Lactoferrin in aseptic and septic inflammation

Lepanto, Maria Stefania; Rosa, Luigi; Paesano, Rosalba; Valenti, Piera; Cutone, Antimo

doi:10.3390/molecules24071323

Cited by 147Iron Metabolism and DisordersInfant Nutrition and HealthImmune Response and Inflammation

Lactoferrin in aseptic and septic inflammation

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Lepanto, Maria Stefania, Rosa, Luigi, Paesano, Rosalba, Valenti, Piera, Cutone, Antimo·2019·Molecules

DOI 10.3390/molecules24071323PMC PMC6480387

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Abstract

Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is synthesized by exocrine glands and neutrophils. Since the first anti-microbial function attributed to Lf, several activities have been discovered, including the relevant anti-inflammatory one, especially associated to the down-regulation of pro-inflammatory cytokines, as IL-6. As high levels of IL-6 are involved in iron homeostasis disorders, Lf is emerging as a potent regulator of iron and inflammatory homeostasis. Here, the role of Lf against aseptic and septic inflammation has been reviewed. In particular, in the context of aseptic inflammation, as anemia of inflammation, preterm delivery, Alzheimer’s disease and type 2 diabetes, Lf administration reduces local and/or systemic inflammation. Moreover, Lf oral administration, by decreasing serum IL-6, reverts iron homeostasis disorders. Regarding septic inflammation occurring in Chlamydia trachomatis infection, cystic fibrosis and inflammatory bowel disease, Lf, besides the anti-inflammatory activity, exerts a significant activity against bacterial adhesion, invasion and colonization. Lastly, a critical analysis of literature in vitro data reporting contradictory results on the Lf role in inflammatory processes, ranging from pro- to anti-inflammatory activity, highlighted that they depend on cell models, cell metabolic status, stimulatory or infecting agents as well as on Lf iron saturation degree, integrity and purity.

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Lactoferrin, through binding to its cognate receptor, promotes the maturation, migration and cell proliferation of many immune cells including macrophages and monocytes, which impact the efficacy of host responses in the course of infections.
“In addition to its role in scavenging iron, lactoferrin, through binding to its cognate receptor, promotes the maturation, migration and cell proliferation of many immune cells including macrophages and monocytes which impact on the efficacy of host responses in the course of infections (Actor et al., 2009; Legrand, 2012; Lepanto et al., 2019).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Lepanto et al., 2019

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Neutrophil Emigration in the Skin, Lungs, and Peritoneum: Different Requirements for CD11/CD18 Revealed by CD18-deficient Mice
Mizgerd, J. P., Kubo, H., Kutkoski, G. J., Bhagwan, S. D., Scharffetter-Kochanek, K., Beaudet, A. L., & Doerschuk, C. M. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.8.1357 · Cited by 7,332 · see citing works
Tolerance, Danger, and the Extended Family
Matzinger, P. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.005015 · Cited by 4,848 · see citing works
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
Ecological and Evolutionary Forces Shaping Microbial Diversity in the Human Intestine
Ley, R. E., Peterson, D. A., & Gordon, J. I. (2006) · Cell · doi:10.1016/j.cell.2006.02.017 · Cited by 3,358 · see citing works
The gut flora as a forgotten organ
O'Hara, A. M., & Shanahan, F. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400731 · Cited by 2,791 · see citing works
IRS-1-Mediated Inhibition of Insulin Receptor Tyrosine Kinase Activity in TNF-α- and Obesity-Induced Insulin Resistance
Hotamisligil, G. S., Peraldi, P., Budavari, A., Ellis, R., White, M. F., & Spiegelman, B. M. (1996) · Science · doi:10.1126/science.271.5249.665 · Cited by 2,630 · see citing works
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
Disorders of Iron Metabolism
Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · see citing works
Ferric Carboxymaltose in Patients with Heart Failure and Iron Deficiency
Anker, S. D., Comin Colet, J., Filippatos, G., Willenheimer, R., Dickstein, K., Drexler, H., Lüscher, T. F., Bart, B., Banasiak, W., Niegowska, J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0908355 · Cited by 2,083 · see citing works
An ecological and evolutionary perspective on human–microbe mutualism and disease
Dethlefsen, L., McFall-Ngai, M., & Relman, D. A. (2007) · Nature · doi:10.1038/nature06245 · Cited by 1,660 · see citing works
Integrated Systems Approach Identifies Genetic Nodes and Networks in Late-Onset Alzheimer’s Disease
Zhang, B., Gaiteri, C., Bodea, L.-G., Wang, Z., McElwee, J., Podtelezhnikov, A. A., Zhang, C., Xie, T., Tran, L., Dobrin, R., et al. (2013) · Cell · doi:10.1016/j.cell.2013.03.030 · Cited by 1,657 · see citing works
Control of pathogens and pathobionts by the gut microbiota
Kamada, N., Chen, G. Y., Inohara, N., & Núñez, G. (2013) · Nature Immunology · doi:10.1038/ni.2608 · Cited by 1,625 · see citing works
The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β
Yin, M.-J., Yamamoto, Y., & Gaynor, R. B. (1998) · Nature · doi:10.1038/23948 · Cited by 1,596 · see citing works
High prevalence of adherent-invasive Escherichia coli associated with ileal mucosa in Crohn’s disease
Darfeuille-Michaud, A., Boudeau, J., Bulois, P., Neut, C., Glasser, A.-L., Barnich, N., Bringer, M.-A., Swidsinski, A., Beaugerie, L., & Colombel, J.-F. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.04.061 · Cited by 1,566 · see citing works
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324 · see citing works
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275 · see citing works
Differential Alteration in Intestinal Epithelial Cell Expression of Toll-Like Receptor 3 (TLR3) and TLR4 in Inflammatory Bowel Disease
Cario, E., & Podolsky, D. K. (2000) · Infection and Immunity · doi:10.1128/iai.68.12.7010-7017.2000 · Cited by 1,245 · see citing works
Anemia of inflammation
Weiss, G., Ganz, T., & Goodnough, L. T. (2019) · Blood · doi:10.1182/blood-2018-06-856500 · Cited by 1,219 · see citing works
Intravascular Danger Signals Guide Neutrophils to Sites of Sterile Inflammation
McDonald, B., Pittman, K., Menezes, G. B., Hirota, S. A., Slaba, I., Waterhouse, C. C. M., Beck, P. L., Muruve, D. A., & Kubes, P. (2010) · Science · doi:10.1126/science.1195491 · Cited by 1,210 · see citing works
REVIEW ARTICLE: Th1/Th2/Th17 and Regulatory T‐Cell Paradigm in Pregnancy
Saito, S., Nakashima, A., Shima, T., & Ito, M. (2010) · American Journal of Reproductive Immunology · doi:10.1111/j.1600-0897.2010.00852.x · Cited by 1,126 · see citing works
Infant mortality statistics from the 2004 period linked birth/infant death data set.
Mathews, T. J., & MacDorman, M. F. (2007) · PubMed · doi:10.13016/v2ql-unmj · Cited by 1,044 · see citing works
Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action
Aguirre, V., Werner, E. D., Giraud, J., Lee, Y. H., Shoelson, S. E., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m101521200 · Cited by 1,010 · see citing works
Infant mortality statistics from the 2001 period linked birth/infant death data set.
Mathews, T. J., Menacker, F., & MacDorman, M. F. (2003) · PubMed · Cited by 967 · see citing works
Mice lacking granulocyte colony-stimulating factor have chronic neutropenia, granulocyte and macrophage progenitor cell deficiency, and impaired neutrophil mobilization
Lieschke, G. J., Grail, D., HODGSON, G. S., Metcalf, D., Stanley, E. G., Cheers, C., Fowler, K., Basu, S., Zhan, Y., & Dunn, A. (1994) · Blood · doi:10.1182/blood.v84.6.1737.1737 · Cited by 956 · see citing works
IL-6 and Its Soluble Receptor Orchestrate a Temporal Switch in the Pattern of Leukocyte Recruitment Seen during Acute Inflammation
Hurst, S. M., Wilkinson, T. S., McLoughlin, R. M., Jones, S., Horiuchi, S., Yamamoto, N., Rose-John, S., Fuller, G. M., Topley, N., & Jones, S. A. (2001) · Immunity · doi:10.1016/s1074-7613(01)00151-0 · Cited by 811 · see citing works
Intestinal Permeability Regulation by Tight Junction: Implication on Inflammatory Bowel Diseases
Lee, S. H. (2015) · Intestinal Research · doi:10.5217/ir.2015.13.1.11 · Cited by 810 · see citing works
The Changing Microbial Epidemiology in Cystic Fibrosis
LiPuma, J. J. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00068-09 · Cited by 801 · see citing works
Central and Systemic Endotoxin Challenges Exacerbate the Local Inflammatory Response and Increase Neuronal Death during Chronic Neurodegeneration
Cunningham, C., Wilcockson, D. C., Campion, S., Lunnon, K., & Perry, V. H. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2614-05.2005 · Cited by 768 · see citing works
Intramuscular desferrioxamine in patients with Alzheimer's disease
MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764 · see citing works
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 · see citing works
LACTOFERRIN, AN IRON-BINBING PROTEIN NI NEUTROPHILIC LEUKOCYTES
Masson, P. L., Heremans, J. F., & Schonne, E. (1969) · The Journal of Experimental Medicine · doi:10.1084/jem.130.3.643 · Cited by 700 · see citing works
A Bactericidal Effect for Human Lactoferrin
Arnold, R. R., Cole, M. F., & McGhee, J. R. (1977) · Science · doi:10.1126/science.327545 · Cited by 677 · see citing works
Iron status during pregnancy: setting the stage for mother and infant
Scholl, T. O. (2005) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/81.5.1218 · Cited by 664 · see citing works
Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease
Weinstein, D. A., Roy, C. N., Fleming, M. D., Loda, M. F., Wolfsdorf, J. I., & Andrews, N. C. (2002) · Blood · doi:10.1182/blood-2002-04-1260 · Cited by 632 · see citing works
Glucose Challenge Stimulates Reactive Oxygen Species (ROS) Generation by Leucocytes
Mohanty, P., Hamouda, W., Garg, R., Aljada, A., Ghanim, H., & Dandona, P. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.8.6854 · Cited by 621 · see citing works
Macrophages in intestinal homeostasis and inflammation
Bain, C. C., & Mowat, A. M. (2014) · Immunological Reviews · doi:10.1111/imr.12192 · Cited by 615 · see citing works
Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N ‐terminal region of bovine lactoferrin
Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., & TOMITA, M. (1992) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1992.tb05007.x · Cited by 588 · see citing works
An iron-binding protein common to many external secretions
Masson, P. L., Heremans, J. F., & Dive, C. H. (1966) · Clinica Chimica Acta · doi:10.1016/0009-8981(66)90004-0 · Cited by 577 · see citing works
A Molecular Basis for Insulin Resistance
Paz, K., Hemi, R., LeRoith, D., Karasik, A., Elhanany, E., Kanety, H., & Zick, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29911 · Cited by 553 · see citing works
Cerclage for Short Cervix on Ultrasonography in Women With Singleton Gestations and Previous Preterm Birth
Berghella, V., Rafael, T. J., Szychowski, J. M., Rust, O. A., & Owen, J. (2011) · Obstetrics and Gynecology · doi:10.1097/aog.0b013e31820ca847 · Cited by 544 · see citing works
The role of interleukin-1 in the pathogenesis of IDDM
Mandrup-Poulsen, T. R. (1996) · Diabetologia · doi:10.1007/bf00400649 · Cited by 543 · see citing works
Bovine Lactoferrin Supplementation for Prevention of Late-Onset Sepsis in Very Low-Birth-Weight Neonates A Randomized Trial
Manzoni, P. (2009) · JAMA · doi:10.1001/jama.2009.1403 · Cited by 520 · see citing works
Inflammatory processes in preterm and term parturition
Christiaens, I., Zaragoza, D. B., Guilbert, L., Robertson, S. A., Mitchell, B. F., & Olson, D. M. (2008) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2008.04.002 · Cited by 490 · see citing works
Iron Homeostasis and the Inflammatory Response
Wessling-Resnick, M. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104804 · Cited by 480 · see citing works
Lactoferrin
Valenti, P., & Antonini, G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5372-0 · Cited by 470 · see citing works
Adherent Invasive Escherichia coli Strains from Patients with Crohn's Disease Survive and Replicate within Macrophages without Inducing Host Cell Death
Glasser, A.-L., Boudeau, J., Barnich, N., Perruchot, M.-H., Colombel, J., & Darfeuille–Michaud, A. (2001) · Infection and Immunity · doi:10.1128/iai.69.9.5529-5537.2001 · Cited by 465 · see citing works
Lactoferrin: Multifunctional roles of lactoferrin: a critical overview
Ward, P. P., Paz, E., & Conneely, O. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5369-8 · Cited by 443 · see citing works
Differential regulation of iron homeostasis during human macrophage polarized activation
Recalcati, S., Locati, M., Marini, A., Santambrogio, P., Zaninotto, F., De Pizzol, M., Zammataro, L., Girelli, D., & Cairo, G. (2010) · European Journal of Immunology · doi:10.1002/eji.200939889 · Cited by 438 · see citing works
Inhibition of SARS Pseudovirus Cell Entry by Lactoferrin Binding to Heparan Sulfate Proteoglycans
Lang, J., Yang, N., Deng, J., Liu, K., Yang, P., Zhang, G., & Jiang, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023710 · Cited by 428 · see citing works
Cytokine-mediated regulation of iron transport in human monocytic cells
Ludwiczek, S., Aigner, E., Theurl, I., & Weiss, G. (2003) · Blood · doi:10.1182/blood-2002-08-2459 · Cited by 420 · see citing works
Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
Moore, S. A., Anderson, B. F., Groom, C. R., Haridas, M., & Baker, E. N. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1386 · Cited by 417 · see citing works
Bacterial Vaginosis Assessed by Gram Stain and Diminished Colonization Resistance to Incident Gonococcal, Chlamydial, and Trichomonal Genital Infection
Brotman, R. M., Klebanoff, M. A., Nansel, T. R., Yu, K. F., Andrews, W. W., Zhang, J., & Schwebke, J. R. (2010) · The Journal of Infectious Diseases · doi:10.1086/657320 · Cited by 417 · see citing works
Iron homeostasis during pregnancy
Fisher, A. L., & Nemeth, E. (2017) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.155812 · Cited by 409 · see citing works
Anemia of inflammation
Nemeth, E., & Ganz, T. (2014) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2014.04.005 · Cited by 401 · see citing works
Sustained effects of interleukin-1 receptor antagonist treatment in type 2 diabetes
Larsen, C. M., Faulenbach, M., Vaag, A., Ehses, J. A., Donath, M. Y., & Mandrup-Poulsen, T. (2009) · Diabetes Care · doi:10.2337/dc09-0533 · Cited by 401 · see citing works
The Solution Structure of Human Hepcidin, a Peptide Hormone with Antimicrobial Activity That Is Involved in Iron Uptake and Hereditary Hemochromatosis
Hunter, H. N., Fulton, D. B., Ganz, T., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205305200 · Cited by 400 · see citing works
Molecular diversity of Escherichia coli in the human gut: New ecological evidence supporting the role of adherent-invasive E. coli (AIEC) in Crohnʼs disease
Martínez-Medina, M., Aldeguer, X., López‐Siles, M., Gónzalez‐Huix, F., López-Oliu, C., Dahbi, G., Blanco, J. E., Blanco, J., Garcia-Gil, L. J., & Darfeuille–Michaud, A. (2009) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20860 · Cited by 398 · see citing works
Receptor-mediated Transcytosis of Lactoferrin through the Blood-Brain Barrier
Fillebeen, C., Descamps, L., Dehouck, M., Fénart, L., Benaı̈ssa, M., Spik, G., Cecchelli, R., & Pierce, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7011 · Cited by 385 · see citing works
Lactoferrin
Suzuki, Y. A., López, V., & Lönnerdal, B. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5371-1 · Cited by 384 · see citing works
Lactoferrin: a natural Glycoprotein involved in iron and inflammatory homeostasis
Rosa, L., Cutone, A., Lepanto, M., Paesano, R., & Valenti, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091985 · Cited by 376 · see citing works
Self-citation
Evaluation of Vaginal Complaints
Anderson, M. (2004) · JAMA · doi:10.1001/jama.291.11.1368 · Cited by 375 · see citing works
Haemostatic reference intervals in pregnancy
Jørgensen, M., Klajnbard, A., Andersen, M. R., Colov, N. P., Stender, S., & Szecsi, P. B. (2010) · Thrombosis and Haemostasis · doi:10.1160/th09-10-0704 · Cited by 364 · see citing works
Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
Andersen, B. F., Baker, H. M., Morris, G. E., Rumball, S. V., & Baker, E. N. (1990) · Nature · doi:10.1038/344784a0 · Cited by 363 · see citing works
β-Defensin-2 Expression Is Regulated by TLR Signaling in Intestinal Epithelial Cells
Vora, P., Youdim, A., Thomas, L. S., Fukata, M., Tesfay, S., Lukasek, K., Michelsen, K. S., Wada, A., Hirayama, T., Arditi, M., et al. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5398 · Cited by 358 · see citing works
Antiviral properties of lactoferrin--a natural immunity molecule
Berlutti, F., Pantanella, F., Natalizi, T., Frioni, A., Paesano, R., Polimeni, A., & Valenti, P. (2011) · Molecules · doi:10.3390/molecules16086992 · Cited by 356 · see citing works
Self-citation
The Isolation of a Red Protein from Milk2
Groves, M. L. (1960) · Journal of the American Chemical Society · doi:10.1021/ja01498a029 · Cited by 350 · see citing works
The role of interleukins in insulin resistance and type 2 diabetes mellitus
Fève, B., & Bastard, J.-P. (2009) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2009.62 · Cited by 343 · see citing works
Hepcidin-Induced Endocytosis of Ferroportin Is Dependent on Ferroportin Ubiquitination
Qiao, B., Sugianto, P., Fung, E., del-Castillo-Rueda, A., Moran-Jimenez, M.-J., Ganz, T., & Nemeth, E. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.03.018 · Cited by 334 · see citing works
Intranasal delivery of Huperzine A to the brain using lactoferrin-conjugated N-trimethylated chitosan surface-modified PLGA nanoparticles for treatment of Alzheimer’s disease
Meng, Q., Wang, A., Hua, H., Jiang, Y. Y., Wang, Y., Mu, H., Wu, Z., & Sun, K. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s151474 · Cited by 313 · see citing works
Lactoferrin in a Context of Inflammation-Induced Pathology
Kruzel, M. L., Zimecki, M., & Actor, J. K. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01438 · Cited by 308 · see citing works
Polarization dictates iron handling by inflammatory and alternatively activated macrophages
Corna, G., Campana, L., Pignatti, E., Castiglioni, A., Tagliafico, E., Bosurgi, L., Campanella, A., Brunelli, S., Manfredi, A. A., Apostoli, P., et al. (2010) · Haematologica · doi:10.3324/haematol.2010.023879 · Cited by 304 · see citing works
Isolation of an Iron-Containing Red Protein from Human Milk.
Johanson, B., Virtanen, A. I., Tweit, R. C., & Dodson, R. M. (1960) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.14-0510 · Cited by 301 · see citing works
Adherent-invasive Escherichia coli in inflammatory bowel disease
Rolhion, N., & Darfeuille–Michaud, A. (2007) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20176 · Cited by 299 · see citing works
Hereditary thrombophilia.
Khan, S., & Dickerman, J. D. (2006) · Thrombosis Journal · doi:10.1186/1477-9560-4-15 · Cited by 290 · see citing works
Iron and Alzheimer’s Disease: From Pathogenesis to Therapeutic Implications
Liu, J., Fan, Y., Yang, Z., Wang, Z., & Guo, C. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00632 · Cited by 286 · see citing works
Lactoferrin: a review
Adlerova, L., Bartoskova, A., & Faldyna, M. (2008) · Veterinární Medicína · doi:10.17221/1978-vetmed · Cited by 285 · see citing works
A structural framework for understanding the multifunctional character of lactoferrin
Baker, E. N., & BAKER, H. (2008) · Biochimie · doi:10.1016/j.biochi.2008.05.006 · Cited by 279 · see citing works
Barrier function in the peripheral and central nervous system—a review
Reinhold, A., & Rittner, H. L. (2016) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-016-1920-8 · Cited by 279 · see citing works
Overview of Lactoferrin as a Natural Immune Modulator.
Legrand, D. (2016) · Jornal de Pediatria · doi:10.1016/j.jpeds.2016.02.071 · Cited by 274 · see citing works
Sterile inflammation and pregnancy complications: a review
Nadeau‐Vallée, M., Obari, D., Palacios, J. L., Brien, M., Duval, C., Chemtob, S., & Girard, S. (2016) · Reproduction · doi:10.1530/rep-16-0453 · Cited by 274 · see citing works
Iron and infection
Ganz, T. (2018) · International Journal of Hematology · doi:10.1007/s12185-017-2366-2 · Cited by 270 · see citing works
Understanding the Bacterial Flora of the Female Genital Tract
Larsen, B., & Monif, G. R. G. (2001) · Clinical Infectious Diseases · doi:10.1086/318710 · Cited by 266 · see citing works
Préparation et propriétés de la lactosidérophiline (lactotransferrine) du lait de femme
Montreuil, J., Tonnelat, J., & Mullet, S. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)91478-5 · Cited by 265 · see citing works
Diversity of Human Vaginal Bacterial Communities and Associations with Clinically Defined Bacterial Vaginosis
Oakley, B. B., Fiedler, T. L., Marrazzo, J. M., & Fredricks, D. N. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02884-07 · Cited by 264 · see citing works
Infant formula and infant nutrition: bioactive proteins of human milk and implications for composition of infant formulas.
Lönnerdal, B. (2014) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.113.071993 · Cited by 263 · see citing works
Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin
van der Kraan, M. I. A., Groenink, J., Nazmi, K., Veerman, E. C. I., Bolscher, J. G. M., & Amerongen, A. V. N. (2004) · Peptides · doi:10.1016/j.peptides.2003.12.006 · Cited by 254 · see citing works
Salicylate (Salsalate) in Patients With Type 2 Diabetes: A Randomized Trial
Goldfine, A. B., Fonseca, V., Jablonski, K. A., Chen, Y.-D. I., Tipton, L., Staten, M. A., & Shoelson, S. E. (2013) · Annals of Internal Medicine · doi:10.7326/0003-4819-159-1-201307020-00003 · Cited by 251 · see citing works
Invasive Escherichia coli are a feature of Crohn's disease
Sasaki, M., Sitaraman, S. V., Babbin, B. A., Gerner‐Smidt, P., Ribot, E. M., Garrett, N. A., Alpern, J. A., Akyildiz, A., Theiss, A. L., Nusrat, A., et al. (2007) · Laboratory Investigation · doi:10.1038/labinvest.3700661 · Cited by 243 · see citing works
Persistence of Human Milk Proteins in the Breast‐Fed Infant
Davidson, L. A., & Lönnerdal, B. L. (1987) · Acta Paediatrica · doi:10.1111/j.1651-2227.1987.tb10557.x · Cited by 238 · see citing works
Inflammation, Infection, and Pulmonary Function in Infants and Young Children with Cystic Fibrosis
Dakin, C., Numa, A. H., Wang, H., Morton, J. R., VERTZYAS, C. C., & Henry, R. L. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.165.7.2010139 · Cited by 233 · see citing works
Expression of iron transport proteins and excessive iron accumulation in the brain in neurodegenerative disorders
Qian, Z., & Wang, Q. (1998) · Brain Research Reviews · doi:10.1016/s0165-0173(98)00012-5 · Cited by 230 · see citing works
Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells
Legrand, D., Vigié, K., Said, E. A., Elass, E., Masson, M., Slomianny, M., Carpentier, M., Briand, J., Mazurier, J., & Hovanessian, A. G. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03929.x · Cited by 228 · see citing works
Interleukin-6 stimulates prostaglandin production by human amnion and decidual cells.
Mitchell, M. D., Dudley, D. J., Edwin, S. S., & Schiller, S. L. (1991) · European Journal of Pharmacology · doi:10.1016/0014-2999(91)90090-d · Cited by 228 · see citing works
Changing Epidemiology of the Respiratory Bacteriology of Patients With Cystic Fibrosis
Salsgiver, E. L., Fink, A. K., Knapp, E. A., LiPuma, J. J., Olivier, K. N., Marshall, B. C., & Saiman, L. M. (2015) · CHEST Journal · doi:10.1378/chest.15-0676 · Cited by 224 · see citing works
Enteral lactoferrin supplementation for prevention of sepsis and necrotizing enterocolitis in preterm infants
Pammi, M., & Suresh, G. (2017) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd007137.pub5 · Cited by 218 · see citing works
Role of Lactobacilli and Lactoferrin in the Mucosal Cervicovaginal Defense
Valenti, P., Rosa, L., Capobianco, D., Lepanto, M. S., Schiavi, E., Cutone, A., Paesano, R., & Mastromarino, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00376 · Cited by 218 · see citing works
Structure and Reactivity of Transferrins
Baker, E. N. (1994) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60176-2 · Cited by 215 · see citing works
Metal Chelation as a Potential Therapy for Alzheimer's Disease
Cuajungco, M. P., Faget, K. Y., Huang, X., Tanzi, R. E., & Bush, A. I. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06938.x · Cited by 215 · see citing works
The orchestration of body iron intake: how and where do enterocytes receive their cues?
Frazer, D. M., & Anderson, G. J. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00039-1 · Cited by 211 · see citing works
The Gut Barrier
Scaldaferri, F., Pizzoferrato, M., Gerardi, V., Lopetuso, L. R., & Gasbarrini, A. (2012) · Journal of Clinical Gastroenterology · doi:10.1097/mcg.0b013e31826ae849 · Cited by 203 · see citing works
Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer's disease
Guo, C., Wang, T., Zheng, W. H., Shan, Z., Teng, W., & Wang, Z. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.05.009 · Cited by 200 · see citing works
G-CSF stimulates angiogenesis and promotes tumor growth: potential contribution of bone marrow-derived endothelial progenitor cells
Natori, T., Sata, M., Washida, M., Hirata, Y., Nagai, R., & Makuuchi, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02335-5 · Cited by 200 · see citing works
A complex interplay between the extracellular matrix and the innate immune response to microbial pathogens
Tomlin, H., & Piccinini, A. M. (2018) · Immunology · doi:10.1111/imm.12972 · Cited by 198 · see citing works
Lactoferrin, a key molecule in immune and inflammatory processes <sup>1</sup> This article is part of Special Issue entitled Lactoferrin and has undergone the Journal’s usual peer review process.
Legrand, D. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-056 · Cited by 193 · see citing works
Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain
Guo, C., Wang, P., Zhong, M., Wang, T., Huang, X., Li, J., & Wang, Z. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.12.005 · Cited by 191 · see citing works
Iron homeostasis: An anthropocentric perspective
Coffey, R., & Ganz, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.781823 · Cited by 189 · see citing works
The role of the intestinal microbiota in enteric infection
Sekirov, I., & Finlay, B. B. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.172742 · Cited by 188 · see citing works
Abnormal Intestinal Permeability Predicts Relapse in Inactive Crohn Disease
Arnott, K. K. I. D. R. (2000) · Scandinavian Journal of Gastroenterology · doi:10.1080/003655200750056637 · Cited by 184 · see citing works
Response of Chlamydia trachomatis serovar E to iron restriction in vitro and evidence for iron-regulated chlamydial proteins
Raulston, J. E. (1997) · Infection and Immunity · doi:10.1128/iai.65.11.4539-4547.1997 · Cited by 177 · see citing works
Structure of Haemophilus influenzae Fe+3-binding protein reveals convergent evolution within a superfamily
Bruns, C. M., Nowalk, A. J., Arvai, A. S., McTigue, M. A., Vaughan, K. G., Mietzner, T. A., & McRee, D. E. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb1197-919 · Cited by 177 · see citing works
Glycosylation of Human Milk Lactoferrin Exhibits Dynamic Changes During Early Lactation Enhancing Its Role in Pathogenic Bacteria-Host Interactions
Barboza, M., Pinzon, J., Wickramasinghe, S., Froehlich, J. W., Moeller, I., Smilowitz, J. T., Ruhaak, L. R., Huang, J., Lönnerdal, B. L., German, J. B., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015248 · Cited by 176 · see citing works
Lactotransferrin immunocytochemistry in Alzheimer and normal human brain.
Kawamata, T., Tooyama, I., Yamada, T., Walker, D. G., & McGeer, P. L. (1993) · PubMed Central · Cited by 173 · see citing works
Local and Systemic Cytokine Levels in Relation to Changes in Vaginal Flora
Hedges, S. R., Barrientes, F. J., Desmond, R. A., & Schwebke, J. R. (2006) · The Journal of Infectious Diseases · doi:10.1086/499824 · Cited by 170 · see citing works
Transferrins: insights into structure and function from studies on lactoferrin
Baker, E. N., Rumball, S. V., & Anderson, B. F. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90163-0 · Cited by 168 · see citing works
Studying Lactoferrin N-Glycosylation
Karav, S., German, J., Rouquié, C., Parc, A. L., & Barile, D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040870 · Cited by 166 · see citing works
Thrombophilia and Pregnancy Complications
Simcox, L. E., Ormesher, L., Tower, C. L., & Greer, I. A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161226104 · Cited by 165 · see citing works
Apo‐ and holo‐lactoferrin are both internalized by lactoferrin receptor via clathrin‐mediated endocytosis but differentially affect ERK‐signaling and cell proliferation in caco‐2 cells
Jiang, R., López, V., Kelleher, S. L., & Lönnerdal, B. L. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22650 · Cited by 162 · see citing works
Bacterial vaginosis as a risk factor for upper genital tract infection
Peipert, J. F., Montagno, A. B., Cooper, A. S., & Sung, C. J. (1997) · American Journal of Obstetrics and Gynecology · doi:10.1016/s0002-9378(97)70038-3 · Cited by 161 · see citing works
Vaginitis.
Hainer, B. L., & Gibson, M. V. (2011) · PubMed · Cited by 157 · see citing works
Differential effects of glucose and alcohol on reactive oxygen species generation and intranuclear nuclear factor-κB in mononuclear cells
Dhindsa, S., Tripathy, D., Mohanty, P., Ghanim, H., Syed, T., Aljada, A., & Dandona, P. (2004) · Metabolism · doi:10.1016/j.metabol.2003.10.013 · Cited by 156 · see citing works
Activated astroglia during chronic inflammation in Alzheimer's disease—Do they neglect their neurosupportive roles?
Fuller, S. L., Steele, M. L., & Münch, G. W. (2009) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2009.08.016 · Cited by 155 · see citing works
Treatment with Anakinra Improves Disposition Index But Not Insulin Sensitivity in Nondiabetic Subjects with the Metabolic Syndrome: A Randomized, Double-Blind, Placebo-Controlled Study
van Asseldonk, E. J. P., Stienstra, R., Koenen, T. B., Joosten, L. A. B., Netea, M. G., & Tack, C. J. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-2992 · Cited by 155 · see citing works
Lactoferrin: Balancing Ups and Downs of Inflammation Due to Microbial Infections
Drago-Serrano, M., Campos-Rodríguez, R., Carrero, J., & De la Garza, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030501 · Cited by 151 · see citing works
Domain Closure in Lactoferrin
Gerstein, M., Anderson, B. F., Norris, G. E., Baker, E. N., Lesk, A. M., & Chothia, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1592 · Cited by 150 · see citing works
Microevolution of Pseudomonas aeruginosa to a Chronic Pathogen of the Cystic Fibrosis Lung
Hogardt, M., & Heesemann, J. (2011) · Current topics in microbiology and immunology · doi:10.1007/82_2011_199 · Cited by 144 · see citing works
Effect of anti‐ IL ‐1β antibody (canakinumab) on insulin secretion rates in impaired glucose tolerance or type 2 diabetes: results of a randomized, placebo‐controlled trial
Rissanen, A., Howard, C. P., Botha, J., Thuren, T. Y., & for the Global Investigators (2012) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2012.01637.x · Cited by 140 · see citing works
Oral administration of lactoferrin reduces colitis in rats via modulation of the immune system and correction of cytokine imbalance
Togawa, J.-I., Nagase, H., Tanaka, K., Inamori, M., Nakajima, A., Ueno, N., Saito, T., & Sekihara, H. (2002) · Journal of Gastroenterology and Hepatology · doi:10.1046/j.1440-1746.2002.02868.x · Cited by 133 · see citing works
The role of N‐linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis
van Veen, H. A., Geerts, M., van Berkel, P. H. C., & Nuijens, J. H. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2003.03965.x · Cited by 132 · see citing works
The iron-binding protein lactotransferrin is present in pathologic lesions in a variety of neurodegenerative disorders: a comparative immunohistochemical analysis
Leveugle, B., Spik, G., Perl, D. P., Bouras, C., Fillit, H. M., & Hof, P. R. (1994) · Brain Research · doi:10.1016/0006-8993(94)90202-x · Cited by 131 · see citing works
Hepcidin agonists as therapeutic tools
Casu, C., Nemeth, E., & Rivella, S. (2018) · Blood · doi:10.1182/blood-2017-11-737411 · Cited by 131 · see citing works
A structural perspective on lactoferrin function <sup>1</sup> This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.
Baker, H. M., & Baker, E. N. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-071 · Cited by 130 · see citing works
Lactoferrin activates macrophages via TLR4-dependent and -independent signaling pathways
Curran, C. S., Demick, K. P., & Mansfield, J. M. (2006) · Cellular Immunology · doi:10.1016/j.cellimm.2006.08.006 · Cited by 130 · see citing works
The preterm parturition syndrome and its implications for understanding the biology, risk assessment, diagnosis, treatment and prevention of preterm birth
Gotsch, F., Gotsch, F., Romero, R. J., Erez, O., Vaisbuch, E., Kusanovic, J. P., Mazaki‐Tovi, S., Kim, S. K., Hassan, S. S., & Yeo, L. (2009) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.1080/14767050902860690 · Cited by 130 · see citing works
Increased Iron Deposition on Brain Quantitative Susceptibility Mapping Correlates with Decreased Cognitive Function in Alzheimer’s Disease
Du, L., Zhao, Z., Cui, A., Zhu, Y., Zhang, L., Liu, J., Shi, S., Fu, C., Han, X., Gao, W., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00194 · Cited by 129 · see citing works
Lactoferrin: A Critical Player in Neonatal Host Defense
Telang, S. (2018) · Nutrients · doi:10.3390/nu10091228 · Cited by 127 · see citing works
Biochemical and molecular impacts of lactoferrin on small intestinal growth and development during early life1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.
Liao, Y., Jiang, R., & Lönnerdal, B. L. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-075 · Cited by 125 · see citing works
Disorders of Iron Metabolism
Conrad, M. E., & Jn, U. (2000) · New England Journal of Medicine · doi:10.1056/nejm200004273421716 · Cited by 125 · see citing works
Structure of human diferric lactoferrin refined at 2.2 Å resolution
Haridas, M., Anderson, B. F., & Baker, E. N. (1995) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994013521 · Cited by 122 · see citing works
Regulation of cytokine production during phagocytosis of apoptotic cells
Chung, E. Y., Kim, S. J., & Jing, X. (2006) · Cell Research · doi:10.1038/sj.cr.7310021 · Cited by 118 · see citing works
Cellular internalization of lactoferrin in intestinal epithelial cells
Ashida, K., Sasaki, H., Suzuki, Y. A., & Lönnerdal, B. (2004) · BioMetals · doi:10.1023/b:biom.0000027710.13543.3f · Cited by 117 · see citing works
Intelectin: A Novel Lipid Raft-Associated Protein in the Enterocyte Brush Border
Wrackmeyer, U., Hansen, G. H., Seya, T., & Danielsen, E. M. (2006) · Biochemistry · doi:10.1021/bi060570x · Cited by 113 · see citing works
NF-κB and the intestine: Friend or foe?
Karrasch, T., & Jobin, C. (2007) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20243 · Cited by 112 · see citing works
Intranasal Lactoferrin Enhances α-Secretase-Dependent Amyloid Precursor Protein Processing via the ERK1/2-CREB and HIF-1α Pathways in an Alzheimer’s Disease Mouse Model
Guo, C., Yang, Z., Zhang, S., Chai, R., Han, X., Zhang, Y., Li, J., & Wang, Z. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2017.8 · Cited by 111 · see citing works
Impact of interleukin-1β antibody (canakinumab) on glycaemic indicators in patients with type 2 diabetes mellitus: Results of secondary endpoints from a randomized, placebo-controlled trial
Hensen, J., Howard, C. P., Walter, V., & Thuren, T. Y. (2013) · Diabetes & Metabolism · doi:10.1016/j.diabet.2013.07.003 · Cited by 107 · see citing works
Iron-sensitive fluorescent probes: monitoring intracellular iron pools
Ma, Y., Abbate, V., & Hider, R. C. (2014) · Metallomics · doi:10.1039/c4mt00214h · Cited by 106 · see citing works
Characterization of the Glycosaminoglycan-Binding Region of Lactoferrin
Wu, H. F., Monroe, D. M., & Church, F. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1139 · Cited by 104 · see citing works
Elevated amniotic fluid interleukin-6 levels at genetic amniocentesis predict subsequent pregnancy loss
Wenstrom, K. D., Andrews, W. W., Tamura, T., DuBard, M. B., Johnston, K. E., & Hemstreet, G. P. (1996) · American Journal of Obstetrics and Gynecology · doi:10.1016/s0002-9378(96)80007-x · Cited by 101 · see citing works
Bovine Lactoferrin Counteracts Toll-Like Receptor Mediated Activation Signals in Antigen Presenting Cells
Puddu, P., Latorre, D., Carollo, M., Catizone, A., Ricci, G., Valenti, P., & Gessani, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022504 · Cited by 100 · see citing works
Recent advancements in the field of nanotechnology for the delivery of anti-Alzheimer drug in the brain region
Agrawal, M., Saraf, S., Saraf, S., Antimisiaris, S. G., Hamano, N., Li, S., Chougule, M. B., Shoyele, S., Gupta, U. D., Ajazuddin, M., et al. (2018) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2018.1471058 · Cited by 100 · see citing works
Lactoferrin Efficiently Counteracts the Inflammation-Induced Changes of the Iron Homeostasis System in Macrophages
Cutone, A., Rosa, L., Lepanto, M. S., Scotti, M. J., Berlutti, F., di Patti, M. C. B., Musci, G., & Valenti, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00705 · Cited by 99 · see citing works
Dynamic properties of the tight junction barrier
Weber, C. R. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06528.x · Cited by 98 · see citing works
The role of gastrointestinal permeability in food allergy
Samadi, N., Klems, M., & Untersmayr, E. (2018) · Annals of Allergy Asthma & Immunology · doi:10.1016/j.anai.2018.05.010 · Cited by 97 · see citing works
A pilot study on the effect of lactoferrin on Alzheimer’s disease pathological sequelae: Impact of the p-Akt/PTEN pathway
Mohamed, W., Salama, R. M., & Schaalan, M. F. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.118 · Cited by 97 · see citing works
The role of inflammation in venous thromboembolism and the link between arterial and venous thrombosis.
Poredoš, P., & Jezovnik, M. K. (2007) · PubMed · Cited by 95 · see citing works
Role of IKK and ERK pathways in intrinsic inflammation of cystic fibrosis airways
Verhaeghe, C., Remouchamps, C., Hennuy, B., Vanderplasschen, A. F. C., Chariot, A., Tabruyn, S. P., Oury, C., & Bours, V. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.03.019 · Cited by 95 · see citing works
Uptake of ingested bovine lactoferrin and its accumulation in adult mouse tissues
Fischer, R., Debbabi, H., Blais, A., Dubarry, M., Rautureau, M., Boyaka, P. N., & Tomé, D. (2007) · International Immunopharmacology · doi:10.1016/j.intimp.2007.05.019 · Cited by 95 · see citing works
Oral administration of lactoferrin increases hemoglobin and total serum iron in pregnant womenThis paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal's usual peer review process.
Paesano, R., Torcia, F., Berlutti, F., Pacifici, E., Ebano, V., Moscarini, M., & Valenti, P. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-040 · Cited by 95 · see citing works
Adherent-invasive Escherichia coli (AIEC) in pediatric Crohn’s disease patients: phenotypic and genetic pathogenic features
Conte, M. P., Longhi, C., Marazzato, M., Conte, A. L., Aleandri, M., Lepanto, M. S., Zagaglia, C., Nicoletti, M., Aloi, M., Totino, V., et al. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-748 · Cited by 94 · see citing works
Efficacy of Lactoferrin Oral Administration in the Treatment of Anemia and Anemia of Inflammation in Pregnant and Non-pregnant Women: An Interventional Study
Lepanto, M. S., Rosa, L., Cutone, A., Conte, M. P., Paesano, R., & Valenti, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02123 · Cited by 90 · see citing works
Relationship between fecal lactoferrin and inflammatory bowel disease
Dai, J., Liu, W., Zhao, Y.-P., Hu, Y., & Ge, Z. (2007) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520701427094 · Cited by 89 · see citing works
Mechanistic Differences Leading to Infectious and Sterile Inflammation
Behnia, F., Sheller‐Miller, S., & Menon, R. (2016) · American Journal of Reproductive Immunology · doi:10.1111/aji.12496 · Cited by 89 · see citing works
The cell surface expressed nucleolin is a glycoprotein that triggers calcium entry into mammalian cells
Losfeld, M., Khoury, D. E., Mariot, P., Carpentier, M., Krust, B., Briand, J., Mazurier, J., Hovanessian, A. G., & Legrand, D. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.10.039 · Cited by 86 · see citing works
Ca2+ binding to bovine lactoferrin enhances protein stability and influences the release of bacterial lipopolysaccharide
Rossi, P., Giansanti, F., Boffi, A., Ajello, M., Valenti, P., Chiancone, E., & Antonini, G. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-209 · Cited by 86 · see citing works
Infant mortality statistics from the 2007 period linked birth/infant death data set.
Mathews, T. J., & MacDorman, M. F. (2011) · PubMed · Cited by 85 · see citing works
Precuneus amyloid burden is associated with reduced cholinergic activity in Alzheimer disease
Ikonomović, M. D., Klunk, W. E., Abrahamson, E. E., Wuu, J., Mathis, C. A., Scheff, S. W., Mufson, E. J., & DeKosky, S. T. (2011) · Neurology · doi:10.1212/wnl.0b013e3182231419 · Cited by 84 · see citing works
Biological effects of mutant ceruloplasmin on hepcidin-mediated internalization of ferroportin
Kono, S., Yoshida, K., Tomosugi, N., Terada, T., Hamaya, Y., Kanaoka, S., & Miyajima, H. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.07.011 · Cited by 83 · see citing works
Determining the Cause of Vulvovaginal Symptoms
Farage, M. A., Miller, K. W., & Ledger, W. J. (2008) · Obstetrical & Gynecological Survey · doi:10.1097/ogx.0b013e318172ee25 · Cited by 82 · see citing works
Lactoferrin downregulates pro-inflammatory cytokines upexpressed in intestinal epithelial cells infected with invasive or noninvasive Escherichia coli strainsThis paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal’s usual peer review process.
Berlutti, F., Schippa, S., Morea, C., Sarli, S., Perfetto, B., Donnarumma, G., & Valenti, P. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-039 · Cited by 82 · see citing works
Integrated Review of Cytokines in Maternal, Cord, and Newborn Blood: Part I—Associations With Preterm Birth
Lyon, D., Cheng, C., Howland, L. C., Rattican, D., Jallo, N., Pickler, R. H., Brown, L., & McGrath, J. M. (2009) · Biological Research For Nursing · doi:10.1177/1099800409344620 · Cited by 80 · see citing works
The In Vitro Protective Role of Bovine Lactoferrin on Intestinal Epithelial Barrier
Zhao, X., Xu, X., Liu, Y., Xi, E.-Z., An, J., Tabys, D., & Liu, N. (2019) · Molecules · doi:10.3390/molecules24010148 · Cited by 80 · see citing works
Microbiota of the upper and lower genital tract
Rampersaud, R., Randis, T. M., & Ratner, A. J. (2011) · Seminars in Fetal and Neonatal Medicine · doi:10.1016/j.siny.2011.08.006 · Cited by 79 · see citing works
Pathophysiology and classification of iron overload diseases; update 2018
Brissot, P., Troadec, M., Loréal, O., & Brissot, É. (2018) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2018.08.006 · Cited by 79 · see citing works
Commensal Bacteria-Specific CD4+ T Cell Responses in Health and Disease
Sorini, C., Cardoso, R. F., Gagliani, N., & Villablanca, E. J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02667 · Cited by 76 · see citing works
The N1 domain of human lactoferrin is required for internalization by caco-2 cells and targeting to the nucleus
Suzuki, Y. A., Wong, H., Ashida, K.-Y., Schryvers, A. B., & Lönnerdal, B. (2008) · Biochemistry · doi:10.1021/bi8012164 · Cited by 75 · see citing works
The increased maternal serum levels of IL-6 are associated with the severity and onset of preeclampsia
Xiao, J., Yin, Y., Gao, Y., Lau, S., Shen, F., Zhao, M., & Chen, Q. (2012) · Cytokine · doi:10.1016/j.cyto.2012.07.039 · Cited by 74 · see citing works
Lactoferrin: an alternative view of its role in human biological fluids1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.
Alexander, D. B., Iigo, M., Yamauchi, K., Suzui, M., & Tsuda, H. (2012) · Biochemistry and Cell Biology · doi:10.1139/o2012-013 · Cited by 73 · see citing works
Do Astrocytes Collaborate with Neurons in Spreading the “Infectious” Aβ and Tau Drivers of Alzheimer’s Disease?
Prà, I. D., Chiarini, A., Gui, L., Chakravarthy, B., Pacchiana, R., Gardenal, E., Whitfield, J. F., & Armato, U. (2014) · The Neuroscientist · doi:10.1177/1073858414529828 · Cited by 73 · see citing works
Cell death in the pathogenesis of immune-mediated diseases
Pisetsky, D. S. (2011) · Swiss Medical Weekly · doi:10.4414/smw.2011.13256 · Cited by 72 · see citing works
Health status and work burden of Alzheimer patients’ informal caregivers
Colvez, A., Joël, M.-È., Ponton-Sanchez, A., & Royer, A.-C. (2002) · Health Policy · doi:10.1016/s0168-8510(01)00215-9 · Cited by 69 · see citing works
Lactoferrin differently modulates the inflammatory response in epithelial models mimicking human inflammatory and infectious diseases
Frioni, A., Conte, M. P., Cutone, A., Longhi, C., Musci, G., di Patti, M. C. B., Natalizi, T., Marazzato, M., Lepanto, M. S., Puddu, P., et al. (2014) · BioMetals · doi:10.1007/s10534-014-9740-9 · Cited by 69 · see citing works
5 The Present Status of Chelating Agents in Medicine
May, P. M., & Bulman, R. A. (1983) · Progress in medicinal chemistry · doi:10.1016/s0079-6468(08)70220-0 · Cited by 69 · see citing works
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Paesano, R., Berlutti, F., Pietropaoli, M., Goolsbee, W., Pacifici, E., & Valenti, P. (2010) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463201002300220 · Cited by 69 · see citing works
Study on the effects of an oral lactobacilli and lactoferrin complex in women with intermediate vaginal microbiota
Russo, R., Edu, A., & Seta, F. D. (2018) · Archives of Gynecology and Obstetrics · doi:10.1007/s00404-018-4771-z · Cited by 68 · see citing works
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Mohamed, W., & Schaalan, M. F. (2018) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-018-0390-x · Cited by 66 · see citing works
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Cutone, A., Frioni, A., Berlutti, F., Valenti, P., Musci, G., & di Patti, M. C. B. (2014) · BioMetals · doi:10.1007/s10534-014-9742-7 · Cited by 63 · see citing works
Structural Heterogeneity and Multifunctionality of Lactoferrin
Albar, A. H., Almehdar, H. A., Uversky, V. N., & Redwan, E. M. M. M. (2014) · Current Protein and Peptide Science · doi:10.2174/1389203715666140919124530 · Cited by 63 · see citing works
Recombinant Human Intelectin Binds Bovine Lactoferrin and Its Peptides
Shin, K., Wakabayashi, H., Yamauchi, K., Yaeshima, T., & Iwatsuki, K. (2008) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.31.1605 · Cited by 62 · see citing works
Effect of recombinant human erythropoietin on anaemia and disease activity in patients with rheumatoid arthritis and anaemia of chronic disease: a randomised placebo controlled double blind 52 weeks clinical trial.
Peeters, H., Jongen‐Lavrencic, M., Vreugdenhil, G., & Swaak, A. J. G. (1996) · Annals of the Rheumatic Diseases · doi:10.1136/ard.55.10.739 · Cited by 60 · see citing works
The Chlamydia trachomatis Ctad1 invasin exploits the human integrin β1 receptor for host cell entry
Stallmann, S., & Hegemann, J. H. (2015) · Cellular Microbiology · doi:10.1111/cmi.12549 · Cited by 60 · see citing works
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Valenti, P., Greco, R., Pitari, G., Rossi, P., Ajello, M., Melino, G., & Antonini, G. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4500 · Cited by 59 · see citing works
Safety and efficacy of lactoferrin versus ferrous sulphate in curing iron deficiency and iron deficiency anaemia in hereditary thrombophilia pregnant women: an interventional study
Paesano, R., Pacifici, E., Benedetti, S., Berlutti, F., Frioni, A., Polimeni, A., & Valenti, P. (2014) · BioMetals · doi:10.1007/s10534-014-9723-x · Cited by 59 · see citing works
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Beigi, R. H., Yudin, M. H., Cosentino, L. A., Meyn, L. A., & Hillier, S. L. (2007) · The Journal of Infectious Diseases · doi:10.1086/521628 · Cited by 59 · see citing works
Management of anemia in patients with congestive heart failure
Goodnough, L. T., Colet, J. C., Leal-Noval, S. R., Ozawa, S. J., Takere, J., Henry, D. H., Javidroozi, M., Hohmuth, B., Bisbe, E., Gross, I., et al. (2016) · American Journal of Hematology · doi:10.1002/ajh.24595 · Cited by 58 · see citing works
Bile salts induce long polar fimbriae expression favouring Crohn's disease‐associated adherent‐invasive Escherichia coli interaction with Peyer's patches
Chassaing, B., Etienne‐Mesmin, L., Bonnet, R., & Darfeuille–Michaud, A. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2012.02824.x · Cited by 57 · see citing works
Multiplex Immunoassay of Lower Genital Tract Mucosal Fluid from Women Attending an Urban STD Clinic Shows Broadly Increased IL1ß and Lactoferrin
Spear, G. T., Kendrick, S. R., Chen, H. Y., Thomas, T. T., Bahk, M., BALDERAS, R. S., Ghosh, S. K., Weinberg, A., & LANDAY, A. L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019560 · Cited by 57 · see citing works
Enhanced antifungal activity of bovine lactoferrin-producing probiotic Lactobacillus casei in the murine model of vulvovaginal candidiasis
Liao, H., Liu, S., Wang, H., Su, H., & Liu, Z. (2019) · BMC Microbiology · doi:10.1186/s12866-018-1370-x · Cited by 55 · see citing works
The clinical use of inflammatory markers during pregnancy
Genç, M., & Ford, C. E. (2010) · Current Opinion in Obstetrics & Gynecology · doi:10.1097/gco.0b013e3283374ac8 · Cited by 54 · see citing works
Venous Thrombosis: Prevalence and Interaction of Risk Factors
Rosendaal, F. R. (1999) · Pathophysiology of Haemostasis and Thrombosis · doi:10.1159/000054106 · Cited by 52 · see citing works
Effects of lactoferrin on intestinal epithelial cell growth and differentiation: an in vivo and in vitro study
Blais, A., Fan, C., Voisin, T., Aattouri, N., Dubarry, M., Blachier, F., & Tomé, D. (2014) · BioMetals · doi:10.1007/s10534-014-9779-7 · Cited by 51 · see citing works

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Can Lactoferrin, a Natural Mammalian Milk Protein, Assist in the Battle against COVID-19?
Einerhand, A. W. C., Bouwman, C. A., Weiss, G. A., Wang, C., Ba, G., Fan, Q., He, B., & Smit, G. (2022) · Nutrients · doi:10.3390/nu14245274 · Cited by 18 · see citing works
Lactoferrin Induces Erythropoietin Synthesis and Rescues Cognitive Functions in the Offspring of Rats Subjected to Prenatal Hypoxia
Av, S., Dubrovskaya, N. M., Kostevich, V. A., Vasilev, D. S., Voynova, I. V., Zakharova, E. T., Runova, O. L., Semak, I. V., Будевич, А. И., Nalivaeva, N. N., et al. (2022) · Nutrients · doi:10.3390/nu14071399 · Cited by 16 · see citing works
Peroxiredoxin Asp f3 Is Essential for Aspergillus fumigatus To Overcome Iron Limitation during Infection
Brantl, V., Boysen, J. M., Yap, A., Golubtsov, E., Ruf, D., Heinekamp, T., Straßburger, M., Dichtl, K., Haas, H., Hillmann, F., et al. (2021) · mBio · doi:10.1128/mbio.00976-21 · Cited by 15 · see citing works
Pleiotropic effect of Lactoferrin in the prevention and treatment of COVID-19 infection: randomized clinical trial, in vitro and in silico preliminary evidencesPreprint
Campione, E., Lanna, C., Cosio, T., Rosa, L., Conte, M., Iacovelli, F., Romeo, A., Falconi, M., Vecchio, C. D., Franchin, E., et al. (2020) · bioRxiv · doi:10.1101/2020.08.11.244996 · Cited by 12 · see citing works
Bovine Lactoferrin Pre-Treatment Induces Intracellular Killing of AIEC LF82 and Reduces Bacteria-Induced DNA Damage in Differentiated Human Enterocytes
Lepanto, M. S., Rosa, L., Cutone, A., Scotti, M. J., Conte, A. L., Marazzato, M., Zagaglia, C., Longhi, C., Berlutti, F., Musci, G., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225666 · Cited by 14 · see citing works
Colostrum and Lactoferrin Protect against Side Effects of Therapy with Antibiotics, Anti-inflammatory Drugs and Steroids, and Psychophysical Stress: A Comprehensive Review
Artym, J., & Zimecki, M. (2023) · Biomedicines · doi:10.3390/biomedicines11041015 · Cited by 14 · see citing works
Molecular mimicry of the receptor-binding domain of the SARS-CoV-2 spike protein: from the interaction of spike-specific antibodies with transferrin and lactoferrin to the antiviral effects of human recombinant lactoferrin
Sokolov, A., Isakova-Sivak, I., Mezhenskaya, D. A., Kostevich, V., Gorbunov, N., Elizarova, A., Matyushenko, V., Berson, Y., Grudinina, N., Kolmakov, N. N., et al. (2022) · Biometals · doi:10.1007/s10534-022-00458-6 · Cited by 11 · see citing works
Recent progress in stimulus-responsive hydrogel-based sensors for inflammation-associated diagnosis and surveillance
Chen, X., Song, W., Zhang, H., Xu, Y., Yi, B., & Zhou, Q. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.159756 · Cited by 13 · see citing works
Tear nanoDSF Denaturation Profile Is Predictive of Glaucoma
Baksheeva, V. E., Tiulina, V. V., Иомдина, Е. Н., Petrov, S. Y., Filippova, O. M., Kushnarevich, N. Y., Suleiman, E. A., Eyraud, R., Devred, F., Serebryakova, M. V., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087132 · Cited by 13 · see citing works
Human Mesenchymal Stem Cell Response to Lactoferrin-based Composite Coatings
Icriverzi, M., Bonciu, A. F., Rusen, L., Sima, L. E., Brajnicov, S., Cîmpean, A., Evans, R. W., Dinca, V. C., & Roșeanu, A. (2019) · Materials · doi:10.3390/ma12203414 · Cited by 13 · see citing works
Lactoferrin in health and disease: A review of its bioavailability and evidence-based benefits across study models
Ng, Z. J., Daud, M. F. A. B. M., Lian, K. O. B., Migeemanathan, S., Shin, G. K., Shunmugham, T. R., Hee, J. C. T., Wei, T. H., Ling, K. Y., Sa’aid, N., et al. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105024 · Cited by 12 · see citing works
Stealthy microbes: How Neisseria gonorrhoeae hijacks bulwarked iron during infection
Stoudenmire, J. L., Greenawalt, A. N., & Cornelissen, C. N. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1017348 · Cited by 12 · see citing works
Nbr1-regulated autophagy in Lactoferrin-induced osteoblastic differentiation
Zhang, Y., Zhang, Z.-N., Li, N., Zhao, L.-J., Xue, Y., Wu, H., & Hou, J. (2020) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2020.1737505 · Cited by 12 · see citing works
The role of nutrition on the treatment of Covid 19
Younes, S. (2024) · Human Nutrition & Metabolism · doi:10.1016/j.hnm.2024.200255 · Cited by 10 · see citing works
Association of salivary lactoferrin, Porphyromoras gingivalis and stress hormone levels in patients with periodontitis: a pilot study
Antequera, D., Buetas, E., García‐Esteban, S., Romualdi, D., Carrero, L., Municio, C., Mira, Á., & Carro, E. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1681095 · Cited by 13 · see citing works
Lactoferrin Can Attenuate SARS-CoV-2: An Analysis of Evidential Relations
Shafqat, F., Rehman, S. U., & Niaz, K. (2022) · Biomedical Research and Therapy · doi:10.15419/bmrat.v9i2.727 · Cited by 10 · see citing works
Lactoferrin reduces mycobacterial M1-type inflammation induced with trehalose 6,6′-dimycolate and facilitates the entry of fluoroquinolone into granulomas
Nguyen, T. K. T., Niaz, Z., d’Aigle, J., Hwang, S., Kruzel, M. L., & Actor, J. K. (2020) · Biochemistry and Cell Biology · doi:10.1139/bcb-2020-0057 · Cited by 10 · see citing works
Modulation of TDM-induced granuloma pathology by human lactoferrin: a persistent effect in mice
Actor, J. K., Nguyen, T. K. T., Wasik-Smietana, A., & Kruzel, M. L. (2022) · BioMetals · doi:10.1007/s10534-022-00434-0 · Cited by 10 · see citing works
Lactoferrin is a dynamic protein in human melioidosis and is a TLR4-dependent driver of TNF-α release in Burkholderia thailandensis infection in vitro
Wright, S. W., Lovelace-Macon, L., Ducken, D. R., Tandhavanant, S., Teparrukkul, P., Hantrakun, V., Limmathurotsakul, D., Chantratita, N., & West, T. E. (2020) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0008495 · Cited by 9 · see citing works
Molecular modeling of lactoferrin for food and nutraceutical applications: insights from in silico techniques
Darmawan, K. K., Karagiannis, T. C., Hughes, J. G., Small, D. M., & Hung, A. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2067824 · Cited by 9 · see citing works
Design of Peptide Ligand for Lactoferrin and Study of Its Binding Specificity
Zimina, T. M., Sitkov, N. O., Karasev, V., Skorik, Y. А., Kolobov, A. A., Kolobov, A. A., Bunenkov, N. S., & Luchinin, V. V. (2023) · Chemosensors · doi:10.3390/chemosensors11030162 · Cited by 8 · see citing works
Role of the protein kinase A signaling pathway and identification of mediators in the cardioprotective effects of enteral lactoferrin for ischemia-reperfusion injury in an isolated rat heart model
Omiya, K., Nakadate, Y., Sato, H., Oguchi, T., Matsuoka, T., Kawakami, A., Schricker, T., & Matsukawa, T. (2023) · Nutrition · doi:10.1016/j.nut.2023.112088 · Cited by 8 · see citing works
Specific Changes of Erythroid Regulators and Hepcidin in Patients Infected by SARS-COV-2
Delaye, J.-B., Alarcan, H., Vallet, N., Veyrat‐Durebex, C., Bernard, L., Hérault, O., Ropert, M., Marlet, J., Gyan, E., Andres, C. R., et al. (2022) · Journal of Investigative Medicine · doi:10.1136/jim-2021-002270 · Cited by 8 · see citing works
Lactoferrin as Immune-Enhancement Strategy for SARS-CoV-2 Infection in Alzheimer’s Disease Patients
Bartolomé, F. B., Rosa, L., Valenti, P., Lopera, F. J., Hernández‐Gallego, J., Cantero, J. L., Orive, G., & Carro, E. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.878201 · Cited by 8 · see citing works
Interaction of Pelargonium sidoides Compounds with Lactoferrin and SARS-CoV-2: Insights from Molecular Simulations
Iacovelli, F., Costanza, G., Romeo, A., Cosio, T., Lanna, C., Bagnulo, A., Maio, U. D., Sbardella, A., Gaziano, R., Grelli, S., et al. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph19095254 · Cited by 8 · see citing works
Effect of bovine lactoferrin on recurrent urinary tract infections: in vitro and in vivo evidences
Conte, A. L., Longhi, C., Conte, M. P., Costanzo, A. M., Paesano, R., Santangeli, S., Venditto, F., Tripepi, G. L., Naldi, E., Pollio, G., et al. (2022) · BioMetals · doi:10.1007/s10534-022-00409-1 · Cited by 8 · see citing works
The potential of lactoferrin: a call for future research in poultry nutrition
Saeed, M., Hussain, N., Ahmed, S., Khan, R. U., Andoh, V., Husain, S., & Huayou, C. (2023) · World s Poultry Science Journal · doi:10.1080/00439339.2023.2239764 · Cited by 8 · see citing works
Cardioprotective effects of enteral vs. parenteral lactoferrin administration on myocardial ischemia-reperfusion injury in a rat model of stunned myocardium
Omiya, K., Nakadate, Y., Oguchi, T., Sato, T., Matsuoka, T., Abe, M., Kawakami, A., Matsukawa, T., & Sato, H. (2022) · BMC Pharmacology and Toxicology · doi:10.1186/s40360-022-00619-w · Cited by 7 · see citing works
Hen Egg White Bovine Colostrum Supplement Reduces Symptoms of mild/moderate COVID-19: a Randomized Control Trial
Mann, J. K., Reddy, T., van der Stok, M., Ngubane, A., Mulaudzi, T., Mchunu, N. N., Nevhungoni, P., Manickchund, N., Manickchund, P., Cairns, C., et al. (2023) · Future Science OA · doi:10.2144/fsoa-2023-0024 · Cited by 7 · see citing works
Use of Lactoferrin Supplement as an Efficient Antioxidant to Ameliorate the Effects of Mercury-induced Oxidative Stress in Male Wistar Rats
Zharani, M. A., Almuqri, E. A., Mubarak, M., Aljarba, N. H., Rudayni, H. A., Yaseen, K. N., Alkahtani, S. H., Nasr, F. A., Al-Doaiss, A. A., & AlEissa, M. S. (2024) · Biomedical and Biotechnology Research Journal (BBRJ) · doi:10.4103/bbrj.bbrj_262_23 · Cited by 7 · see citing works
Lactoferrin levels in cervical fluid from in vitro fertilization (IVF) patients — correlation with IVF parameters
Massa, E., Pelusa, F., Celso, A. L., Madariaga, M. J., Filocco, L., Morente, C., & Ghersevich, S. A. (2020) · Biochemistry and Cell Biology · doi:10.1139/bcb-2020-0098 · Cited by 7 · see citing works
Urinary Reference Values and First Insight into the Urinary Proteome of Captive Giraffes
Fasoli, S., Andreani, G., Dondi, F., Ferlizza, E., Bellei, E., & Isani, G. (2020) · Animals · doi:10.3390/ani10091696 · Cited by 7 · see citing works
Biomaterial-Based Delivery Systems for Chemotherapeutics
Gugulothu, D. B., Dhawan, D., Sachdeva, A., Deepali, & Chauhan, M. K. (2023) · Biological and medical physics, biomedical engineering · doi:10.1007/978-981-19-9786-0_4 · Cited by 7 · see citing works
Identification of iron metabolism-related genes as diagnostic signatures in sepsis by blood transcriptomic analysis
Li, H., Wang, X., Yang, Q., Cheng, L., & Zeng, H. (2023) · Open Life Sciences · doi:10.1515/biol-2022-0549 · Cited by 8 · see citing works
Bovine lactoferrin inhibits inflammatory response and apoptosis in lipopolysaccharide-induced acute lung injury by targeting the PPAR-γ pathway
Li, Y., Li, J., Dong, Y., Wang, C., & Cai, Z. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09436-2 · Cited by 6 · see citing works
Effectiveness of managing suspected metastasis using plasma D-dimer testing in gastric cancer patients.
Zhang, X., Wang, X., Li, W., Dang, C., & Diao, D. (2022) · PubMed Central · Cited by 6 · see citing works
Evaluating Prophylactic Effect of Bovine Colostrum on Intestinal Barrier Function in Zonulin Transgenic Mice: A Transcriptomic Study
Asbjornsdottir, B., Sigurðsson, S., Miranda-Ribera, A., Fiorentino, M. R., Konno, T., Lan, J., Gudmundsson, L. S., Gottfreðsson, M., Lauth, B., Birgisdóttir, B. E., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914730 · Cited by 6 · see citing works
Lactoferrin improves symptoms of dextran sulfate sodium-induced colitis in mice through modulation of cellular senescence
Sienkiewicz, M., Zielińska, M., Jacenik, D., Machelak, W., Owczarek, K., & Fichna, J. (2023) · Nutrition Research · doi:10.1016/j.nutres.2023.10.001 · Cited by 6 · see citing works
A Clinical Study to Evaluate the Anti-inflammatory Effect of Lactoferrin + Disodium Guanosine Monophosphate Therapy in the Patients with Chronic Kidney Disease
Yadav, R. K., Sangha, S. S., Yadav, S., Sharma, P., Shah, H., & Bhowmik, D. M. (2025) · Journal of the Association of Physicians of India · doi:10.59556/japi.73.0757 · Cited by 6 · see citing works
Pathogenic and Protective Roles of Neutrophils in Chlamydia trachomatis Infection
Wilton, Z. E. R., Jamus, A. N., Core, S. B., & Frietze, K. M. (2025) · Pathogens · doi:10.3390/pathogens14020112 · Cited by 6 · see citing works
An Overview on Immunity Booster Foods in Coronavirus Disease (COVID-19)
Sahiba, N., Sethiya, A., Agarwal, D. K., & Agarwal, S. (2022) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207325666220629161828 · Cited by 6 · see citing works
Bovine lactoferrin suppresses inflammatory cytokine expression in endometrial stromal cells in chronic endometritis
Nakamura, A., Kimura, F., Tsuji, S., Hanada, T., Takebayashi, A., Takahashi, A., Kitazawa, J., Morimune, A., Amano, T., Kushima, R., et al. (2022) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2022.103761 · Cited by 5 · see citing works
Managing children with frequent respiratory infections and associated wheezing: a preliminary randomized study with a new multicomponent nasal spray
Tosca, M. A., Varricchio, A., Schiavetti, I., Naso, M., Damiani, V., & Ciprandi, G. (2024) · Allergologia et Immunopathologia · doi:10.15586/aei.v52i3.1040 · Cited by 5 · see citing works
Colostrum-Induced Temporary Changes in the Expression of Proteins Regulating the Epithelial Barrier Function in the Intestine
Rzeszotek, S., Trybek, G., Tarnowski, M., Serwin, K., Jaroń, A., Schneider, G., Kolasa, A., & Wiszniewska, B. (2022) · Foods · doi:10.3390/foods11050685 · Cited by 5 · see citing works
Editorial to Special Issue—Anti-Inflammatory Activity of Natural Products
Miguel, M. G. (2020) · Molecules · doi:10.3390/molecules25081926 · Cited by 5 · see citing works

Lactoferrin against inflammatory and iron disorders in different infection models
Rosa, L. (2021) · IRIS Research product catalog (Sapienza University of Rome)
Lactoferrin: A Multifunctional Glycoprotein Involved in the Modulation of the Inflammatory Process
Baveye, S., Elass, E., Mazurier, J., Spik, G., & Legrand, D. (1999) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1999.049 · Cited by 340 · see citing works
Lactoferrin: a natural Glycoprotein involved in iron and inflammatory homeostasis
Rosa, L., Cutone, A., Lepanto, M., Paesano, R., & Valenti, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091985 · Cited by 376 · see citing works
Lactoferrin Efficiently Counteracts the Inflammation-Induced Changes of the Iron Homeostasis System in Macrophages
Cutone, A., Rosa, L., Lepanto, M. S., Scotti, M. J., Berlutti, F., di Patti, M. C. B., Musci, G., & Valenti, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00705 · Cited by 99 · see citing works
Lactoferrin: Balancing Ups and Downs of Inflammation Due to Microbial Infections
Drago-Serrano, M., Campos-Rodríguez, R., Carrero, J., & De la Garza, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030501 · Cited by 151 · see citing works

Authors: Lepanto, M. S., Rosa, L., Paesano, R., Valenti, P., & Cutone, A.
Affiliations: Sapienza University of Rome (IT)
Microbo S.R.L., 00153 Rome, Italy
University of Molise (IT)
Corresponding author: Cutone, Antimo
ORCID: Lepanto, Maria Stefania
Rosa, Luigi
Paesano, Rosalba
Valenti, Piera
Cutone, Antimo
Venue: Molecules
Publisher: MDPI AG
Published: 2019-04-03
Volume: 24
Issue: 7
Pages: 1323
ISSN: 1420-3049 (ISSN-L)
DOI: 10.3390/molecules24071323
PMC: PMC6480387
OpenAlex: W2935579023
Cited by: 147
References: 240
Citations by year: 2026: 6 · 2025: 17 · 2024: 16 · 2023: 23 · 2022: 31 · 2021: 24 · 2020: 23 · 2019: 6 · 2018: 1
FWCI: 3.35
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Molecules (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
IRIS Research product catalog (Sapienza University of Rome) (submittedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Archivio Istituzionale della Ricerca - Università degli Studi del Molise (submittedVersion)
Funders: Sapienza Università di Roma
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Health Sciences › Nursing › Nutrition and Dietetics › Infant Nutrition and Health
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: lactoferrin, sterile inflammation, septic inflammation, interleukin-6, iron homeostasis, anti-inflammatory activity, anemia of chronic disease, preterm birth, Alzheimer's disease, type 2 diabetes, Chlamydia trachomatis infection, cystic fibrosis, inflammatory bowel disease, bacterial adhesion, iron saturation
MeSH terms: Anemia, Animals, Anti-Infective Agents, Anti-Inflammatory Agents, Humans, Inflammation, Iron, Lactoferrin, Biomarkers, Sepsis

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Lactoferrin in aseptic and septic inflammation

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