Glycosaminoglycan chains from [alpha]^sub 5^[beta]^sub 1^ integrin are involved in fibronectin-dependent cell migration

• Published in: Biochemistry and cell biology Vol. 87; no. 4; p. 677
• Main Authors: Franco, Célia RC, Trindade, Edvaldo S, Rocha, Hugo AO, da Silveira, Rafael Bertoni, Paludo, Katia Sabrina, Chammas, Roger, Veiga, Silvio S, Nader, Helena B, Dietrich, Carl P
• Format: Journal Article
• Language: English
• Published: Ottawa Canadian Science Publishing NRC Research Press 01.08.2009
• Subjects: Biochemistry; Biosynthesis; Cell adhesion & migration; Chemical reactions; Fluorescence; Fluorescence microscopy; Glycosylation; Monoclonal antibodies; Sulfates
• ISSN: 0829-8211; 1208-6002

α...β... integrin from both wild-type CHO cells (CHO-K1) and deficient in proteoglycan biosynthesis (CHO-745) is post-translationally modified by glycosaminoglycan chains. We demonstrated this using [...]sulfate metabolic labeling of the cells, enzymatic degradation, immunoprecipitation reaction with monoclonal antibody, fluorescence microscopy, and flow cytometry. The α...β... integrin heterodimer is a hybrid proteoglycan containing both chondroitin and heparan sulfate chains. Xyloside inhibition of sulfate incorporation into α...β... integrin also supports that integrin is a proteoglycan. Also, cells grown with xyloside adhered on fibronectin with no alteration in α...β... integrin expression. However, haptotactic motility on fibronectin declined in cells grown with xyloside or chlorate as compared with controls. Thus, α...β... integrin is a proteoglycan and the glycosaminoglycan chains of the integrin influence cell motility on fibronectin. Similar glycosylation of α...β... integrin was observed in other normal and malignant cells, suggesting that this modification is conserved and important in the function of this integrin. Therefore, these glycosaminoglycan chains of α...β... integrin are involved in cellular migration on fibronectin. (ProQuest: ... denotes formulae/symbols omitted.)