Linked Life Data

1980159

Source:http://linkedlifedata.com/resource/pubmed/id/1980159

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-2-21
pubmed:abstractText
The localization and biosynthesis of functional thrombomodulin (TM) on the cell surfaces of human platelets, megakaryocytes and a human megakaryoblastic cell line (MEG-01) were investigated. TM was demonstrated on the cell surfaces and in cytoplasms of human platelets, megakaryocytes and MEG-01 by an indirect immunofluorescent technique using monospecific rabbit anti-human TM serum. Immunoelectronmicroscopic analysis revealed that TM was localized in plasma membranes of MEG-01 cells as well as human megakaryocytes. 125I-monoclonal antithrombomodulin IgG binding assay showed that one MEG-01 cell possessed approximately 78,000 TM molecules on its cell surface. Thrombin-dependent protein C activating-cofactor activity was demonstrated on MEG-01 cells. Northern hybridization technique using cDNA probe of TM revealed that poly(A)(+)-RNA from MEG-01 cells showed a single band of 3.8 kb similar to that from human endothelial cells. These data suggest that human megakaryocytes synthesize functional TM, and thereby platelets possess TM on their surfaces. TM on platelets may participate in the activation of protein C at the site of a hemostatic plug.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
297-301
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Localization and biosynthesis of functional thrombomodulin in human megakaryocytes and a human megakaryoblastic cell line (MEG-01).
pubmed:affiliation
First Dept. of Internal Medicine, Nagoya University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't