Linked Life Data

838706

Source:http://linkedlifedata.com/resource/pubmed/id/838706

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1977-4-15
pubmed:abstractText
Tunicamycin, an inhibitor of lipid carrier-dependent protein glycosylation, was used in studies of procollagen synthesis, secretion, and proteolytic modification by chick cranial bones in organ culture and by chick tendon fibroblasts in tissue culture. Tunicamycin inhibited the incorporation of D-[2-3H]mannose into procollagen by greater than 90% whereas general protein synthesis and collagen synthesis were decreased by only 10 to 20%. The procollagen synthesized in the presence of tunicamycin was secreted normally and its immunological characteristics, as detected by an antiserum to the intact protein, were unchanged. However, tunicamycin caused an accumulation of biosynthetic intermediates containing disulfide-bonded COOH-terminal extensions in both cell and bone culture. Cleavage of NH2-terminal extensions was not detectably impaired. These findings provide additional support for the involvement of more than one enzyme in the limited proteolytic conversion of procollagen to collagen.
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
10
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
955-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Impaired conversion of procollagen to collagen by fibroblasts and bone treated with tunicamycin, an inhibitor of protein glycosylation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.