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Review

Studying Lactoferrin N-Glycosylation

1
Department of Molecular Biology and Genetics, Canakkale Onsekiz Mart University, 17100 Canakkale, Turkey
2
Department of Food Science and Technology, University of California, One Shields Avenue, Davis, CA 95616, USA
3
Foods for Health Institute, University of California, One Shields Avenue, Davis, CA 95616, USA
*
Author to whom correspondence should be addressed.
Current address: Prolacta Bioscience®, 757 Baldwin Park Blvd, City of Industry, CA 91746, USA.
Academic Editors: David Arráez-Román and Vito Verardo
Int. J. Mol. Sci. 2017, 18(4), 870; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18040870
Received: 5 February 2017 / Revised: 10 April 2017 / Accepted: 12 April 2017 / Published: 20 April 2017
(This article belongs to the Special Issue Lipidomics and Glycomics: New Advances in Food Science and Nutrition)
Lactoferrin 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. View Full-Text
Keywords: lactoferrin; N-glycans; deglycosylating enzymes; mass spectrophotometry; bioinfomatic libraries; structure-activity studies lactoferrin; N-glycans; deglycosylating enzymes; mass spectrophotometry; bioinfomatic libraries; structure-activity studies
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MDPI and ACS Style

Karav, S.; German, J.B.; Rouquié, C.; Le Parc, A.; Barile, D. Studying Lactoferrin N-Glycosylation. Int. J. Mol. Sci. 2017, 18, 870. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18040870

AMA Style

Karav S, German JB, Rouquié C, Le Parc A, Barile D. Studying Lactoferrin N-Glycosylation. International Journal of Molecular Sciences. 2017; 18(4):870. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18040870

Chicago/Turabian Style

Karav, Sercan, J. B. German, Camille Rouquié, Annabelle Le Parc, and Daniela Barile. 2017. "Studying Lactoferrin N-Glycosylation" International Journal of Molecular Sciences 18, no. 4: 870. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18040870

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