Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
2001-6-25
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23632-8
pubmed:dateRevised
2006-11-15
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
pubmed:year
2001
pubmed:articleTitle
Post-translational processing of bovine chondromodulin-I.
pubmed:affiliation
Center for Research in Skeletal Development and Pediatric Orthopedics, Shriners Hospital for Children, Tampa, Florida 33612, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't