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http://purl.uniprot.org/citations/17435175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17435175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17435175http://www.w3.org/2000/01/rdf-schema#comment"The regulation of matrix metalloproteinases (MMP) has been studied extensively due to the fundamental roles these zinc-endopeptidases play in diverse physiological and pathological processes. However, phosphorylation has not previously been considered as a potential modulator of MMP activity. The ubiquitously expressed MMP-2 contains 29 potential phosphorylation sites. Mass spectrometry reveals that at least five of these sites are phosphorylated in hrMMP-2 expressed in mammalian cells. Treatment of HT1080 cells with an activator of protein kinase C results in a change in MMP-2 immunoreactivity on 2D immunoblots consistent with phosphorylation, and purified MMP-2 is phosphorylated by protein kinase C in vitro. Furthermore, MMP-2 from HT1080 cell-conditioned medium is immunoreactive with antibodies directed against phosphothreonine and phosphoserine, which suggests that it is phosphorylated. Analysis of MMP-2 activity by zymography, gelatin dequenching assays, and measurement of kinetic parameters shows that the phosphorylation status of MMP-2 significantly affects its enzymatic properties. Consistent with this, dephosphorylation of MMP-2 immunoprecipitated from HT1080 conditioned medium with alkaline phosphatase significantly increases its activity. We conclude that MMP-2 is modulated by phosphorylation on multiple sites and that protein kinase C may be a regulator of this protease in vivo."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.org/dc/terms/identifier"doi:10.1096/fj.06-7938com"xsd:string
http://purl.uniprot.org/citations/17435175http://purl.org/dc/terms/identifier"doi:10.1096/fj.06-7938com"xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Sawicki G."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Sawicki G."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Holt A."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Holt A."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Holmes C."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Holmes C."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Berthiaume L.G."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Berthiaume L.G."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Schulz R."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Schulz R."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Ballermann B.J."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Ballermann B.J."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Sawicka J."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Sawicka J."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Sariahmetoglu M."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Sariahmetoglu M."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Crawford B.D."xsd:string
http://purl.uniprot.org/citations/17435175http://purl.uniprot.org/core/author"Crawford B.D."xsd:string