Lipocalins and Insulin Resistance: Etiological Role of Retinol-Binding Protein 4 and Lipocalin-2?
Abstract
The prevalence of type 2 diabetes is increasing dramatically worldwide. Excess adiposity is an important contributor to the development of type 2 diabetes and cardiovascular diseases (1). Insulin resistance, inflammation, hypertension, and dyslipidemia, components of the metabolic syndrome, have been implicated in the effects of adiposity on type 2 diabetes and cardiovascular diseases, but the mechanisms responsible for these detrimental effects of adiposity have not been fully elucidated. Two paradigms are currently areas of intense study: one focused on ectopic fat and the other on the endocrine function of adipose tissue (2). Ectopic fat is present in nonadipose tissues such as the liver, muscle, and probably pancreatic β-cells. Both lipodystrophy (failure to develop adipose tissue) and obesity with full adipose cells are characterized by a lack of fat-storage capacity, resulting in overflow to other tissues of triglycerides and free fatty acids in the form of ectopic fat. Normal physiological processes can be disrupted by this ectopic fat, leading to insulin resistance and impaired insulin secretion. The endocrine function of adipose tissue is an important regulatory process throughout the body that is carried out by signaling proteins secreted by adipose tissue. These signaling proteins are called adipocytokines or adipokines, and they include leptin, adiponectin, resistin, tumor necrosis factor-α, and interleukin-6. Members of the lipocalin family of proteins have large sequence differences but share a common tertiary structure formed by segments termed lipocalin folds (3). Lipocalin folds consist of 8 antiparallel β-sheets that surround a hydrophobic pocket and allow lipocalins to function as transport or carrier proteins. Several human lipocalins have been identified, including retinol-binding protein 4 (RBP4), which has recently been added to the list of adipokines that may link obesity and insulin resistance (4)(5). In this issue of Clinical Chemistry, Dr. Wang and colleagues report on the association of lipocalin-2 with obesity, insulin resistance, and inflammation in mice and humans (6). Lipocalin-2 (also known as neutrophil gelatinase-associated lipocalin, siderocalin, 24p3, and uterocalin) has previously been shown to play a role in the innate immune response to infection by binding to iron-laden bacterial siderophores and thereby limiting bacterial growth (7). Wang et al. now report that circulating concentrations of lipocalin-2, as well as expression of lipocalin-2 in adipose and liver tissue, were increased in db/db obese diabetic mice compared with normal mice (6). Furthermore, plasma lipocalin-2 concentrations were higher in obese than in lean humans and were correlated with body mass index (BMI) and various components of the metabolic syndrome. After adjustment for BMI, statistically significant associations remained with fasting glucose, the Homeostasis Model Assessment (HOMA) index for insulin resistance, and C-reactive protein concentration. Treatment with the peroxisome proliferator–activated receptor-γ agonist rosiglitazone markedly decreased lipocalin-2 expression in mice and circulating concentrations in both mice and humans. These changes in lipocalin-2 were correlated with changes in C-reactive protein and HOMA insulin resistance (HOMA-IR) index. The authors should be commended for conducting this careful study using various techniques in both mice and humans. Their intriguing results raise the question whether lipocalin-2 can be useful as a predictor of cardiovascular diseases and whether lipocalin-2 has causal effects on insulin resistance, hyperglycemia, or inflammation and could thus be a treatment target. In the human study reported by Wang et al., the association between lipocalin-2 concentrations and indicators of glucose metabolism was attenuated after adjustment for BMI: No significant association remained with type 2 diabetes, 2-h plasma glucose concentrations, or fasting insulin concentrations, and only modest correlations remained with fasting glucose and the HOMA-IR index (6). Given that BMI may not have fully captured the effect of body fat or specific body fat depots, the strength of the reported associations independent of body fatness may have been overestimated. However, the parallel decrease in lipocalin-2 and HOMA-IR after rosiglitazone treatment provides some reassurance that cross-sectional associations with insulin resistance are not solely attributable to incomplete control for body fatness. Possibly, the independent associations with HOMA-IR and fasting glucose, but not 2-h glucose concentrations, reflect a specific association between lipocalin-2 and hepatic insulin sensitivity or glucose output rather than peripheral insulin sensitivity (8). Further human studies with more precise measures of body fatness and glucose homeostasis are needed to confirm the associations reported by Wang et al. (6). Decreased adipocyte expression of glucose transporter 4 (
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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 (siderocalin/NGAL) is strongly associated with the development of diabetes.
“Most importantly, lipocalin 2 (siderocalin/NGAL) is strongly associated with the development of diabetes [612,613].”
Cites
Wild, S., Roglic, G., Green, A., Sicree, R., & King, H. (2004) · Diabetes Care · doi:10.2337/diacare.27.5.1047 · Cited by 15,297 · see citing works
Tuomilehto, J., Lindström, J., Eriksson, J. G., Valle, T. T., Hämäläinen, H., Ilanne-Parikka, P., Keinänen-Kiukaanniemi, S., Laakso, M., Louheranta, A., Rastas, M., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejm200105033441801 · Cited by 10,873 · see citing works
Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes
Yang, Q., Graham, T. E., Mody, N., Preitner, F., Peroni, O. D., Zabolotny, J. M., Kotani, K., Quadro, L., & Kahn, B. B. (2005) · Nature · doi:10.1038/nature03711 · Cited by 2,086 · see citing works
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 · see citing works
Optimal Diets for Prevention of Coronary Heart Disease
Hu, F. B. (2002) · JAMA · doi:10.1001/jama.288.20.2569 · Cited by 1,503 · see citing works
Self-citationRetinol-Binding Protein 4 and Insulin Resistance in Lean, Obese, and Diabetic Subjects
Graham, T. E., Yang, Q., Blüher, M., Hammarstedt, A., Ciaraldi, T. P., Henry, R. R., Wason, C. J., Oberbach, A., Jansson, P.-A., Smith, U., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa054862 · Cited by 1,319 · see citing works
The endocrine function of adipose tissue: an update
Ronti, T., Lupattelli, G., & Mannarino, E. (2006) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2006.02474.x · Cited by 906 · see citing works
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 · see citing works
Retinol-Binding Protein 4 in Human Obesity
Janke, J., Engeli, S., Boschmann, M., Adams, F., Böhnke, J., Luft, F. C., Sharma, A. M., & Jordan, J. (2006) · Diabetes · doi:10.2337/db06-0616 · Cited by 351 · see citing works
Meyer, C., Pimenta, W., Woerle, H. J., Van Haeften, T., Szoke, E., Mitrakou, A., & Gerich, J. (2006) · Diabetes Care · doi:10.2337/dc06-0438 · Cited by 308 · see citing works
Neutrophil Gelatinase-associated Lipocalin, a Siderophore-binding Eukaryotic Protein
Borregaard, N., & Cowland, J. B. (2006) · BioMetals · doi:10.1007/s10534-005-3251-7 · Cited by 165 · see citing works
Markers of inflammation and their clinical significance
Ballantyne, C. M., & Nambi, V. (2005) · Atherosclerosis Supplements · doi:10.1016/j.atherosclerosissup.2005.02.005 · Cited by 164 · see citing works
Retinol-Binding Protein 4 and Insulin Resistance
Takashima, N., Tomoike, H., & Iwai, N. (2006) · New England Journal of Medicine · doi:10.1056/nejmc061863 · Cited by 106 · see citing works
Retinol-binding protein 4 and insulin resistance.
Erikstrup, C., Mortensen, O. H., & Pedersen, B. K. (2006) · PubMed · Cited by 70 · see citing works
Meade, T., Humphries, S. E., & Stavola, B. L. D. (2006) · International Journal of Epidemiology · doi:10.1093/ije/dyl149 · Cited by 15 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 555 · see citing works
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Identification of Liver Cancer-Specific Aptamers Using Whole Live Cells
Shangguan, D., Meng, L. H., Cao, Z. C., Xiao, Z., Fang, X., Li, Y., Cardona, D. M., Witek, R. P., Liu, C., & Tan, W. (2008) · Analytical Chemistry · doi:10.1021/ac701962v · Cited by 316 · see citing works
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 · see citing works
High Sugar-Induced Insulin Resistance in Drosophila Relies on the Lipocalin Neural Lazarillo
Pasco, M. Y., & Léopold, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036583 · Cited by 225 · see citing works
Free fatty acids and skeletal muscle insulin resistance
Kraegen, E. W., & Cooney, G. J. (2008) · Current Opinion in Lipidology · doi:10.1097/01.mol.0000319118.44995.9a · Cited by 206 · see citing works
Control of Metabolic Homeostasis by Stress Signaling Is Mediated by the Lipocalin NLaz
Hull‐Thompson, J., Muffat, J., Sánchez, D., Walker, D. W., Benzer, S., Ganfornina, M. D., & Jasper, H. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000460 · Cited by 146 · see citing works
Regulation of Drosophila lifespan by JNK signaling
Biteau, B., Karpac, J., Hwangbo, D., & Jasper, H. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.11.003 · Cited by 138 · see citing works
Lipocalin-2 Induces Cardiomyocyte Apoptosis by Increasing Intracellular Iron Accumulation
Xu, G., Ahn, J. H., Chang, S. Y., Eguchi, M., Ogier, A., Han, S., Park, Y., Shim, C. Y., Jang, Y., Yang, B., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.275719 · Cited by 136 · see citing works
Grenier, F. C., Ali, S., Syed, H., Workman, R., Martens, F., Liao, M., Wang, Y., & Wong, P.-Y. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.12.008 · Cited by 132 · see citing works
Auguet, T., Quintero, Y., Terra, X., Martínez, S., Lucas, A., Pellitero, S., Aguilar, C., Hernández, M., Castillo, D. D., & Richart, C. (2011) · Obesity · doi:10.1038/oby.2011.61 · Cited by 97 · see citing works
Nobili, V., Alkhouri, N., Alisi, A., Ottino, S., López, R., Manco, M., & Feldstein, A. E. (2009) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2008.12.031 · Cited by 76 · see citing works
Liu, J. T. C., Song, E., Xu, A., Berger, T., Mak, T. W., Tse, H., Law, I. K. M., Huang, B., Liang, Y., Vanhoutte, P. M., et al. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01587.x · Cited by 70 · see citing works
Kanaka‐Gantenbein, C., Margeli, A., Pervanidou, P., Sakka, S. D., Mastorakos, G. P., Chrousos, G. P., & Papassotiriou, I. (2008) · Clinical Chemistry · doi:10.1373/clinchem.2007.099002 · Cited by 61 · see citing works
Petta, S., Cammà, C., Marco, V. D., Alessi, N., Barbaria, F., Cabibi, D., Caldarella, R., Ciminnisi, S., Licata, A., Massenti, M. F., et al. (2008) · Hepatology · doi:10.1002/hep.22316 · Cited by 60 · see citing works
Retinol-binding protein-4 in experimental and clinical metabolic disease
von Eynatten, M., & Humpert, P. M. (2008) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.8.3.289 · Cited by 49 · see citing works
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 · see citing works
Hasanuzzam, M., Saidur, R., & Masjuki, H. H. (2008) · Journal of Applied Sciences · doi:10.3923/jas.2008.1822.1831 · Cited by 43 · see citing works
Rashad, N. M., El‐Shal, A. S., Etewa, R. L., & Wadea, F. M. (2017) · IUBMB Life · doi:10.1002/iub.1594 · Cited by 42 · see citing works
Cengız, C., Akışın, Y. A., Bulut, S., & Boyacıoğlu, S. (2010) · European Journal of Gastroenterology & Hepatology · doi:10.1097/meg.0b013e32833283cb · Cited by 38 · see citing works
Corripio, R., González-Clemente, J. M., Pérez, J., Näf, S., Gallart, L., Nosas, R., Vendrell, J. J., & Caixàs, A. (2010) · European Journal of Endocrinology · doi:10.1530/eje-10-0408 · Cited by 34 · see citing works
Yang, B., Fan, P., Xu, A., Lam, K. S., Berger, T., Mak, T. W., Tse, H., Yue, J. W., Song, E., Vanhoutte, P. M., et al. (2012) · Europe PMC (PubMed Central) · Cited by 32 · see citing works
Zhou, Z., Chen, H., Ju, H., & Sun, M. (2017) · Lipids in Health and Disease · doi:10.1186/s12944-017-0566-7 · Cited by 31 · see citing works
Petta, S., Tripodo, C., Grimaudo, S., Cabibi, D., Cammà, C., Cristina, A. D., Marco, V. D., Vita, G. D., Ingrao, S., Mazzola, A., et al. (2011) · Digestive and Liver Disease · doi:10.1016/j.dld.2010.12.013 · Cited by 30 · see citing works
Li, M., Wang, Z., Zhu, L., Shui, Y., Zhang, S., & Guo, W. (2021) · Bioscience Reports · doi:10.1042/bsr20210328 · Cited by 28 · see citing works
Wang, D., Zhao, Y., Wang, L., Ren, G., Wang, F., Xia, Z., Wang, X., Zhang, T., Pan, Q., Dai, Z., et al. (2010) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-010-0927-3 · Cited by 27 · see citing works
Lipocalin-2 plasmatic levels are reduced in patients with long-term type 2 diabetes mellitus.
de la Chesnaye, E., Manuel‐Apolinar, L., Zárate, A., Damasio, L., Espino, N., Revilla-Monsalve, M. C., & Islas‐Andrade, S. (2015) · PubMed Central · Cited by 26 · see citing works
Serum AFBP levels are elevated in patients with nonalcoholic fatty liver disease
Suh, J.-B., Kim, S. M., Cho, G.-J., & Choi, K. M. (2014) · Scandinavian Journal of Gastroenterology · doi:10.3109/00365521.2013.836754 · Cited by 24 · see citing works
Effects of Resistance versus Endurance Training on Plasma Lipocalin-2 in Young Men.
Moghadasi, M., & Domieh, A. M. (2014) · Europe PMC (PubMed Central) · Cited by 23 · see citing works
Serum FGF21 and RBP4 levels in patients with chronic hepatitis C
Kukla, M., Berdowska, A., Stygar, D. M., Gabriel, A., Mazur, W., Łogiewa-Bazger, B., Sobala‐Szczygieł, B., Bułdak, R. J., Rokitka, M., Zajęcki, W., et al. (2012) · Scandinavian Journal of Gastroenterology · doi:10.3109/00365521.2012.694901 · Cited by 23 · see citing works
The importance of steatosis in chronic hepatitis C infection and its management: A review
Cross, T., Rashid, M. M., Berry, P., & Harrison, P. (2010) · Hepatology Research · doi:10.1111/j.1872-034x.2010.00626.x · Cited by 20 · see citing works
Review article Insulin resistance and its consequences in chronic hepatitis C
Kukla, M., Piotrowski, D., Waluga, M., & Hartleb, M. (2015) · Clinical and Experimental Hepatology · doi:10.5114/ceh.2015.51375 · Cited by 18 · see citing works
González-Lopez, M., Sealls, W., Jesch, E. D., Brosnan, M. J., Ladunga, I., Ding, X., Black, P. N., & Dirusso, C. (2010) · Physiological Genomics · doi:10.1152/physiolgenomics.00209.2010 · Cited by 18 · see citing works
Akelma, A. Z., Abacı, A., Özdemir, O., Çelik, A., Avcı, Z., Razi, C. H., Hızlı, Ş., & Akın, O. (2012) · Journal of Pediatric Endocrinology and Metabolism · doi:10.1515/jpem-2011-0477 · Cited by 16 · see citing works
Molecular interactions of the neuronal GPI‐anchored lipocalin Lazarillo
Sánchez, D., Ortega‐Cubero, S., Åkerström, B., Herrera, M., Bastiani, M. J., & Ganfornina, M. D. (2008) · Journal of Molecular Recognition · doi:10.1002/jmr.902 · Cited by 16 · see citing works
Navrotskaya, V., Oxenkrug, G., Vorobyova, L., & Summergrad, P. (2015) · Integrative Obesity and Diabetes · doi:10.15761/iod.1000120 · Cited by 14 · see citing works
Lipocalin-2: Response to a Progressive Treadmill Protocol in Obese and Normal-weight Men
Damirchi, A., Rahmani‐Nia, F., & Mehrabani, J. (2011) · Asian Journal of Sports Medicine · doi:10.5812/asjsm.34821 · Cited by 14 · see citing works
Tyczyńska, M., Hunek, G., Szczasny, M., Brachet, A., Januszewski, J., Forma, A., Portincasa, P., Flieger, J., & Baj, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094916 · Cited by 13 · see citing works
Horvath, J. E., Seres, I., Paragh, G., Fülöp, P., & Jenei, Z. (2024) · Nutrients · doi:10.3390/nu16234251 · Cited by 11 · see citing works
Związek między stężeniami lipokaliny-2 i testosteronu wolnego w zespole policystycznych jajników
Yilmaz, Ö., Temür, M., Çalan, M., Küme, T., Özbay, P. Ö., Karakulak, M., & Yapucu, S. (2017) · Endokrynologia Polska · doi:10.5603/ep.2017.0002 · Cited by 11 · see citing works
The Transthyretin—Retinol-Binding Protein Complex
Monaco, H. L. (2009) · Springer eBooks · doi:10.1007/978-3-642-00646-3_8 · Cited by 11 · see citing works
Plasma lipocalin‐2 levels in pregnancy
CESUR, S., Yücel, A., Noyan, V., & Sağsöz, N. (2011) · Acta Obstetricia Et Gynecologica Scandinavica · doi:10.1111/j.1600-0412.2011.01158.x · Cited by 9 · see citing works
de la Chesnaye, E., Manuel‐Apolinar, L., Damasio, L., Olivares, A., Palomino, M. A., Santos, I., & ndez, J. P. M. ⁄. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6196 · Cited by 7 · see citing works
Botta, A. M., Forest, A., Daneault, C., Pantopoulos, K., Tantiworawit, A., Phrommintikul, A., Chattipakorn, S. C., Chattipakorn, N., Rosiers, C. D., & Sweeney, G. (2021) · Metabolites · doi:10.3390/metabo11020070 · Cited by 7 · see citing works
Ou, H., Wu, H., Yang, Y., Wu, J., Cheng, J., & Chang, C. (2011) · Hormone and Metabolic Research · doi:10.1055/s-0031-1271746 · Cited by 6 · see citing works
The role of novel adipokines in hepatocellular carcinoma progression: a mini review
Hu, P. (2024) · American Journal of Cancer Research · doi:10.62347/pzdm1736 · Cited by 4 · see citing works
The role of free iron in cardiovascular diseases - Part I
Izzo, M., Gasbarro, V., & Coscia, V. (2017) · Journal of Theoretical and Applied Vascular Research · doi:10.24019/jtavr.23 · Cited by 3 · see citing works
Lipocalin-2: Response to a short-term treadmill protocol in obese and normal-weight men
Damirchi, A., Rahmani‐Nia, F., & Mehrabani, J. (2011) · Journal of Human Sport and Exercise · doi:10.4100/jhse.2011.61.07 · Cited by 2 · see citing works
Rasmy, H. S., Malatawy, M. A. E. F. E., ElKarmoty, K. Z., Abdelwarth, E. Y., & Isaac, A. (2023) · Egyptian Liver Journal · doi:10.1186/s43066-023-00251-1 · Cited by 1 · see citing works
Function of eEF-1γ in the nucleus in response to insulin in hepatocellular carcinoma cells
Hossain, A. J., Hamza, A., Islam, R., Dogsom, O., & Park, J. (2025) · Communications Biology · doi:10.1038/s42003-025-08247-w · Cited by 1 · see citing works
Kim, J., Rhee, E., Choi, E.-S., Won, J. C., Park, C., Lee, W., Oh, K.-W., Kim, B. J., Sung, K., Kim, B., et al. (2009) · Korean Diabetes Journal · doi:10.4093/kdj.2009.33.2.105 · Cited by 1 · see citing works
Fan, P., & Wang, Y. (2011) · InTech eBooks · doi:10.5772/20378
Salem, G., & Pasha, H. F. (2015)
Choi, K. M. (2008) · Journal of Korean Endocrine Society · doi:10.3803/jkes.2008.23.4.219
Lin, Y., Cui, X., Zhu, N., Li, Y., Wang, P., Wang, X., Yi, Y., & Li, X. (2024) · Diseases · doi:10.3390/diseases12110291
- Authors
- van Dam, R. M., & Hu, F. B.
- Affiliations
- Departments of Nutrition and Epidemiology, Harvard School of Public Health, Boston MA
- Brigham and Women's Hospital (US)
- ORCID
- Hu, Frank B
- Venue
- Clinical Chemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-01-01
- Volume
- 53
- Issue
- 1
- Pages
- 5-7
- ISSN
- 0009-9147 (ISSN-L)
- 1530-8561
- OpenAlex
- W2065104239
- Cited by
- 57
- References
- 15
- Citations by year
- 2025: 1 · 2024: 4 · 2023: 1 · 2021: 2 · 2019: 1 · 2018: 1 · 2017: 5 · 2015: 4 · 2014: 2 · 2012: 5
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- Clinical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- lipocalin, insulin resistance, retinol-binding protein 4, neutrophil gelatinase-associated lipocalin, siderocalin, adipokines, obesity, ectopic fat, lipodystrophy, inflammation, type 2 diabetes, metabolic syndrome, adipose tissue endocrine function, iron metabolism, innate immunity
- MeSH terms
- Lipocalin-2, Rosiglitazone, Acute-Phase Proteins, Adipose Tissue, Animals, C-Reactive Protein, Humans, Inflammation, Insulin Resistance, Liver, Mice, Obese, Obesity, Proto-Oncogene Proteins, Retinol-Binding Proteins, Oncogene Proteins, Body Mass Index, Thiazolidinediones, PPAR gamma, Mice, Lipocalins, Retinol-Binding Proteins, Plasma
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
