Purification of a glycoprotein vascular endothelial cell mitogen from a rat glioma-derived cell line

G. Conn, D. D. Soderman, M. T. Schaeffer, M. Wile, V. B. Hatcher, K. A. Thomas

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Abstract

A growth factor that is mitogenic for vascular endothelial cells, with an ED50 of ~ 1 ng/ml, has been purified 170,000-fold to apparent homogeneity from tissue culture medium conditioned by a rat glioma-derived cell line. The pure protein is a 46-kDa dimer composed of two subunits of equivalent mass as established by comparison of migration in SDS/polyacrylamide gels with and without prior reduction. This glioma-derived growth factor is a glycoprotein and is not mitogenic for BALB/c 3T3 fibroblasts, properties that further distinguish it from other well-characterized vascular endothelial cell mitogens. In contrast to acidic and basic fibroblast growth factors and to platelet-derived endothelial cell growth factor, which have no secretory leader sequences and might only be released by leakage from damaged cells, the glycoprotein nature of this mitogen implies that it is processed through the glycosylating secretory pathway. This secretable growth factor could, therefore, be readily available in the extracellular space under normal physiological conditions in vivo to promote vascular endothelial cell proliferation associated with blood-vessel growth and maintenance.

Original languageEnglish (US)
Pages (from-to)1323-1327
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number4
DOIs
Publication statusPublished - Jan 1 1990
Externally publishedYes

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Keywords

  • angiogenesis
  • cancer
  • neurobiology
  • protein growth factor

ASJC Scopus subject areas

  • General

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