Year: 2007
Type: article
Abstract: Integrins are cell surface transmembrane glycoproteins that function as adhesion receptors in cell-ECM interactions and link matrix proteins to the cytoskeleton. Integrins play an important role in cytoskeleton organization and in the transduction of intracellular signals, regulating various processes such as proliferation, differentiation, apoptosis, and cell migration. Although integrin-mediated adhesion is based on the binding of alpha and beta subunits to a defined peptide sequence, the strength of this binding is modulated by various factors including the status of glycosylation of integrin. Glycosylation reactions are catalyzed by the catalytic action of glycosyltransferases, such as N-acetylglucosaminyltransferase III, V and alpha1,6 fucosyltransferase, etc., which catalyze the formation of glycosidic bonds. In this talk we will briefly overview the N-glycan structures of integrins, such as alpha3beta1 and alpha5beta1, and their related functions arising from recent studies, which provide insight into some long-standing questions concerning N-glycosylation functions.
Source: YAKUGAKU ZASSHI
Author: Jianguo GU
Institution: Tohoku Medical and Pharmaceutical University
Language: English
Subfield: Immunology and Allergy
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
OpenAlex ID: W2879637183