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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1994-1-31
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pubmed:abstractText |
Human proteoglycan was aggregated to an immobilized hyaluronan solid phase on a 96-well ELISA plate. This complex was then degraded by recombinant human stromelysin. The remaining proteoglycan fragments were detected using a monoclonal antibody probe directed against the chondroitin sulfate (CS) region of the core protein. Stromelysin degraded the aggregate in a time and dose dependent manner as reflected by the loss of the CS epitope. Assay sensitivity was 0.125 U/well with total loss of the CS epitope occurring at 4 U/well. o-phenanthroline (IC50 = 52 microM) and U24522 (IC50 = 9 microM) inhibited degradation, while phosphoramidon did not. Serine and cysteine protease inhibitors had no effect. A comparative analysis of this assay with a reference method, substance P assay, gave similar inhibitor profiles. The use of aggregated human proteoglycan (native conformation) as a substrate, may better reflect how stromelysin inhibitors behave in the presence of complex substrates such as cartilage matrix.
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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/1,10-phenanthroline,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Phenanthrolines,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Substance P,
http://linkedlifedata.com/resource/pubmed/chemical/phosphoramidon
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pubmed:status |
MEDLINE
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pubmed:issn |
0065-4299
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
39 Spec No
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C151-3
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7506000-Animals,
pubmed-meshheading:7506000-Antibodies, Monoclonal,
pubmed-meshheading:7506000-Cartilage, Articular,
pubmed-meshheading:7506000-Chondroitin Sulfates,
pubmed-meshheading:7506000-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:7506000-Femur,
pubmed-meshheading:7506000-Glycopeptides,
pubmed-meshheading:7506000-Humans,
pubmed-meshheading:7506000-Hyaluronic Acid,
pubmed-meshheading:7506000-Matrix Metalloproteinase 3,
pubmed-meshheading:7506000-Metalloendopeptidases,
pubmed-meshheading:7506000-Mice,
pubmed-meshheading:7506000-Phenanthrolines,
pubmed-meshheading:7506000-Proteoglycans,
pubmed-meshheading:7506000-Recombinant Proteins,
pubmed-meshheading:7506000-Substance P
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pubmed:year |
1993
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pubmed:articleTitle |
A stromelysin assay for the assessment of metalloprotease inhibitors on human aggregated proteoglycan.
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pubmed:affiliation |
Research Department, CIBA-GEIGY Corp., Summit, NJ 07901.
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pubmed:publicationType |
Journal Article
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