MT1‐MMP on the cell surface causes focal degradation of gelatin films

FEBS Letters

Murphy, Gillian¹  Stanton, Heather¹  Hembry, Rosalind M³  Butler, Michael¹  Atkinson, Susan J¹  d'Ortho, Marie-Pia² 

[1] School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK;INSERM U296, Faculté de Médecine, 8 avenue du Général Sarrail, 94010 Créteil, France;Strangeways Research Laboratory, Worts' Causeway, Cambridge CB1 4RN, UK

关键词: Matrix metalloproteinase;    Membrane-type matrix metalloproteinase;    Gelatinase A;    Matrix degradation;    Confocal microscopy;    DMEM;    Dulbecco's modified Eagle's medium;    FBS;    foetal bovine serum;    FITC;    fluorescein isothiocyanate;    HIFFs;    human infant foreskin fibroblasts;    NSS;    normal sheep serum;    PBS;    phosphate buffered saline pH 7.4;    rt;    room temperature;    tPA;    tissue-type plasminogen activator;    TR;    Texas red;   

DOI  :  10.1016/S0014-5793(97)01555-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The membrane-type matrix metalloproteinases (MT-MMPs) are a subclass of the matrix metalloproteinase (MMP) family which uniquely possess a C-terminal transmembrane domain and are initiators of an activation cascade for progelatinase A (MMP-2). Recent studies have shown that they can also efficiently directly degrade a number of matrix macromolecules. We now show that cells expressing MT1-MMP on their cell surfaces cause subjacent proteolysis of a gelatin film and that this proteolysis is inhibited by TIMP-2 but not by TIMP-1. These data indicate that expression of MT1-MMP on the cell surface may lead to both progelatinase A activation and extracellular matrix degradation.

【 授权许可】

Unknown