Linked Life Data

7592883

Source:http://linkedlifedata.com/resource/pubmed/id/7592883

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
1995-12-21
pubmed:abstractText
We have previously shown that soluble partially degraded fibrin(ogen) remains in solution after fibrin clot formation and is a potent fibroblast mitogen (Gray, A.J., Bishop, J.E., Reeves J.T., Mecham, R.P., and Laurent, G.J. (1995) Am. J. Cell Mol. Biol. 12, 684-690). Mitogenic sites within the fibrin(ogen) molecule are located on the A alpha and B beta chains of the protein (Gray, A.J., Bishop, J. E., Reeves, J.T., and Laurent, G.J. (1993) J. Cell Sci. 104, 409-413). However, receptor pathways through which mitogenic effects are mediated are unknown. The present study sought to determine the nature of fibrin(ogen) receptors expressed on human fibroblasts which interact with the fibrinogen B beta chain. Receptor complexes were isolated from 125I-surface-labeled fibroblasts and purified on a fibrinogen B beta chain affinity column. Subsequent high performance liquid chromatography and SDS-polyacrylamide gel electrophoresis analysis indicated fibrinogen B beta chain bound specifically to a 60-kDa surface protein. Sequence analysis of the amino terminus of this protein indicated 100% homology to human calreticulin. Immunoprecipitation experiments employing a polyclonal anti-calreticulin antibody provided further evidence that the 60-kDa protein isolated in this study was calreticulin. Further, polyclonal antibodies to human calreticulin significantly inhibited the mitogenic activity of fibrinogen B beta chain on human fibroblasts. The present study has shown that cell surface calreticulin binds to the B beta chain of fibrinogen mediating its mitogenic activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26602-6
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed-meshheading:7592883-Amino Acid Sequence, pubmed-meshheading:7592883-Antibodies, pubmed-meshheading:7592883-Calcium-Binding Proteins, pubmed-meshheading:7592883-Calreticulin, pubmed-meshheading:7592883-Cell Division, pubmed-meshheading:7592883-Cell Line, pubmed-meshheading:7592883-Cell Membrane, pubmed-meshheading:7592883-Chromatography, Affinity, pubmed-meshheading:7592883-Chromatography, High Pressure Liquid, pubmed-meshheading:7592883-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7592883-Fibrinogen, pubmed-meshheading:7592883-Fibroblasts, pubmed-meshheading:7592883-Humans, pubmed-meshheading:7592883-Immunohistochemistry, pubmed-meshheading:7592883-Lectins, pubmed-meshheading:7592883-Lung, pubmed-meshheading:7592883-Macromolecular Substances, pubmed-meshheading:7592883-Mitogens, pubmed-meshheading:7592883-Molecular Sequence Data, pubmed-meshheading:7592883-Molecular Weight, pubmed-meshheading:7592883-Peptide Fragments, pubmed-meshheading:7592883-Ribonucleoproteins
pubmed:year
1995
pubmed:articleTitle
The mitogenic effects of the B beta chain of fibrinogen are mediated through cell surface calreticulin.
pubmed:affiliation
University College London Medical School, Division of Cardiopulmonary Biochemistry, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't