Linked Life Data

9643649

Source:http://linkedlifedata.com/resource/pubmed/id/9643649

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1999-3-29
pubmed:abstractText
In order to elucidate the mechanisms determining the variability in the proteoglycan structure and the factors involved in this determination, we treated chick embryo skin fibroblasts with beta-D-xyloside to obtain glycosaminoglycan chains deprived of core proteins, and with different cytokines (transforming growth factor alpha and beta, interleukin-1) to produce variability. The different cytokines specifically regulate both cellular and extracellular amount and composition of glycosaminoglycans. Beta-D-xyloside treatment does not change protein content and protein synthesis, whereas it increases overall extracellular sulphated glycosaminoglycan production, heparan sulphate and chondroitin sulphate content, and reduces that of dermatan sulphate. This indicates that the core protein regulates quantitative proteoglycan production, and probably directs (with appropriate signals) the core oligosaccharide bound to it to the right synthesizing enzymes. The modulatory action of the different cytokines on sulphated glycosaminoglycan production and classes remains, even though the core protein is absent. This indicates that the cytokines also act on the glycosyltransferases. Our results suggest that the proteoglycan production may be subject to a double control, one of which is at the level of the core protein and the other, mediated by environmental signals, at the level of glycosaminoglycan synthesizing enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
A contribution to the regulation of proteoglycan production: modulation by TGF alpha, TGF beta and IL-1 of glycosaminoglycan biosynthesis on beta-D-xyloside in chick embryo fibroblasts.
pubmed:affiliation
Istituto di Istologia ed Embriologia Generale, Università degli Studi di Ferrara, Italy. enr@dns.unife.it
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't