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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1996-11-7
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pubmed:abstractText |
Membrane type 1-matrix metalloproteinase (MT1-MMP) initiates the activation of the zymogen progelatinase A/ 72-kDa type IV collagenase by cleavage of the Asn66-Leu peptide bond. We previously pointed out that MT1-MMP possesses a unique amino acid sequence Arg-Arg-Lys-Arg111 which is a potential recognition sequence for furin-like proteases (Nature, 370 (1994) 61-65). Here, using a recombinant MT1-MMP expressed in Escherichia coli we demonstrated that furin specifically cleaves MT1-MMP between Arg111-Tyr in vitro, which resulted in a stimulation of progelatinase A-activation function. Tissue inhibitor of metalloproteinases (TIMP)-2 inhibited activation of progelatinase A by forming a stable complex with activated MT1-MMP.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Furin,
http://linkedlifedata.com/resource/pubmed/chemical/Gelatinases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins,
http://linkedlifedata.com/resource/pubmed/chemical/Thiophenes,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Inhibitor of...,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/batimastat,
http://linkedlifedata.com/resource/pubmed/chemical/progelatinase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
393
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
101-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8804434-Arginine,
pubmed-meshheading:8804434-Binding Sites,
pubmed-meshheading:8804434-Enzyme Activation,
pubmed-meshheading:8804434-Enzyme Precursors,
pubmed-meshheading:8804434-Furin,
pubmed-meshheading:8804434-Gelatinases,
pubmed-meshheading:8804434-Glycoproteins,
pubmed-meshheading:8804434-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:8804434-Metalloendopeptidases,
pubmed-meshheading:8804434-Phenylalanine,
pubmed-meshheading:8804434-Protease Inhibitors,
pubmed-meshheading:8804434-Proteins,
pubmed-meshheading:8804434-Recombinant Fusion Proteins,
pubmed-meshheading:8804434-Subtilisins,
pubmed-meshheading:8804434-Thiophenes,
pubmed-meshheading:8804434-Tissue Inhibitor of Metalloproteinase-2,
pubmed-meshheading:8804434-Tissue Inhibitor of Metalloproteinases,
pubmed-meshheading:8804434-Tyrosine
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pubmed:year |
1996
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pubmed:articleTitle |
Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2.
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pubmed:affiliation |
Department of Molecular Virology and Oncology, Kanazawa University, Japan. vhsato@kenroku.ipc.kanazawa-u.ac.jp
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pubmed:publicationType |
Journal Article
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