Chondroitin sulfate-cell membrane effectors as regulators of growth factor-mediated vascular and cancer cell migration |
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Authors: | Evangelia Pantazaka Evangelia Papadimitriou |
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Affiliation: | Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras GR26504, Greece |
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Abstract: | BackgroundGlycosylation is a multi-step post-translational enzymatic process which enhances the functional diversity of secreted or membrane proteins and is implicated in physiological and pathological conditions. Chondroitin sulfate (CS) chains are glycosaminoglycan chains, consisting of disaccharide units of glucuronic acid and N-acetylgalactosamine, attached to proteins as part of proteoglycans.Scope of ReviewThe existing knowledge on glycosylation by CS (CS glycanation) of cell membrane proteins and receptors, such as syndecans, chondroitin sulfate proteoglycan 4, betaglycan, neuropilin-1, integrins and receptor protein tyrosine phosphatase β/ζ, is summarized and the importance of CS glycanation in growth factor-induced migration, angiogenesis and tumor growth and invasion is described.Major ConclusionsIdentification of glycosylation so far used to be a means of further characterizing and categorizing proteins and receptors. Although there is a significant amount of information regarding the interaction of growth factors with CS chains, very little information exists on the core proteins involved. It is now evident that there is more than meets the eye regarding the addition of glycans.General SignificanceFuture effort should focus on characterizing CS glycanation of membrane proteins and receptors of interest in an attempt to elucidate its contribution in fine-tuning growth factor-induced signaling. This article is part of a Special Issue entitled Matrix-mediated cell behaviour and properties. |
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Keywords: | Angiogenesis Cell migration Glycosaminoglycan Glycosylation Proteoglycan Receptor protein tyrosine phosphatase β/ζ |
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