Source:http://linkedlifedata.com/resource/pubmed/id/12392761
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2002-10-23
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pubmed:abstractText |
ADAM-TS5 (aggrecanase 2), one of two cartilage aggrecanases is a member of the ADAM protein family. Like ADAM-TS4 (aggrecanase 1) the enzyme cleaves cartilage aggrecan at the Glu(373)-Ala(374) bond, a marker of aggrecanase activity. In this study we have characterized the substrate specificity of ADAM-TS5 and compared it with that of ADAM-TS4. The recombinant human ADAM-TS5, like ADAM-TS4 cleaves aggrecan at Glu(1480)-Gly(1481), Glu(1667)-Gly(1668), Glu(1771)-Ala(1772) and Glu(1871)-Leu(1872) bonds more readily than at the Glu(373)-Ala(374) bond. In addition, ADAM-TS5 exhibited an additional site of cleavage in the region spanning residues Gly(1481) and Glu(1667), representing a unique cleavage of ADAM-TS5. ADAM-TS5 cleaved aggrecan approximately 2-fold slower than ADAM-TS4. Neither ADAM-TS5 nor ADAM-TS4 was able to cleave the extracellular matrix proteins fibronectin, thrombospondin, type I collagen, type II collagen, gelatin or general protein substrates such as casein and transferrin. Finally, the zymogen of stromelysin (MMP-3) was not activated by either ADAM-TS4 or ADAM-TS5.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADAM Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ADAMTS5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Aggrecans,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen N-Endopeptidase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/aggrecanase-1
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0945-053X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2002 Elsevier Science B.V. and International Society of Matrix Biology
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pubmed:issnType |
Print
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
499-511
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12392761-ADAM Proteins,
pubmed-meshheading:12392761-Aggrecans,
pubmed-meshheading:12392761-Animals,
pubmed-meshheading:12392761-Cell Line,
pubmed-meshheading:12392761-Drosophila,
pubmed-meshheading:12392761-Extracellular Matrix Proteins,
pubmed-meshheading:12392761-Humans,
pubmed-meshheading:12392761-Lectins, C-Type,
pubmed-meshheading:12392761-Metalloendopeptidases,
pubmed-meshheading:12392761-Procollagen N-Endopeptidase,
pubmed-meshheading:12392761-Proteoglycans,
pubmed-meshheading:12392761-Recombinant Proteins,
pubmed-meshheading:12392761-Substrate Specificity,
pubmed-meshheading:12392761-Time Factors
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pubmed:year |
2002
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pubmed:articleTitle |
Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4).
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pubmed:affiliation |
Department of Inflammatory Diseases Research, DuPont Pharmaceuticals Company, Wilmington, DE 19880-0400, USA. micky.d.tortorella@pharmacia.com
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pubmed:publicationType |
Journal Article,
Comparative Study
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