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http://purl.uniprot.org/citations/11710594http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11710594http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11710594http://www.w3.org/2000/01/rdf-schema#comment"

Purpose

Integrins are transmembrane heterodimeric molecules that mediate cellular adhesion and are involved in different biological processes, such as tumor development and invasion of tumor cells. Matrixmetalloproteases (MMP) are a family of secreted or membrane proteins capable of digesting extracellular matrix. It has been shown that MMP-2 binds to alphavbeta3 integrin. Recent evidence suggests that a complex of membrane-type MMP (MT1-MMP) and tissue inhibitor of metalloptroteinase-2 (TIMP-2) participate in the activation of alphavbeta3-associated MMP-2. We investigated whether alphavbeta3 and MMP-2 are associated on the membranes of a human cell line, SiHa, and the possible involvement of MT1-MMP and TIMP-2 in the modulation of MMP-2 activity.

Methods

Immunoprecipitation of SiHa membrane extracts with monoclonal antibodies against alphav or MMP-2, and western blots of immunoprecipitates and serum-free conditioned media were performed. TIMP-2 in conditioned medium and MT1-MMP in the membrane fraction was assayed by western blot. Zymography of anti-alphav antibody immunoprecipitates and conditioned media were used to show gelatinolytic activity.

Results

The coprecipitation of MMP-2 with alphavbeta3 by anti-alphav antibody is a strong indication that SiHa cell surface alphavbeta3 integrin is a receptor for MMP-2. Immunoblot assays show the expression of MT1-MMP on SiHa cell membranes and secreted TIMP-2 and pro-MMP-2 in the medium.

Conclusions

SiHa cells express all the molecules which are reported to form a complex to activate pro-MMP-2. Active MMP-2 associated with alphavbeta3 may regulate matrix degradation and thereby modulate directed motility of SiHa cells."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.org/dc/terms/identifier"doi:10.1007/s004320100271"xsd:string
http://purl.uniprot.org/citations/11710594http://purl.org/dc/terms/identifier"doi:10.1007/s004320100271"xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Chatterjee A."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Chatterjee A."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Mitra A."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Mitra A."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Frei E."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Frei E."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Chattopadhyay N."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/author"Chattopadhyay N."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/name"J. Cancer Res. Clin. Oncol."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/name"J. Cancer Res. Clin. Oncol."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/pages"653-658"xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/pages"653-658"xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/title"Human cervical tumor cell (SiHa) surface alphavbeta3 integrin receptor has associated matrix metalloproteinase (MMP-2) activity."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/title"Human cervical tumor cell (SiHa) surface alphavbeta3 integrin receptor has associated matrix metalloproteinase (MMP-2) activity."xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/volume"127"xsd:string
http://purl.uniprot.org/citations/11710594http://purl.uniprot.org/core/volume"127"xsd:string
http://purl.uniprot.org/citations/11710594http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11710594
http://purl.uniprot.org/citations/11710594http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11710594
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