Studying Lactoferrin N-Glycosylation

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dc.authoridKARAV, SERCAN/0000-0003-4056-1673
dc.authoridRouquie, Camille/0000-0002-8290-7778
dc.authoridbarile, daniela/0000-0002-3889-1596
dc.contributor.authorKarav, Sercan
dc.contributor.authorGerman, J. Bruce
dc.contributor.authorRouquie, Camille
dc.contributor.authorLe Parc, Annabelle
dc.contributor.authorBarile, Daniela
dc.date.accessioned2025-01-27T20:54:21Z
dc.date.available2025-01-27T20:54:21Z
dc.date.issued2017
dc.departmentÇanakkale Onsekiz Mart Üniversitesi
dc.description.abstractLactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and differentiation, and as an anti-bacterial, anti-viral, and anti-parasitic protein. These functions differ among lactoferrin homologs in mammals. Although considerable attention has been given to the many functions of lactoferrin, its primary nutritional contribution is presumed to be related to its iron-binding characteristics, whereas the role of glycosylation has been neglected. Given the critical role of glycan binding in many biological processes, the glycan moieties in lactoferrin are likely to contribute significantly to the biological roles of lactoferrin. Despite the high amino acid sequence homology in different lactoferrins (up to 99%), each exhibits a unique glycosylation pattern that may be responsible for heterogeneity of the biological properties of lactoferrins. An important task for the production of biotherapeutics and medical foods containing bioactive glycoproteins is the assessment of the contributions of individual glycans to the observed bioactivities. This review examines how the study of lactoferrin glycosylation patterns can increase our understanding of lactoferrin functionality.
dc.description.sponsorshipNational Institutes of Health, USDA NIFA Hatch project [R01AT007079, R01AT008759, 232719]
dc.description.sponsorshipThe authors thank Cora J. Dillard for editing this manuscript. This research was supported in part by funding from the National Institutes of Health awards R01AT007079 and R01AT008759, USDA NIFA Hatch project 232719.
dc.identifier.doi10.3390/ijms18040870
dc.identifier.issn1422-0067
dc.identifier.issue4
dc.identifier.pmid28425960
dc.identifier.scopus2-s2.0-85018525914
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.3390/ijms18040870
dc.identifier.urihttps://hdl.handle.net/20.500.12428/26052
dc.identifier.volume18
dc.identifier.wosWOS:000402639400191
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherMdpi
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.relation.publicationcategoryinfo:eu-repo/semantics/openAccess
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WoS_20250125
dc.subjectlactoferrin
dc.subjectN-glycans
dc.subjectdeglycosylating enzymes
dc.subjectmass spectrophotometry
dc.subjectbioinfomatic libraries
dc.subjectstructure-activity studies
dc.titleStudying Lactoferrin N-Glycosylation
dc.typeReview Article

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