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rdf:type |
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lifeskim:mentions |
umls-concept:C0007382,
umls-concept:C0145988,
umls-concept:C0172537,
umls-concept:C0205224,
umls-concept:C0596901,
umls-concept:C1514562,
umls-concept:C1611645,
umls-concept:C1704675,
umls-concept:C1707271,
umls-concept:C1879547,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:dateCreated |
1992-6-23
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pubmed:abstractText |
Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1537400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1646720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1647201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1647782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1649175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1649600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1655733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1770006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1868085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1909113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-1911847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2039471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2071592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2158484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2169338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2197998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2269296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2461732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2539808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2551898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2557822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2744487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2793861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2834383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-2844164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-3095317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-3281418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-3431465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-4204102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-6086649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-6162199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-6272745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1317162-7041891
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
283 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
637-41
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1317162-Base Sequence,
pubmed-meshheading:1317162-Catalysis,
pubmed-meshheading:1317162-Cell Membrane,
pubmed-meshheading:1317162-DNA,
pubmed-meshheading:1317162-Enzyme Activation,
pubmed-meshheading:1317162-Gelatinases,
pubmed-meshheading:1317162-Glycoproteins,
pubmed-meshheading:1317162-Humans,
pubmed-meshheading:1317162-Kinetics,
pubmed-meshheading:1317162-Molecular Sequence Data,
pubmed-meshheading:1317162-Molecular Weight,
pubmed-meshheading:1317162-Mutagenesis,
pubmed-meshheading:1317162-Neoplasm Proteins,
pubmed-meshheading:1317162-Pepsin A,
pubmed-meshheading:1317162-Peptide Fragments,
pubmed-meshheading:1317162-Structure-Activity Relationship,
pubmed-meshheading:1317162-Tissue Inhibitor of Metalloproteinase-2,
pubmed-meshheading:1317162-Tissue Inhibitor of Metalloproteinases
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pubmed:year |
1992
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pubmed:articleTitle |
The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases.
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pubmed:affiliation |
Strangeways Research Laboratory, Worts Causeway, Cambridge, U.K.
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pubmed:publicationType |
Journal Article
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