Open AccessThe N-glycans of lactoferrin: more than just a sweet decoration
Author(s) -
Kristina Zlatina,
Sebastian P. Galuska
Publication year - 2021
Publication title -
biochemistry and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.843
H-Index - 91
eISSN - 1208-6002
pISSN - 0829-8211
DOI - 10.1139/bcb-2020-0106
Subject(s) - lactoferrin , glycosylation , glycoprotein , glycan , golgi apparatus , endoplasmic reticulum , biochemistry , biology , microbiology and biotechnology , chemistry
Nearly all extracellular proteins undergo post-translational modification with sugar chains during their transit through the endoplasmic reticulum and the Golgi apparatus. These “sweet” modifications not only influence the activity of its carrier protein, but they themselves often have bioactivity, independent of the carrier function. Lactoferrin belongs to the group of glycoproteins and is modified with several different N-glycans. This minireview summarizes several studies dealing with the diverse glycosylation patterns of lactoferrin from different origins, and the potential impact of these post-translational modifications on the functionality of lactoferrin. A special emphasis is placed on the differences between human and bovine lactoferrin, because the latter form is often selected for the development of novel therapeutic approaches in humans. For this reason, the potential impact of the bovine-specific glycosylation patterns on the observed heterogeneous effects of lactoferrin in humans is discussed within this minireview.