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 |
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Rok vydání: | 1999 |
Předmět: |
Integrins
Proteases Invadopodium Integrin Cell Fluorescent Antibody Technique Biochemistry Fibroblast activation protein alpha Endopeptidases Biomarkers Tumor Tumor Cells Cultured medicine Animals Melanoma Molecular Biology biology Serine Endopeptidases Integrin alpha3beta1 Membrane Proteins Cell Biology Precipitin Tests Neoplasm Proteins Cell biology medicine.anatomical_structure Microscopy Fluorescence Membrane protein Gelatinases Antigens Surface Invadopodia biology.protein Collagen Type I collagen |
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 |
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