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Synthesis and secretion of thrombospondin by cultured human endothelial cells.

Open access
Mosher, D F, Doyle, M J, Jaffe, E A·1982·The Journal of cell biology

Abstract

Thrombospondin, the major glycoprotein released from alpha-granules of thrombin-stimulated platelets, is a disulfide-bonded trimer of 160 kilodalton subunits and apparently functions as a platelet lectin. Because cultured human umbilical vein endothelial cells synthesize and secrete a glycoprotein (GP-160) which is a disulfide-bonded multimer of 160 kdalton subunits, the possibility that GP-160 is thrombospondin was investigated. Tritiated GP-160 could be immunoisolated from [3H]leucine-labeled endothelial cell postculture medium using a rabbit antiserum to human platelet thrombospondin. Thrombospondin and GP-160 comigrated in two different two-dimensional electrophoretic systems. Both proteins are disulfide-bonded trimers of acidic 160-kdalton subunits. A competitive radioimmunoassay for binding of 125I-thrombospondin to the rabbit antibodies indicated that 49 micrograms of thrombospondin antigen per 10(6) confluent endothelial cells accumulated in postculture medium over 24 h. Thus, endothelial cells secrete large amounts of a glycoprotein that is identical or very similar to platelet thrombospondin.

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Metadata

Authors
Mosher, D. F., Doyle, M. J., & Jaffe, E. A.
Venue
The Journal of cell biology
Published
1982-05-01
Volume
93
Issue
2
Pages
343-348
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2085931182
Cited by
304
References
0
FWCI
15.22
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Synthesis and secretion of thrombospondin by cultured human endothelial cells. https://app.cochat.ai/papers/10.1083/jcb.93.2.343
The paper
Mosher, D. F., Doyle, M. J., & Jaffe, E. A. (1982). Synthesis and secretion of thrombospondin by cultured human endothelial cells. The Journal of cell biology. https://doi.org/10.1083/jcb.93.2.343

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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