Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1976-10-2
pubmed:abstractText
[14C]Proline and [14C]lysine were incorporated into collagen by cultures of endothelial cells derived from calf aortae. The isomer 3-hydroxy[14C]proline accounted for 10% of the total hydroxy[14C]proline in the collagen isolated from the medium. Approximately 81% of the hydroxy[14C]lysine isolated from the medium was glycosylated, and 91% of the glycosylated hydroxy[14C]lysine was in the form of the disaccharide glucosylgalactose. Gel filtration chromatography or acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate indicated that the initially synthesized peptide chain of [14C]collagen had a molecular weight of about 135,000; after pepsin digestion this was converted to 115,000. The ratio of hydroxy[14C]proline to total [14C]proline x 100 in the pesin-resistant fraction was 59. When examined by immunofluorescence microscopy, the endothelial cultures stained positively with antiserum to (Type IV) collagen from basement membrane of bovine anterior lens capsule. The data indicate that cultured endothelial cells derived from calf aortae synthesize collagen that resembles that of basement membrane collagen.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-1150659, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-1175598, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-1249049, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-178327, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4198817, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4337858, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4337936, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4351528, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4355998, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4363161, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4509328, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4555424, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4583355, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4718112, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4841213, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-4900997, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-5937008, http://linkedlifedata.com/resource/pubmed/commentcorrection/59926-5959433
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2361-4
pubmed:dateRevised
2010-9-1
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Characterization of the collagen synthesized by endothelial cells in culture.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.