A Novel Protease-docking Function of Integrin at Invadopodia

Autor: Steven K. Akiyama, Linda Howard, Giulio Ghersi, Qing-Xiang Amy Sang, Hirokazu Nakahara, Wen-Tien Chen, Mayra L. Piñeiro-Sánchez, Yunyun Yeh, Susette C. Mueller
Rok vydání: 1999
Předmět:
Zdroj: Journal of Biological Chemistry. 274:24947-24952
ISSN: 0021-9258
DOI: 10.1074/jbc.274.35.24947
Popis: Invadopodia are membrane extensions of aggressive tumor cells that function in the activation of membrane-bound proteases occurring during tumor cell invasion. We explore a novel and provocative activity of integrins in docking proteases to sites of invasion, termed invadopodia. In the absence of collagen, alpha(3)beta(1) integrin and the gelatinolytic enzyme, seprase, exist as nonassociating membrane proteins. Type I collagen substratum induces the association of alpha(3)beta(1) integrin with seprase as a complex on invadopodia. The results show that alpha(3)beta(1) integrin is a docking protein for seprase to form functional invadopodia. In addition, alpha(5)beta(1) integrin may participate in the adhesion process necessary for invadopodial formation. Thus, alpha(3)beta(1) and alpha(5)beta(1) integrins play major organizational roles in the adhesion and formation of invadopodia, promoting invasive cell behavior.
Databáze: OpenAIRE