Linked Life Data

2825666

Source:http://linkedlifedata.com/resource/pubmed/id/2825666

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-12-21
pubmed:abstractText
Mouse calvarial osteoblasts grown on native type I collagen films degrade collagen in response to 1,25 (OH) 2vitD3. Collagen degradation is accompanied by increased latent collagenase and gelatinase secretion and by a reduction in free TIMP. Exogenous human recombinant TIMP abolished 1,25 (OH) 2vitD3 stimulated collagen degradation and inhibited background collagenolysis. No active metalloproteinases were detectable in the culture medium suggesting sequestration of active enzyme at the site of action or inhibition by residual TIMP. Chondrocytes could not mimic osteoblasts in this system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
596-602
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Degradation of type I collagen films by mouse osteoblasts is stimulated by 1,25 dihydroxyvitamin D3 and inhibited by human recombinant TIMP (tissue inhibitor of metalloproteinases).
pubmed:affiliation
Cell Physiology, Strangeways Research Laboratory, Worts Causeway, Cambridge.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't