𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

✍ Scribed by Emmanuelle Tillet; Blandine Gential; Robert Garrone; William B. Stallcup

Publisher
John Wiley and Sons
Year
2002
Tongue
English
Weight
251 KB
Volume
86
Category
Article
ISSN
0730-2312

No coin nor oath required. For personal study only.

✦ Synopsis

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 beta(1) integrin heterodimers. Use of these cells has allowed us to study beta(1) 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. beta(1) 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.

📜 SIMILAR VOLUMES

Activation of the α2β1 integrin-mediated
Activation of the α2β1 integrin-mediated malignant phenotype on type I collagen in pancreatic cancer cells by shifts in the concentrations of extracellular Mg2+ and Ca2+
✍ John J. Grzesiak; Michael Bouvet 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 French ⚖ 755 KB

## Abstract The authors have previously demonstrated that α~2~β~1~ integrin‐mediated pancreatic cancer cell adhesion to Type I collagen is Mg^2+^‐dependent, inhibited by Ca^2+^, and that this integrin, purified from cell lysates using Type I‐collagen‐sepharose in Mg^2+^, can be eluted with Ca^2+^.