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NG2 proteoglycan mediates β1 integrin‐independent cell adhesion and spreading on collagen VI

NG2 proteoglycan mediates β1 integrin‐independent cell adhesion and spreading on collagen VI Collagens V and VI have been previously identified as specific extracellular matrix (ECM) ligands for the NG2 proteoglycan. In order to study the functional consequences of NG2/collagen interactions, we have utilized the GD25 cell line, which does not express the major collagen‐binding β1 integrin heterodimers. Use of these cells has allowed us to study β1 integrin‐independent phenomena that are mediated by binding of NG2 to collagens V and VI. Heterologous expression of NG2 in the GD25 line endows these cells with the capability of attaching to surfaces coated with collagens V and VI. The specificity of this effect is emphasized by the failure of NG2‐positive GD25 cells to attach to other collagens or to laminin‐1. More importantly, NG2‐positive GD25 cells spread extensively on collagen VI. β1 integrin‐independent extension of ruffling lamellipodia demonstrates that engagement of NG2 by the collagen VI substratum triggers signaling events that lead to rearrangement of the actin cytoskeleton. In contrast, even though collagens V and VI each bind to the central segment of the NG2 ectodomain, collagen V engagement of NG2 does not trigger cell spreading. The distinct morphological consequences of NG2/collagen VI and NG2/collagen V interaction indicate that closely‐related ECM ligands for NG2 differ in their ability to initiate transmembrane signaling via engagement of the proteoglycan. J. Cell. Biochem. 86: 726–736, 2002. © 2002 Wiley‐Liss, Inc. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cellular Biochemistry Wiley

NG2 proteoglycan mediates β1 integrin‐independent cell adhesion and spreading on collagen VI

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References (68)

Publisher
Wiley
Copyright
Copyright © 2002 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0730-2312
eISSN
1097-4644
DOI
10.1002/jcb.10268
pmid
12210739
Publisher site
See Article on Publisher Site

Abstract

Collagens V and VI have been previously identified as specific extracellular matrix (ECM) ligands for the NG2 proteoglycan. In order to study the functional consequences of NG2/collagen interactions, we have utilized the GD25 cell line, which does not express the major collagen‐binding β1 integrin heterodimers. Use of these cells has allowed us to study β1 integrin‐independent phenomena that are mediated by binding of NG2 to collagens V and VI. Heterologous expression of NG2 in the GD25 line endows these cells with the capability of attaching to surfaces coated with collagens V and VI. The specificity of this effect is emphasized by the failure of NG2‐positive GD25 cells to attach to other collagens or to laminin‐1. More importantly, NG2‐positive GD25 cells spread extensively on collagen VI. β1 integrin‐independent extension of ruffling lamellipodia demonstrates that engagement of NG2 by the collagen VI substratum triggers signaling events that lead to rearrangement of the actin cytoskeleton. In contrast, even though collagens V and VI each bind to the central segment of the NG2 ectodomain, collagen V engagement of NG2 does not trigger cell spreading. The distinct morphological consequences of NG2/collagen VI and NG2/collagen V interaction indicate that closely‐related ECM ligands for NG2 differ in their ability to initiate transmembrane signaling via engagement of the proteoglycan. J. Cell. Biochem. 86: 726–736, 2002. © 2002 Wiley‐Liss, Inc.

Journal

Journal of Cellular Biochemistry – Wiley

Published: Jan 1, 2002

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