The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Lactoferrin and host defence: an overview of its immuno-modulating and anti-inflammatory properties
Abstract
Lactoferrin is a member of the transferrin family of iron-binding glycoproteins that is abundantly expressed and secreted from glandular epithelial cells. In secretions, such as milk and fluids of the intestinal tract, lactoferrin is an important component of the first line of host defence. During the inflammatory process, lactoferrin, a prominent component of the secondary granules of neutrophils (PMNs), is released in infected tissues and in blood and then it is rapidly cleared by the liver. In addition to the antimicrobial properties of lactoferrin, a set of studies has focused on its ability to modulate the inflammatory process and the overall immune response. Though many in vitro and in vivo studies report clear regulation of the immune response and protective effect against infection and septic shock by lactoferrin, elucidation of all the cellular and molecular mechanisms of action is far from being achieved. At the cellular level, lactoferrin modulates the migration, maturation and function of immune cells. At the molecular level and in addition to iron binding, interactions of lactoferrin with a plethora of compounds, either soluble or membrane molecules, account for its modulatory properties. This paper reviews our current understanding of the cellular and molecular mechanisms that explain the regulatory properties of lactoferrin in host defence.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“Neutrophils further limit nutrient metal availability by releasing lactoferrin to sequester iron (Legrand et al., 2004)”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Legrand et al., 2004
In the citing paper
“Both target free Fe3+, 122 and can therefore reduce its availability.”
From The battle for iron in enteric infections (2020) · cites this paper as [122]
Citations
Cites
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
Lactoferrin is a lipid A-binding protein
Appelmelk, B. J., An, Y. Q., Geerts, M., Thijs, B. G., de Boer, H. A., MacLaren, D. M., Graaff, J., & Nuijens, J. H. (1994) · Infection and Immunity · doi:10.1128/iai.62.6.2628-2632.1994 · Cited by 362
Lactoferrin down-regulates the LPS-induced cytokine production in monocytic cells via NF-κB
Håversen, L., Ohlsson, B. G., Hahn‐Zoric, M., Hanson, L. Å., & Mattsby‐Baltzer, I. (2002) · Cellular Immunology · doi:10.1016/s0008-8749(03)00006-6 · Cited by 338
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 266
Elass, E., Roșeanu, A., Legrand, D., Trif, M., Salmon, V., Motaş, C., Montreuil, J., & Spik, G. (1995) · Biochemical Journal · doi:10.1042/bj3120839 · Cited by 250
Self-citationLactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo.
Machnicki, M., Zimecki, M., & Zagulski, T. (1993) · Europe PMC (PubMed Central) · Cited by 232
Mann, D. M., Romm, E., & Migliorini, M. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31566-1 · Cited by 227
Elass, E., Legrand, D., Salmon, V., Roșeanu, A., Trif, M., Tobias, P. S., Mazurier, J., & Spik, G. (1998) · Infection and Immunity · doi:10.1128/iai.66.2.486-491.1998 · Cited by 195
Self-citationvan Hooijdonk, A. C. M., Kussendrager, K. D., & Steijns, J. M. (2000) · British Journal Of Nutrition · doi:10.1017/s000711450000235x · Cited by 188
Mazurier, J., Legrand, D., Hu, W., Montreuil, J., & Spik, G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14578.x · Cited by 163
Self-citation
Cited by
Sorted by citations
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
The Impact of Dietary Transition Metals on Host-Bacterial Interactions
Lopez, C. A., & Skaar, E. P. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.05.008 · Cited by 190
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
He, C.-S., Tsai, M.-L., Ko, M.-H., Chang, C.-K., & Fang, S.-H. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1574-8 · Cited by 67
The battle for iron in enteric infections
Sousa Gerós, A., Simmons, A., Drakesmith, H., Aulicino, A., & Frost, J. N. (2020) · Immunology · doi:10.1111/imm.13236 · Cited by 58
Metadata
- Authors
- Legrand, D., Elass, E., Pierce, A., & Mazurier, J.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Legrand, Dominique
- Venue
- Biometals
- Published
- 2004-06
- Volume
- 17
- Issue
- 3
- Pages
- 225-229
- ISSN
- 0966-0844 (ISSN-L)
- 1572-8773
- OpenAlex
- W1996525939
- Cited by
- 149
- References
- 57
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 4 · 2023: 2 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 7 · 2018: 5 · 2017: 12 · 2016: 1 · 2015: 4 · 2014: 11 · 2013: 5 · 2012: 11
- FWCI
- 1.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- BioMetals (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- lactoferrin, host defense, immunomodulation, anti-inflammatory activity, iron-binding glycoprotein, antimicrobial activity, leukocyte migration, immune cell maturation, septic shock, innate immunity
- MeSH terms
- Animals, Anti-Infective Agents, Anti-Inflammatory Agents, Humans, Immune System, Immunologic Factors, Lactoferrin
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Lactoferrin and host defence: an overview of its immuno-modulating and anti-inflammatory properties. https://app.cochat.ai/papers/10.1023/b:biom.0000027696.48707.42
- The paper
- Legrand, D., Elass, E., Pierce, A., & Mazurier, J. (2004). Lactoferrin and host defence: an overview of its immuno-modulating and anti-inflammatory properties. Biometals. https://doi.org/10.1023/b%3Abiom.0000027696.48707.42
