Abstract
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.
Highlights
Lactoferrin is a highly glycosylated protein that was first isolated from bovine milk in 1939 by Sorensen and Sorensen [1], and later identified in human milk in 1960 by Johanson [2]
Lactoferrin— known as lactotransferrin—is comprised of 692 amino acids folded into two globular lobes that are connected by an α–helix
Expected that the diverse structures and functions of lactoferrin will remain a popular target for investigations, and that this research will reveal additional functions and health benefits in the near future
Summary
Lactoferrin is a highly glycosylated protein that was first isolated from bovine milk in 1939 by Sorensen and Sorensen [1], and later identified in human milk in 1960 by Johanson [2]. It has been identified in secretions from exocrine glands as well as in specific granules of neutrophils [3]. Lactoferrin is used to inhibit lipid oxidation due its iron-binding capacity, as iron-promoted lipid oxidation is responsible for rancidity, and decreases the shelf life of commercial products, including infant formula and skincare cosmetics [22]
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