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- W2023152124 abstract "α 5 β 1 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 [ 35 S]sulfate metabolic labeling of the cells, enzymatic degradation, immunoprecipitation reaction with monoclonal antibody, fluorescence microscopy, and flow cytometry. The α 5 β 1 integrin heterodimer is a hybrid proteoglycan containing both chondroitin and heparan sulfate chains. Xyloside inhibition of sulfate incorporation into α 5 β 1 integrin also supports that integrin is a proteoglycan. Also, cells grown with xyloside adhered on fibronectin with no alteration in α 5 β 1 integrin expression. However, haptotactic motility on fibronectin declined in cells grown with xyloside or chlorate as compared with controls. Thus, α 5 β 1 integrin is a proteoglycan and the glycosaminoglycan chains of the integrin influence cell motility on fibronectin. Similar glycosylation of α 5 β 1 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 5 β 1 integrin are involved in cellular migration on fibronectin." @default.
- W2023152124 created "2016-06-24" @default.
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- W2023152124 date "2009-08-01" @default.
- W2023152124 modified "2023-10-16" @default.
- W2023152124 title "Glycosaminoglycan chains from α<sub>5</sub>β<sub>1</sub>integrin are involved in fibronectin-dependent cell migrationDedicated to the memory of Professor Carl P. Dietrich." @default.
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- W2023152124 doi "https://doi.org/10.1139/o09-047" @default.
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