Linked Life Data

2914936

Source:http://linkedlifedata.com/resource/pubmed/id/2914936

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-3-21
pubmed:abstractText
Two forms of dermatan sulfate proteoglycans, called DS-PGI and DS-PGII, have been isolated from both bovine fetal skin and calf articular cartilage and characterized. The proteoglycans were isolated using either (a) molecular sieve chromatography under conditions where DS-PGI selectively self-associates or (b) chromatography on octyl-Sepharose, which separates DS-PGI from DS-PGII based on differences in the hydrophobic properties of their core proteins. The NH2-terminal amino acid sequence of DS-PGI from skin and cartilage is identical. The NH2-terminal amino acid sequence of DS-PGII from skin and cartilage is identical. However, the amino acid sequence data and tryptic peptide maps demonstrate that the core proteins of DS-PGI and DS-PGII differ in primary structure. In DS-PGI from bovine fetal skin, 81-84% of the glycosaminoglycan was composed of IdoA-GalNAc(SO4) disaccharide repeating units. In DS-PGI from calf articular cartilage, only 25-29% of the glycosaminoglycan was composed of IdoA-GalNAc(SO4). In DS-PGII from bovine fetal skin, 85-93% of the glycosaminoglycan was IdoA-GalNAc(SO4), whereas in DS-PGII from calf articular cartilage, only 40-44% of the glycosaminoglycan was IdoA-GalNAc(SO4). Thus, analogous proteoglycans from two different tissues, such as DS-PGI from skin and cartilage, possess a core protein with the same primary structure, yet contain glycosaminoglycan chains which differ greatly in iduronic acid content. These differences in the composition of the glycosaminoglycan chains must be determined by tissue-specific mechanisms which regulate the degree of epimerization of GlcA-GalNAc(SO4) into IdoA-GalNAc(SO4) and not by the primary structure of the core protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2876-84
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:2914936-Amino Acid Sequence, pubmed-meshheading:2914936-Animals, pubmed-meshheading:2914936-Bone and Bones, pubmed-meshheading:2914936-Cartilage, Articular, pubmed-meshheading:2914936-Cattle, pubmed-meshheading:2914936-Chondroitin, pubmed-meshheading:2914936-Chondroitin Sulfate Proteoglycans, pubmed-meshheading:2914936-Chromatography, Gel, pubmed-meshheading:2914936-Dermatan Sulfate, pubmed-meshheading:2914936-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2914936-Female, pubmed-meshheading:2914936-Fetus, pubmed-meshheading:2914936-Guanidine, pubmed-meshheading:2914936-Guanidines, pubmed-meshheading:2914936-Humans, pubmed-meshheading:2914936-Molecular Sequence Data, pubmed-meshheading:2914936-Placenta, pubmed-meshheading:2914936-Pregnancy, pubmed-meshheading:2914936-Proteoglycans, pubmed-meshheading:2914936-Skin
pubmed:year
1989
pubmed:articleTitle
Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography.
pubmed:affiliation
Orthopedic Research Laboratories, Montefiore Medical Center, Bronx, New York 10467.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't