Source:http://linkedlifedata.com/resource/pubmed/id/12907688
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
43
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| pubmed:dateCreated |
2003-10-20
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| pubmed:abstractText |
ADAMTS-1 (a disintegrin and metalloprotease with thrombospondin motifs-1) is a member of the ADAMTS family of metalloproteases which, together with ADAMTS-4 and ADAMTS-5, has been shown to degrade members of the lectican family of proteoglycans. ADAMTS-1 mRNA is induced in granulosa cells of periovulatory follicles by the luteinizing hormone surge through a progesterone receptor-dependent mechanism. Female progesterone receptor knockout (PRKO) mice are infertile primarily due to ovulatory failure and lack the normal periovulatory induction of ADAMTS-1 mRNA. We therefore investigated the protein localization and function of ADAMTS-1 in ovulating ovaries. Antibodies against two specific peptide regions, the pro-domain and the metalloprotease domain of ADAMTS-1, were generated. Pro-ADAMTS-1 of 110 kDa was identified in mural granulosa cells and appears localized to cytoplasmic secretory vesicles. The mature (85-kDa pro-domain truncated) form accumulated in the extracellular matrix of the cumulus oocyte complex (COC) during the process of matrix expansion. Each form of ADAMTS-1 protein increased >10-fold after the ovulatory luteinizing hormone surge in wild-type but not PRKO mice. Versican is also localized selectively to the ovulating COC matrix and was found to be cleaved yielding a 70-kDa N-terminal fragment immunopositive for the neoepitope DPEAAE generated by ADAMTS-1 and ADAMTS-4 protease activity. This extracellular processing of versican was reduced in ADAMTS-1-deficient PRKO mouse ovaries. These observations suggest that one function of ADAMTS-1 in ovulation is to cleave versican in the expanded COC matrix and that the anovulatory phenotype of PRKO mice is at least partially due to loss of this function.
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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/Adamts1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Cspg2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Disintegrins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/Versicans
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
24
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| pubmed:volume |
278
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
42330-9
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:12907688-ADAM Proteins,
pubmed-meshheading:12907688-Animals,
pubmed-meshheading:12907688-Antibodies, Monoclonal,
pubmed-meshheading:12907688-Chondroitin Sulfate Proteoglycans,
pubmed-meshheading:12907688-Disintegrins,
pubmed-meshheading:12907688-Enzyme Precursors,
pubmed-meshheading:12907688-Extracellular Matrix,
pubmed-meshheading:12907688-Female,
pubmed-meshheading:12907688-Granulosa Cells,
pubmed-meshheading:12907688-Immunohistochemistry,
pubmed-meshheading:12907688-Isoenzymes,
pubmed-meshheading:12907688-Lectins, C-Type,
pubmed-meshheading:12907688-Metalloendopeptidases,
pubmed-meshheading:12907688-Mice,
pubmed-meshheading:12907688-Mice, Inbred C57BL,
pubmed-meshheading:12907688-Mice, Knockout,
pubmed-meshheading:12907688-Oocytes,
pubmed-meshheading:12907688-Ovulation,
pubmed-meshheading:12907688-Peptide Hydrolases,
pubmed-meshheading:12907688-Receptors, Progesterone,
pubmed-meshheading:12907688-Tissue Distribution,
pubmed-meshheading:12907688-Versicans
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| pubmed:year |
2003
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| pubmed:articleTitle |
Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation.
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| pubmed:affiliation |
Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
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| pubmed:publicationType |
Journal Article
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