Linked Life Data

9228042

Source:http://linkedlifedata.com/resource/pubmed/id/9228042

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1997-9-9
pubmed:databankReference
pubmed:abstractText
The epiphysis of developing bones is a cartilaginous structure that is eventually replaced by bone during skeletal maturation. We have separated a dermatan sulfate proteoglycan, epiphycan, from decorin and biglycan by using dissociative extraction of bovine fetal epiphyseal cartilage, followed by sequential ion-exchange, gel permeation, hydrophobic, and Zn2+ chelate chromatographic steps. Epiphycan is a member of the small leucine-rich proteoglycan family, contains seven leucine-rich repeats (LRRs), is related to osteoglycin (osteoinductive factor) (Bentz, H., Nathan, R. M., Rosen, D. M., Armstrong, R. M., Thompson, A. Y., Segarini, P. R., Mathews, M. C., Dasch, J., Piez, K. A., and Seyedin, S. M. (1989) J. Biol. Chem. 264, 20805-20810), and appears to be the bovine equivalent of the chick proteoglycan PG-Lb (Shinomura, T., and Kimata, K. (1992) J. Biol. Chem. 267, 1265-1270). The intact proteoglycan had a median size of approximately 133 kDa. The core protein was 46 kDa by electrophoretic analysis, had a calculated size of 34,271 Da, and had two approximately equimolar N termini (APTLES ... and ETYDAT ... ) separated by 11 amino acids. There were at least three O-linked oligosaccharides in the N-terminal region of the protein, based on blank cycles in Edman degradation and corresponding serine or threonine residues in the translated cDNA sequence. The glycosaminoglycans ranged in size from 23 to 34 kDa were more heterogeneous than those in other dermatan sulfate small leucine-rich proteoglycans and were found in the acidic N-terminal region of the protein core, N-terminal to the LRRs. A four-cysteine cluster was present at the N terminus of the LRRs, and a disulfide-bonded cysteine pair was present at the C terminus of the protein core. The seventh LRR and an N-linked oligosaccharide were between the two C-terminal cysteines. An additional potential N-glycosylation site near the C terminus did not appear to be substituted at a significant level.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18709-17
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9228042-Amino Acid Sequence, pubmed-meshheading:9228042-Animals, pubmed-meshheading:9228042-Base Sequence, pubmed-meshheading:9228042-Biglycan, pubmed-meshheading:9228042-Cattle, pubmed-meshheading:9228042-Chromatography, Affinity, pubmed-meshheading:9228042-Chromatography, Gel, pubmed-meshheading:9228042-Chromatography, Ion Exchange, pubmed-meshheading:9228042-Decorin, pubmed-meshheading:9228042-Extracellular Matrix Proteins, pubmed-meshheading:9228042-Glycosylation, pubmed-meshheading:9228042-Growth Plate, pubmed-meshheading:9228042-Leucine, pubmed-meshheading:9228042-Molecular Sequence Data, pubmed-meshheading:9228042-Molecular Weight, pubmed-meshheading:9228042-Peptide Mapping, pubmed-meshheading:9228042-Protein Processing, Post-Translational, pubmed-meshheading:9228042-Proteoglycans, pubmed-meshheading:9228042-Sequence Alignment
pubmed:year
1997
pubmed:articleTitle
Characterization of epiphycan, a small proteoglycan with a leucine-rich repeat core protein.
pubmed:affiliation
Center for Extracellular Matrix Biology, Albert B. Alkek Institute of Biosciences and Technology and the Department of Biochemistry and Biophysics, Texas A & M University, Houston, Texas 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't