Source:http://linkedlifedata.com/resource/pubmed/id/11323410
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
2001-6-25
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pubmed:abstractText |
Chondromodulin-I (ChM-I) is a small glycoprotein that is abundant in fetal cartilage. Mature chondromodulin-I is processed from a larger precursor form, presumably at a proteolytic site RERR-ELVR. The precursor, mature chondromodulin-I and two processed products, the remnant left after removal of mature chondromodulin-I and a smaller, unglycosylated form, were identified using antipeptide antisera. The products of chondromodulin-I precursor processing were seen in cultured chondrocytes, a stable long-term culture chondrosarcoma cell line, as well as Chinese hamster ovary (CHO) cells transfected with an expression plasmid that contained cDNA coding for the chondromodulin-I precursor. Pulse-chase analysis allowed a processing pathway to be analyzed for chondromodulin-I. To further dissect the processing events, three constructs that express recombinant wild-type or mutant chondromodulin-I were transfected into CHO cells. We showed that chondromodulin-I is cleaved intracellularly at the predicted cleavage site, and that the mature glycopeptide is rapidly secreted immediately after processing. The chondromodulin-1 precursor has a short half-life and is not readily apparent in tissue samples, suggesting that chondromodulin is not a member of the juxtacrine family of growth factors, despite some similarities. The smaller unglycosylated form of chondromodulin-I was only observed in cartilage and not in short-term cultures or transfected cells, suggesting an extracellular processing event. No processing occurred when the precursor cleavage site was mutated to RERQ-SLVR or when precursor chondromodulin-I was expressed in the furin-deficient CHO cell line, suggesting the involvement of furin in processing.
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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/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/Furin,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23632-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11323410-Animals,
pubmed-meshheading:11323410-Antibodies,
pubmed-meshheading:11323410-CHO Cells,
pubmed-meshheading:11323410-Cattle,
pubmed-meshheading:11323410-Cells, Cultured,
pubmed-meshheading:11323410-Chondrocytes,
pubmed-meshheading:11323410-Cricetinae,
pubmed-meshheading:11323410-Culture Media, Conditioned,
pubmed-meshheading:11323410-Furin,
pubmed-meshheading:11323410-Growth Substances,
pubmed-meshheading:11323410-Half-Life,
pubmed-meshheading:11323410-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:11323410-Peptides,
pubmed-meshheading:11323410-Protein Precursors,
pubmed-meshheading:11323410-Protein Processing, Post-Translational,
pubmed-meshheading:11323410-Subtilisins,
pubmed-meshheading:11323410-Transfection,
pubmed-meshheading:11323410-Tumor Cells, Cultured
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pubmed:year |
2001
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pubmed:articleTitle |
Post-translational processing of bovine chondromodulin-I.
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pubmed:affiliation |
Center for Research in Skeletal Development and Pediatric Orthopedics, Shriners Hospital for Children, Tampa, Florida 33612, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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