann-Weiler, R., Schroll, A., Engl, S., Nairz, M., Talasz, H., Seifert, M., & Weiss, G. (2013) · Immunobiology · doi:10.1016/j.imbio.2012.11.004 · Cited by 43
EGCG inhibit chemical reactivity of iron through forming an Ngal–EGCG–iron complex
Bao, G., Xu, J., Hu, F., Wan, X., Deng, S., & Barasch, J. M. (2013) · BioMetals · doi:10.1007/s10534-013-9681-8 · Cited by 43
Early expression of serum neutrophil gelatinase-associated lipocalin (NGAL) is associated with neurological severity immediately after traumatic brain injury
Zhao, J., Chen, H., Zhang, M., Zhang, Y., Qian, C., Liu, Y., He, S., Zou, Y., & Liu, H. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.07.060 · Cited by 42
Siderocalin inhibits the intracellular replication ofMycobacterium tuberculosisin macrophages
Johnson, E. E., Srikanth, C. V., Sandgren, A., Harrington, L., Trebicka, E., Wang, L., Borregaard, N., Murray, M. B., & Cherayil, B. J. (2009) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2009.00622.x · Cited by 41
Estimation of tissue and serum lipocalin-2 in psoriasis vulgaris and its relation to metabolic syndrome
Hadidi, H. H. E., Samir, N., Shaker, O. G., & Otb, S. (2013) · Archives of Dermatological Research · doi:10.1007/s00403-013-1414-x · Cited by 39
Galline Ex-FABP Is an Antibacterial Siderocalin and a Lysophosphatidic Acid Sensor Functioning through Dual Ligand Specificities
Correnti, C., Clifton, M. C., Abergel, R. J., Allred, B. E., Hoette, T. M., Ruiz, M., Cancedda, R., Raymond, K. N., Descalzi, F., & Strong, R. K. (2011) · Structure · doi:10.1016/j.str.2011.09.019 · Cited by 38
Human Metabolome-derived Cofactors Are Required for the Antibacterial Activity of Siderocalin in Urine
Shields‐Cutler, R. R., Crowley, J. R., Miller, C. D., Stapleton, A. E., Cui, W., & Henderson, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.759183 · Cited by 38
Inhibition of Oxidative Stress in Renal Ischemia-Reperfusion Injury
Choi, E. K., Jung, H., Kwak, K. H., Yi, S., Lim, J. A., Park, S. H., Park, J., Kim, S., Jee, D., & Lim, D. G. (2016) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000001565 · Cited by 37
Lipocalin 2 Enhances Migration and Resistance against Cisplatin in Endometrial Carcinoma Cells
Miyamoto, T., Kashima, H., Yamada, Y., Kobara, H., Asaka, R., Ando, H., Higuchi, S., Ida, K., Mvunta, D. H., & Shiozawa, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155220 · Cited by 36
Six-transmembrane epithelial antigen of prostate 4 and neutrophil gelatinase-associated lipocalin expression in visceral adipose tissue is related to iron status and inflammation in human obesity
Catalán, V., Gómez‐Ambrosi, J., Rodrı́guez, A., Ramírez, B., Rotellar, F., Valentí, V., Silva, C., Gil, M. J., Salvador, J., & Frühbeck, G. (2012) · European Journal of Nutrition · doi:10.1007/s00394-012-0464-8 · Cited by 34
Interleukin-8 Secretion in Response to Aferric Enterobactin Is Potentiated by Siderocalin
Nelson, A. L., Ratner, A. J., Barasch, J. M., & Weiser, J. N. (2007) · Infection and Immunity · doi:10.1128/iai.01719-06 · Cited by 34
Neutrophil gelatinase-associated lipocalin immunoexpression in renal tumors: Correlation with histotype and histological grade
Barresi (2010) · Oncology Reports · doi:10.3892/or_00000860 · Cited by 31
Lipocalin-2 Induces Apoptosis in Human Hepatocellular Carcinoma Cells Through Activation of Mitochondria Pathways
Chien, M., Ying, T.-H., Yang, S., Yu, J.-K., Hsu, C.-W., Hsieh, S.-C., & Hsieh, Y. (2012) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9370-1 · Cited by 30
Inactivation of 3- hydroxybutyrate dehydrogenase 2 delays zebrafish erythroid maturation by conferring premature mitophagy
Davuluri, G., Song, P., Liu, Z., Wald, D. N., Sakaguchi, T. F., Green, M. R., & Devireddy, L. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600077113 · Cited by 30
Fecal Lipocalin-2 as a Sensitive and Noninvasive Biomarker in the TNBS Crohn’s Inflammatory Bowel Disease Model
Hsieh, H., Morin, J., Filliettaz, C., Rao, V. P., Labarre, S., & Radi, Z. A. (2016) · Toxicologic Pathology · doi:10.1177/0192623316665927 · Cited by 30
Lipocalin 2 alleviates iron toxicity by facilitating hypoferremia of inflammation and limiting catalytic iron generation
Xiao, X., Yeoh, B. S., Saha, P., Olvera, R. A., Singh, V., & Vijay–Kumar, M. (2016) · BioMetals · doi:10.1007/s10534-016-9925-5 · Cited by 29
No Effect of NGAL/lipocalin-2 on Aggressiveness of Cancer in the MMTV-PyMT/FVB/N Mouse Model for Breast Cancer
Cramer, E. P., Glenthøj, A. B., Häger, M., Juncker‐Jensen, A., Engelholm, L. H., Santoni‐Rugiu, E., Lund, L. R., Lærum, O. D., Cowland, J. B., & Borregaard, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039646 · Cited by 28
Exogenous Lipocalin 2 Ameliorates Acute Rejection in a Mouse Model of Renal Transplantation
Ashraf, M., Schwelberger, H. G., Brendel, K., Feurle, J., Andrassy, J., Kotsch, K., Regele, H. M., Pratschke, J., Maier, H. T., & Aigner, F. (2015) · American Journal of Transplantation · doi:10.1111/ajt.13521 · Cited by 28
Role of Lipocalin-2 in Thrombin-Induced Brain Injury
Mao, S., Xi, G., Keep, R. F., & Hua, Y. (2016) · Stroke · doi:10.1161/strokeaha.115.012153 · Cited by 28
Siderophore Biosynthesis Governs the Virulence of Uropathogenic Escherichia coli by Coordinately Modulating the Differential Metabolism
Su, Q., Guan, T., He, Y., & Lv, H. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00061 · Cited by 28
Synthetic, potentiometric and spectroscopic studies of chelation between Fe(III) and 2,5-DHBA supports salicylate-mode of siderophore binding interactions
Porwal, S. K., Furia, E., Harris, M. E., Viswanathan, R., & Devireddy, L. R. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.12.010 · Cited by 26
Cerebrospinal fluid lipocalin 2 in patients with clinically isolated syndromes and early multiple sclerosis
Khalil, M., Renner, A., Langkammer, C., Enzinger, C., Ropele, S., Stojaković, T., Scharnagl, H., Bachmaier, G., Pichler, A., Archelos, J.-J., et al. (2016) · Multiple Sclerosis Journal · doi:10.1177/1352458515624560 · Cited by 25
Anticalins directed against vascular endothelial growth factor receptor 3 (VEGFR-3) with picomolar affinities show potential for medical therapy and in vivo imaging
Richter, A., & Skerra, A. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0195 · Cited by 25
Lipocalin 2 performs contrasting, location-dependent roles in APCmin tumor initiation and progression
Reilly, P. T., Teo, W. L., Low, M., Amoyo-Brion, A. A., Dominguez‐Brauer, C., Elia, A., Berger, T., Greicius, G., Pettersson, S., & Mak, T. W. (2012) · Oncogene · doi:10.1038/onc.2012.159 · Cited by 22
Intravenous application of an anticalin dramatically lowers plasma digoxin levels and reduces its toxic effects in rats
Eyer, F., Steimer, W., Nitzsche, T., Jung, N., Neuberger, H., Müller, C., Schlapschy, M., Zilker, T. R., & Skerra, A. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.07.009 · Cited by 21
Neutrophil gelatinase‐associated lipocalin regulates gut microbiota of mice
Mori, K., Suzuki, T., Minamishima, S., Igarashi, T., Inoue, K., Nishimura, D., Seki, H., Yamada, T., Kosugi, S., Katori, N., et al. (2015) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.13042 · Cited by 16
Transcription factor 7-like 1 dysregulates keratinocyte differentiation through upregulating lipocalin 2
Xu, M., Zhang, Y., Cheng, H., Liu, Y., Zou, X., Zhan, N., Xiao, S., & Xia, Y. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2016.28 · Cited by 16
The chelation of colonic luminal iron by a unique sodium alginate for the improvement of gastrointestinal health
Horniblow, R. D., Latunde-Dada, G. O., Harding, S. E., Schneider, M., Almutairi, F. M., Sahni, M., Bhatti, A., Ludwig, C., Norton, I. T., Iqbal, T. H., et al. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500882 · Cited by 16
Modulation of urinary siderophores by the diet, gut microbiota and inflammation in mice
Xiao, X., Yeoh, B. S., Saha, P., Tian, Y., Singh, V., Patterson, A. D., & Vijay-Kumar, M. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.11.014 · Cited by 16
Self-citation
Microarray analysis of gastric mucosa among children with Helicobacter pylori infection
Ikuse, T., Ohtsuka, Y., Kudo, T., Hosoi, K., Obayashi, N., Jimbo, K., Aoyagi, Y., Fujii, T., Nagata, S., & Shimizu, T. (2012) · Pediatrics International · doi:10.1111/j.1442-200x.2012.03573.x · Cited by 15
N-acetilcisteína e deferoxamina protegem contra insuficiência renal aguda induzida por isquemia/reperfusão em ratos
Bernardi, R. M., Constantino, L. D. S., Machado, R. A., Vuolo, F. S., Budni, P., Ritter, C., & Dal‐Pizzol, F. (2012) · Revista Brasileira de Terapia Intensiva · doi:10.1590/s0103-507x2012000300003 · Cited by 13

Flagged first, then by citations

Research works printed but not linked: 5

Chakraborty S, 2012, Biochim. Biophys. Acta, 1826, 129
Gregory A, 2014, GeneReviews
Hraba-Renevey S, 1989, Oncogene, 4, 601
Lee EK, 2011, Int. J. Oncol., 38, 325
Vijay-Kumar M, 2007, J. Clin. Investig., 117, 3909

Sorted by citations

System Xc−/GSH/GPX4 axis: An important antioxidant system for the ferroptosis in drug-resistant solid tumor therapy
Li, F., Long, H., Zhou, Z.-W., Luo, H., Xu, S., & Gao, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.910292 · Cited by 476
Beyond adiponectin and leptin: adipose tissue-derived mediators of inter-organ communication
Funcke, J., & Scherer, P. E. (2019) · Journal of Lipid Research · doi:10.1194/jlr.r094060 · Cited by 354
A targetable LIFR−NF-κB−LCN2 axis controls liver tumorigenesis and vulnerability to ferroptosis
Yao, F., Deng, Y., Zhao, Y., Mei, Y., Zhang, Y., Liu, X., Martinez, C., Su, X., Rosato, R. R., Teng, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27452-9 · Cited by 328
NUPR1 is a critical repressor of ferroptosis
Liu, J., Song, X., Kuang, F., Zhang, Q., Xie, Y., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Communications · doi:10.1038/s41467-021-20904-2 · Cited by 290
The Review of Current Knowledge on Neutrophil Gelatinase-Associated Lipocalin (NGAL)
Romejko, K., Markowska, M., & Niemczyk, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310470 · Cited by 264
Iron Metabolism in Obesity and Metabolic Syndrome
González-Domínguez, Á., Visiedo-García, F. M., Domínguez-Riscart, J., González-Domínguez, R., Mateos, R. M., & Lechuga-Sancho, A. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155529 · Cited by 227
The Impact of Dietary Transition Metals on Host-Bacterial Interactions
Lopez, C. A., & Skaar, E. P. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.05.008 · Cited by 190
Microbial Siderophore Enterobactin Promotes Mitochondrial Iron Uptake and Development of the Host via Interaction with ATP Synthase
Qi, B., & Han, M. (2018) · Cell · doi:10.1016/j.cell.2018.07.032 · Cited by 164
The Iron Tug-of-War between Bacterial Siderophores and Innate Immunity
Golonka, R. M., Yeoh, B. S., & Vijay–Kumar, M. (2019) · Journal of Innate Immunity · doi:10.1159/000494627 · Cited by 180
Bacteroidetes Species Are Correlated with Disease Activity in Ulcerative Colitis
Nomura, K., Ishikawa, D., Okahara, K., Ito, S., Haga, K., Takahashi, M., Arakawa, A., Shibuya, T., Osada, T., Kuwahara-Arai, K., et al. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10081749 · Cited by 150
Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics
Klebba, P. E., Newton, S. M. C., Six, D. A., Kumar, A., Yang, T., Nairn, B. L., Munger, C., & Chakravorty, S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01005 · Cited by 150
More than a simple biomarker: the role of NGAL in cardiovascular and renal diseases
Buonafine, M., Martínez‐Martínez, E., & Jaisser, F. (2018) · Clinical Science · doi:10.1042/cs20171592 · Cited by 154
Cerebrospinal fluid lipocalin 2 as a novel biomarker for the differential diagnosis of vascular dementia
Llorens, F., Hermann, P., Villar‐Piqué, A., Lucena, D. D., Nägga, K., Hansson, O., Santana, I. J., Schmitz, M., Schmidt, C., Varges, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14373-2 · Cited by 115
Lipocalin-2 silencing suppresses inflammation and oxidative stress of acute respiratory distress syndrome by ferroptosis via inhibition of MAPK/ERK pathway in neonatal mice
Wang, X., Zhang, C., Zou, N., Chen, Q., Wang, C., Zhou, X., Luo, L., Qi, H., Li, J., Liu, Z., et al. (2021) · Bioengineered · doi:10.1080/21655979.2021.2009970 · Cited by 108
Retracted
LCN2 secreted by tissue-infiltrating neutrophils induces the ferroptosis and wasting of adipose and muscle tissues in lung cancer cachexia
Wang, D., Li, X., Jiao, D., Cai, Y., Qian, L., Shen, Y., Lu, Y., Zhou, Y., Fu, B., Sun, R., et al. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01429-1 · Cited by 112
Siderophore conjugates to combat antibiotic-resistant bacteria
Rayner, B., Verderosa, A. D., Ferro, V., & Blaskovich, M. A. T. (2023) · RSC Medicinal Chemistry · doi:10.1039/d2md00465h · Cited by 110
Reduced secretion of LCN2 (lipocalin 2) from reactive astrocytes through autophagic and proteasomal regulation alleviates inflammatory stress and neuronal damage
Jung, B.-K., Park, Y., Yoon, B., Bae, J.-S., Han, S.-W., Heo, J. E., Kim, D., & Ryu, K. (2023) · Autophagy · doi:10.1080/15548627.2023.2180202 · Cited by 107
Zebrafish: an efficient vertebrate model for understanding role of gut microbiota
Xia, H., Chen, H., Cheng, X., Yin, M., Yao, X., Ma, J., Huang, M., Chen, G., & Liu, H. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00579-1 · Cited by 107
Molecular and Cellular Mechanisms of Itch in Psoriasis
Komiya, E., Tominaga, M., Kamata, Y., Suga, Y., & Takamori, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218406 · Cited by 96
An Integrative Pan-Cancer Analysis Revealing LCN2 as an Oncogenic Immune Protein in Tumor Microenvironment
Xu, W., Zhang, J., Hua, Y.-T., Yang, S., Wang, D., & Tang, J.-H. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.605097 · Cited by 95
Faecal Biomarkers in Inflammatory Bowel Diseases: Calprotectin Versus Lipocalin-2-a Comparative Study
Zollner, A., Schmiderer, A., Reider, S. J., Oberhuber, G., Pfister, A., Texler, B., Watschinger, C., Koch, R., Effenberger, M., Raine, T., et al. (2021) · Journal of Crohn's and Colitis · doi:10.1093/ecco-jcc/jjaa124 · Cited by 95
Lipocalin 2 as a link between ageing, risk factor conditions and age-related brain diseases
Dekens, D. W., Eisel, U. L. M., Gouweleeuw, L., Schoemaker, R. G., Deyn, P. P. D., & Naudé, P. J. W. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101414 · Cited by 93
The role of ferroptosis in acute lung injury
Liu, X., Zhang, J., & Xie, W. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04327-7 · Cited by 93
PGAM1 Inhibition Promotes HCC Ferroptosis and Synergizes with Anti‐PD‐1 Immunotherapy
Zheng, Y.-M., Wang, Y., Zhou, L., Wan, J., Jiang, L., Song, D., Wei, C., Gao, C., Shi, G., Zhou, J., et al. (2023) · Advanced Science · doi:10.1002/advs.202301928 · Cited by 92
Identification of gut microbiota and microbial metabolites regulated by an antimicrobial peptide lipocalin 2 in high fat diet-induced obesity
Qiu, X., Macchietto, M. G., Liu, X., Lu, Y., Ma, Y., Guo, H., Saqui–Salces, M., Bernlohr, D., Chen, C., Shen, S., et al. (2020) · International Journal of Obesity · doi:10.1038/s41366-020-00712-2 · Cited by 90
Iron Homeostasis and Metabolism: Two Sides of a Coin
Venkataramani, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_3 · Cited by 96
Mechanism of sorafenib resistance associated with ferroptosis in HCC
Guo, L., Hu, C., Yao, M., & Han, G. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1207496 · Cited by 97
Hepatocytes and neutrophils cooperatively suppress bacterial infection by differentially regulating lipocalin‐2 and neutrophil extracellular traps
Li, H., Feng, D., Cai, Y., Liu, Y., Xu, M., Xiang, X., Zhou, Z., Xia, Q., Kaplan, M. J., Kong, X., et al. (2018) · Hepatology · doi:10.1002/hep.29919 · Cited by 77
Iron status in the elderly: A review of recent evidence
Wawer, A. A., Jennings, A., & Fairweather‐Tait, S. J. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.07.003 · Cited by 77
Lipocalin-2: a therapeutic target to overcome neurodegenerative diseases by regulating reactive astrogliosis
Jung, B.-K., & Ryu, K. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01098-7 · Cited by 76
Obesity and Pancreatic Cancer: Insight into Mechanisms
Eibl, G., & Rozengurt, E. (2021) · Cancers · doi:10.3390/cancers13205067 · Cited by 76
Role of lipocalin 2 in stroke
Zhao, R., Wei, P., Sun, X., Zhang, D., He, Q., Liu, J., Chang, J., Yang, Y. R., & Guo, Z. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106044 · Cited by 72
PRMT1 is a novel molecular therapeutic target for clear cell renal cell carcinoma
Wang, J., Wang, C., Xu, P., Li, X., Lu, Y., Jin, D., Yin, X., Jiang, H., Huang, J. L., Xiong, H., et al. (2021) · Theranostics · doi:10.7150/thno.42345 · Cited by 70
Alterations in glutathione redox homeostasis among adolescents with obesity and anemia
Alkazemi, D. U. Z., Rahman, A., & Habra, B. (2021) · Scientific Reports · doi:10.1038/s41598-021-82579-5 · Cited by 77
Comprehensive review of lipocalin 2-mediated effects in lung inflammation
Guardado, E. S., Ojeda-Juárez, D., Kaul, M., & Nordgren, T. M. (2021) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00080.2021 · Cited by 70
Synergistic antitumor activity of pan-PI3K inhibition and immune checkpoint blockade in bladder cancer
Zhu, S., Ma, A.-H., Zhu, Z. G., Adib, E., Rao, T., Li, N., Ni, K., Chittepu, V. C. S. R., PRABHALA, R. H., Risco, J. G., et al. (2021) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2021-002917 · Cited by 66
Iron and iron-related proteins in COVID-19
Suriawinata, E., & Mehta, K. J. (2022) · Clinical and Experimental Medicine · doi:10.1007/s10238-022-00851-y · Cited by 70
Antioxidant Systems as Modulators of Ferroptosis: Focus on Transcription Factors
Punziano, C., Trombetti, S., Cesaro, E., Grosso, M., & Faraonio, R. (2024) · Antioxidants · doi:10.3390/antiox13030298 · Cited by 70
The battle for iron in enteric infections
Sousa Gerós, A., Simmons, A., Drakesmith, H., Aulicino, A., & Frost, J. N. (2020) · Immunology · doi:10.1111/imm.13236 · Cited by 58
Lcn2-derived Circular RNA (hsa_circ_0088732) Inhibits Cell Apoptosis and Promotes EMT in Glioma via the miR-661/RAB3D Axis
Jin, T., Liu, M., Liu, Y., Li, Y., Xu, Z., He, H., Liu, J., Zhang, Y., & Ke, Y. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00170 · Cited by 62
Lipocalin 2 regulates iron homeostasis, neuroinflammation, and insulin resistance in the brains of patients with dementia: Evidence from the current literature
Lim, D., Jeong, J., & Song, J. (2021) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13653 · Cited by 64
A bacterial immunomodulatory protein with lipocalin-like domains facilitates host–bacteria mutualism in larval zebrafish
Rolig, A. S., Sweeney, E. G., Kaye, L. E., DeSantis, M. D., Perkins, A., Banse, A. V., Hamilton, M. K., & Guillemin, K. J. (2018) · eLife · doi:10.7554/elife.37172 · Cited by 61
Glioma-derived exosomes hijack the blood–brain barrier to facilitate nanocapsule delivery via LCN2
Yang, C., Wu, Y., Wang, L., Li, S., Zhou, J., Tan, Y., Song, J. L., Xing, H., Yi, K., Zhan, Q., et al. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.03.038 · Cited by 61
Neutrophil extracellular trap-associated molecules: a review on their immunophysiological and inflammatory roles
Morales-Primo, A. U., Becker, I., & Zamora‐Chimal, J. (2021) · International Reviews of Immunology · doi:10.1080/08830185.2021.1921174 · Cited by 64
IL-6-mediated hepatocyte production is the primary source of plasma and urine neutrophil gelatinase associated lipocalin during acute kidney injury
Skrypnyk, N. I., Gist, K. M., Okamura, K., Montford, J. R., You, Z.-Y., Yang, H.-C., Moldovan, R., Bodoni, E., Blaine, J., Edelstein, C., et al. (2019) · Kidney International · doi:10.1016/j.kint.2019.11.013 · Cited by 53
Interleukin-33 Signaling Controls the Development of Iron-Recycling Macrophages
Lu, Y., Basatemur, G., Scott, I. C., Chiarugi, D., Clément, M., Harrison, J. E., Jugdaohsingh, R., Yu, X., Newland, S. A., Jolin, H. E., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.03.006 · Cited by 59
Lipocalin 2—not only a biomarker: a study of current literature and systematic findings of ongoing clinical trials
Asaf, S., Maqsood, F., Jalil, J., Sarfraz, Z., Sarfraz, A., Mustafa, S., & Chérrez-Ojeda, I. (2022) · Immunologic Research · doi:10.1007/s12026-022-09352-2 · Cited by 58
Single-cell and Spatial Transcriptomics Reveals Ferroptosis as The Most Enriched Programmed Cell Death Process in Hemorrhage Stroke-induced Oligodendrocyte-mediated White Matter Injury
Gu, L., Chen, H., Geng, R., Sun, M., Shi, Q., Chen, Y., Chang, J., Wei, J., Ma, W., Xiao, J., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.96262 · Cited by 58
Revisiting Neutrophil Gelatinase-Associated Lipocalin (NGAL) in Cancer: Saint or Sinner?
Bauvois, B., & Susín, S. A. (2018) · Cancers · doi:10.3390/cancers10090336 · Cited by 56
Tumor necrosis factor-α-primed mesenchymal stem cell-derived exosomes promote M2 macrophage polarization via Galectin-1 and modify intrauterine adhesion on a novel murine model
Li, J., Pan, Y., Yang, J., Wang, J., Jiang, Q., Dou, H., & Hou, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.945234 · Cited by 60
Mechanisms of iron homeostasis in Pseudomonas aeruginosa and emerging therapeutics directed to disrupt this vital process
Sánchez-Jiménez, A., Marcos‐Torres, F. J., & Llamas, M. A. (2023) · Microbial Biotechnology · doi:10.1111/1751-7915.14241 · Cited by 59
Molecular characterization of PANoptosis-related genes with features of immune dysregulation in systemic lupus erythematosus
Sun, W., Li, P., Wang, M., Xu, Y., Shen, D., Zhang, X., & Liu, Y. (2023) · Clinical Immunology · doi:10.1016/j.clim.2023.109660 · Cited by 56
Humoral regulation of iron metabolism by extracellular vesicles drives antibacterial response
Kuang, H., Dou, G., Cheng, L., Wang, X., Xu, H., Liu, X., Ding, F., Yang, X., Liu, S., Bao, L., et al. (2023) · Nature Metabolism · doi:10.1038/s42255-022-00723-5 · Cited by 53
Hypoxia Induces Astrocyte-Derived Lipocalin-2 in Ischemic Stroke
Taklimie, F. R., Gasterich, N., Scheld, M., Weiskirchen, R., Beyer, C., Clarner, T., & Zendedel, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061271 · Cited by 52
Identification of Zinc-Dependent Mechanisms Used by Group B Streptococcus To Overcome Calprotectin-Mediated Stress
Burcham, L. R., Le Breton, Y., Radin, J. N., Spencer, B. L., Deng, L., Hiron, A., Ransom, M. R., Mendonça, J. D. C., Belew, A. T., El-Sayed, N. M., et al. (2020) · mBio · doi:10.1128/mbio.02302-20 · Cited by 47
Organokines, Sarcopenia, and Metabolic Repercussions: The Vicious Cycle and the Interplay with Exercise
Minniti, G., Pescinini-Salzedas, L. M., Minniti, G. A. D. S., Laurindo, L. F., Barbalho, S. M., Sinatora, R. V., Sloan, L. A., Haber, R. S. D. A., Araújo, A. C., Quesada, K. R., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113452 · Cited by 53
Identification of Lipocalin 2 as a Potential Ferroptosis-related Gene in Ulcerative Colitis
Deng, L., He, S., Li, Y., Ding, R., Li, X., Guo, N., & Luo, L. (2023) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izad050 · Cited by 52
MafG/MYH9-LCN2 axis promotes liver fibrosis through inhibiting ferroptosis of hepatic stellate cells
Deng, Y., Lu, L., Zhu, D., Zhang, H., Fu, Y., Tan, Y., Tan, X., Guo, M., Zhang, Y., Yang, H., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01322-5 · Cited by 53
Mapping the Tooth Enamel Proteome and Amelogenin Phosphorylation Onto Mineralizing Porcine Tooth Crowns
Green, D. R., Schulte, F., Lee, K.-H., Pugach, M. K., Hardt, M., & Bidlack, F. B. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00925 · Cited by 48
3D two-photon brain imaging reveals dihydroartemisinin exerts antiepileptic effects by modulating iron homeostasis
Shao, C., Liu, Y., Chen, Z., Qin, Y., Wang, X., Wang, X., Yan, C., Zhu, H., Zhao, J., & Qian, Y. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.12.006 · Cited by 48
Iron metabolism, ferroptosis, and lncRNA in cancer: knowns and unknowns
Qu, L., He, X., Tang, Q., Xiao, F., Liu, J., & Lin, A. (2022) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2200194 · Cited by 48
LCN2 Mediates Skin Inflammation in Psoriasis through the SREBP2‒NLRC4 Axis
Ma, J., Chen, J., Xue, K., Chen, Y., Dang, E., Qiao, H., Fang, H., Pang, B., Li, Q., Sun, Z., et al. (2022) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.01.012 · Cited by 47
The interaction of lipocalin-2 and astrocytes in neuroinflammation: mechanisms and therapeutic application
Tan, Q., Zhang, C., Rao, X., Wan, W., Lin, W. J., Huang, S., Ying, J., Lin, Y., & Hua, F. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1358719 · Cited by 47
Paradoxical role of lipocalin-2 in metabolic disorders and neurological complications
Bhusal, A., Rahman, M. H., Lee, W., Bae, Y. C., Lee, I., & Suk, K. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113626 · Cited by 44
Controversies and Opportunities in the Use of Inflammatory Markers for Diagnosis or Risk Prediction in Fatty Liver Disease
Lambrecht, J., & Tacke, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.634409 · Cited by 46
Fast and Robust Proteome Screening Platform Identifies Neutrophil Extracellular Trap Formation in the Lung in Response to Cobalt Ferrite Nanoparticles
Billing, A. M., Knudsen, K. B., Chetwynd, A. J., Ellis, L. A., Tang, S. V. Y., Berthing, T., Wallin, H., Lynch, I., Vogel, U. B., & Kjeldsen, F. (2020) · ACS Nano · doi:10.1021/acsnano.9b08818 · Cited by 42
Plasma lipocalin‐2 levels in the preclinical stage of Alzheimer's disease
Eruysal, E., Ravdin, L., Kamel, H., Iadecola, C., & Ishii, M. (2019) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2019.07.004 · Cited by 42
Role of iron and iron‐related proteins in mesenchymal stem cells: Cellular and clinical aspects
Mehta, K. J. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30383 · Cited by 43
Identification and analysis of a prognostic ferroptosis and iron-metabolism signature for esophageal squamous cell carcinoma
Zhao, M., Li, M., Zheng, Y., Hu, Z., Liang, J., Bi, G., Bian, Y., Sui, Q., Zhan, C., Lin, M., et al. (2022) · Journal of Cancer · doi:10.7150/jca.68568 · Cited by 42
Dihydromyricetin attenuates intracerebral hemorrhage by reversing the effect of LCN2 via the system Xc- pathway
Liu, X., Li, Y., Chen, S., Yang, J., Jing, J., Li, J., Wu, X., Wang, J., Wang, J., Zhang, G., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154756 · Cited by 41
GPX4 restricts ferroptosis of NKp46+ILC3s to control intestinal inflammation
Li, X., He, J., Gao, X., Zheng, G., Chen, C., Chen, Y., Xing, Z., Wang, T., Tang, J., Guo, Y., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07060-3 · Cited by 40
Apocrine glands are bystanders in hidradenitis suppurativa and their involvement is gender specific
Zouboulis, C. C., da Costa, A. N., Fimmel, S., & Zouboulis, K. (2020) · Journal of the European Academy of Dermatology and Venereology · doi:10.1111/jdv.16264 · Cited by 40
Emerging role of ferrous iron in bacterial growth and host–pathogen interaction: New tools for chemical (micro)biology and antibacterial therapy
Gonciarz, R. L., & Renslo, A. R. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.01.015 · Cited by 39
Therapy-induced senescence promotes breast cancer cells plasticity by inducing Lipocalin-2 expression
Morales-Valencia, J., Lau, L., Martí-Nin, T., Özerdem, U., & David, G. (2022) · Oncogene · doi:10.1038/s41388-022-02433-4 · Cited by 40
Review of the potential of mesenchymal stem cells for the treatment of infectious diseases
Sharma, A., Chakraborty, A., & Jaganathan, B. G. (2021) · World Journal of Stem Cells · doi:10.4252/wjsc.v13.i6.568 · Cited by 38
Lipocalin-2 in Diabetic Complications of the Nervous System: Physiology, Pathology, and Beyond
Bhusal, A., Lee, W., & Suk, K. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.638112 · Cited by 37
Macrophage-derived mitochondria-rich extracellular vesicles aggravate bone loss in periodontitis by disrupting the mitochondrial dynamics of BMSCs
Yan, J., Tian, Y., Ma, S., Li, D., Hu, C., & Tan, J. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03178-4 · Cited by 40
Lipocalin-2 Functions as Inhibitor of Innate Resistance to Mycobacterium tuberculosis
Dahl, S. L., Woodworth, J. S., Lerche, C. J., Cramer, E. P., Nielsen, P. R., Moser, C. E., Thomsen, A. R., Borregaard, N., & Cowland, J. B. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02717 · Cited by 38
Comparative analysis of inflammatory signature profiles in eosinophilic and noneosinophilic chronic rhinosinusitis with nasal polyposis
Yao, Y., Yang, C., Yi, X., Xie, S., & Sun, H. (2020) · Bioscience Reports · doi:10.1042/bsr20193101 · Cited by 37
Caloric restriction reverses left ventricular hypertrophy through the regulation of cardiac iron homeostasis in impaired leptin signaling mice
An, H. S., Lee, J. Y., Choi, E. B., Jeong, E. A., Shin, H. J., Kim, K. E., Park, K.-A., Jin, Z. H., Lee, J. E., Koh, J. S., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-64201-2 · Cited by 36
Lipocalin‐2 Protects Against Diet‐Induced Nonalcoholic Fatty Liver Disease by Targeting Hepatocytes
Xu, Y., Zhu, Y., Jadhav, K. S., Li, Y., Sun, H., Yin, L., Kasumov, T., Chen, X., & Zhang, Y. (2019) · Hepatology Communications · doi:10.1002/hep4.1341 · Cited by 36
Biological Roles of Lipocalins in Chemical Communication, Reproduction, and Regulation of Microbiota
Stopková, R., Otcenásková, T., Matějková, T., Kuntová, B., & Stopka, P. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.740006 · Cited by 33
Transcriptome Profile in Hippocampus During Acute Inflammatory Response to Surgery: Toward Early Stage of PND
Xiang, X., Yu, Y., Tang, X., Chen, M., Zheng, Y., & Zhu, S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00149 · Cited by 33
Specific Commensal Bacterium Critically Regulates Gut Microbiota Osteoimmunomodulatory Actions During Normal Postpubertal Skeletal Growth and Maturation
Hathaway‐Schrader, J. D., Poulides, N. A., Carson, M. D., Kirkpatrick, J. E., Warner, A. J., Swanson, B. A., Taylor, E. V., Chew, M. E., Reddy, S. V., Liu, B., et al. (2020) · JBMR Plus · doi:10.1002/jbm4.10338 · Cited by 35
Role of Adipokines in Sarcopenia
Lu, W., Feng, W., Lai, J., Yuan, D., Xiao, W., & Li, Y. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002255 · Cited by 34
Whole-Blood Transcriptome Analysis of Feedlot Cattle With and Without Bovine Respiratory Disease
Jiminez, J. A., Timsit, E., Orsel, K., van der Meer, F. J. U. M., Guan, L. L., & Plastow, G. S. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.627623 · Cited by 33
Lipocalin-2: A Nurturer of Tumor Progression and a Novel Candidate for Targeted Cancer Therapy
Živalj, M., Ginderachter, J. A. V., & Stijlemans, B. (2023) · Cancers · doi:10.3390/cancers15215159 · Cited by 35
Inflammation Mediated by Gut Microbiome Alterations Promotes Lung Cancer Development and an Immunosuppressed Tumor Microenvironment
Rahal, Z., Liu, Y., Peng, F., Yang, S., Jamal, M. A., Sharma, M., Moreno, H., Damania, A. V., Wong, M. C., Ross, M. C., et al. (2024) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-24-0469 · Cited by 34
Rusty Microglia: Trainers of Innate Immunity in Alzheimer's Disease
Sfera, A., Gradini, R., Cummings, M., Diaz, E. L., Price, A. I., & Osorio, C. P. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.01062 · Cited by 32
Metagenomic Analysis of the Pediatric-Onset Multiple Sclerosis Gut Microbiome
Mirza, A., Zhu, F., Knox, N., Forbes, J. D., Domselaar, G. V., Bernstein, C. N., Graham, M., Marrie, R. A., Hart, J., Yeh, E. A., et al. (2021) · Neurology · doi:10.1212/wnl.0000000000013245 · Cited by 31
Identification of key candidate biomarkers for severe influenza infection by integrated bioinformatical analysis and initial clinical validation
Liu, S., Huang, Z., Deng, X., Zou, X., Li, H., Mu, S., & Cao, B. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16275 · Cited by 30
Severe anaemia, iron deficiency, and susceptibility to invasive bacterial infections
Abuga, K. M., Nairz, M., MacLennan, C. A., & Atkinson, S. H. (2023) · Wellcome Open Research · doi:10.12688/wellcomeopenres.18829.1 · Cited by 30
Loss of SREBP-1c ameliorates iron-induced liver fibrosis by decreasing lipocalin-2
Lee, E., Lee, J., ‍Kim, D. Y., Lee, Y.-S., Jo, Y., Dao, T., Kim, K. E., Song, D., Seo, J. H., Seo, Y., et al. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01213-2 · Cited by 29
Enterobactin induces the chemokine, interleukin-8, from intestinal epithelia by chelating intracellular iron
Saha, P., Yeoh, B. S., Xiao, X., Golonka, R. M., Abokor, A. A., Wenceslau, C. F., Shah, Y. M., Joe, B., & Vijay‐Kumar, M. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1841548 · Cited by 29
Serum lipocalin-2 is a potential biomarker for the clinical diagnosis of nonalcoholic steatohepatitis
Xu, G., Wang, Y., Ying, M., Chen, S., Li, Z., Ma, H., Zheng, M., Wu, J. H., & Ding, C. (2021) · Clinical and Molecular Hepatology · doi:10.3350/cmh.2020.0261 · Cited by 30
Lipocalin-2 participates in sepsis-induced myocardial injury by mediating lipid accumulation and mitochondrial dysfunction
Liu, W., Guo, X., Jin, L., Hong, T., Zhang, Q., Su, F., Shen, Y. X., Li, S., & He, B. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1009726 · Cited by 29
Lipocalin-2 promotes CKD vascular calcification by aggravating VSMCs ferroptosis through NCOA4/FTH1-mediated ferritinophagy
Wang, Y., Zhang, Y., Gao, M., Chen, Z., Lu, J., Li, Y., Di, Y., Zhao, Y., Liu, B.-C., & Tang, R. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07260-x · Cited by 28
Compensatory intestinal antibody response against pro-inflammatory microbiota after bariatric surgery
Scheithauer, T. P. M., Davids, M., Winkelmeijer, M., Verdoes, X., Aydin, Ö., de Brauw, M., van de Laar, A. W. J. M., Meijnikman, A. S., Gerdes, V. E. A., van Raalte, D. H., et al. (2022) · Gut Microbes · doi:10.1080/19490976.2022.2031696 · Cited by 29
Endocrine disrupting chemicals: A promoter of non-alcoholic fatty liver disease
Chen, Y., Wang, Y., Cui, Z., Liu, W., Liu, B., Zeng, Q., Zhao, X., Dou, J., & Cao, J. (2023) · Frontiers in Public Health · doi:10.3389/fpubh.2023.1154837 · Cited by 33
Bioinformatics and experimental approach identify lipocalin 2 as a diagnostic and prognostic indicator for lung adenocarcinoma
Li, A., Zhang, K., Zhou, J., Li, M., Fan, M., Gao, H., Ma, R., Gao, L., & Chen, M. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.132797 · Cited by 27

Lipocalin 2 alleviates iron toxicity by facilitating hypoferremia of inflammation and limiting catalytic iron generation
Xiao, X., Yeoh, B. S., Saha, P., Olvera, R. A., Singh, V., & Vijay–Kumar, M. (2016) · BioMetals · doi:10.1007/s10534-016-9925-5 · Cited by 29
Lipocalin 2, an innate immune protein, plays a key role in immune‐complex (IC) mediated inflammation
Aitken, J. D., Srinivasan, G., Sashidhramurthy, R., Parkos, C. A., Selvaraj, P., & Vijay–Kumar, M. (2012) · The FASEB Journal · doi:10.1096/fasebj.26.1_supplement.55.11
Lipocalin-2 is involved in immune-complex mediated inflammation (102.23)
Shashidharamurthy, R., Parkos, C. A., Selvaraj, P., & Vijay–Kumar, M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.186.supp.102.23
13 Lipocalin 2 exerts protective activity by alleviating inflammatory responses
Li, S. (2019) · Journal of Animal Science · doi:10.1093/jas/skz258.035
Characterization of lipocalin 2 ontogenic expression profile
Cruz, R. F. S. (2010) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

Authors: Xiao, X., Yeoh, B. S., & Vijay-Kumar, M.
Affiliations: Pennsylvania State University (US)
Department of Nutritional Sciences, The Pennsylvania State University, University Park, Pennsylvania 16802;
ORCID: Xiao, Xia
Yeoh, Beng San
Venue: Annual Review of Nutrition
Publisher: Annual Reviews
Published: 2017-08-21
Volume: 37
Issue: 1
Pages: 103-130
ISSN: 0199-9885 (ISSN-L)
1545-4312
DOI: 10.1146/annurev-nutr-071816-064559
OpenAlex: W2527347986
Cited by: 426
References: 204
Citations by year: 2026: 45 · 2025: 64 · 2024: 83 · 2023: 59 · 2022: 57 · 2021: 52 · 2020: 32 · 2019: 20 · 2018: 13
FWCI: 2.81
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.annualreviews.org/licenses/tdm (tdm)
Locations: Annual Review of Nutrition (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK097865)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords: neutrophil gelatinase-associated lipocalin, iron homeostasis, inflammation, nutritional immunity, siderophores, hypoferremia, labile iron pool, bacteriostatic activity, inflammatory bowel disease, neurodegenerative diseases, metabolic syndrome, kidney disease, skin diseases, cancer, therapeutic target
MeSH terms: Lipocalin-2, Animals, Bacteria, Homeostasis, Humans, Inflammation, Iron

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Lipocalin 2: An Emerging Player in Iron Homeostasis and Inflammation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks