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Science 18 October 1985:
Vol. 230. no. 4723, pp. 327 - 330
DOI: 10.1126/science.2996133
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Articles

Science, Vol 230, Issue 4723, 327-330
Copyright © 1985 by American Association for the Advancement of Science

articles

Evidence that the v-sis gene product transforms by interaction with the receptor for platelet-derived growth factor

F Leal, LT Williams, KC Robbins, and SA Aaronson

A scheme for partial purification of biologically active v-sis-coded protein from cells transformed with simian sarcoma virus (SSV) has made possible a functional comparison of the transforming protein with platelet-derived growth factor (PDGF). The SSV-transforming gene product is capable of specifically binding PDGF receptors, stimulating tyrosine phosphorylation of PDGF receptors, and inducing DNA synthesis in quiescent fibroblasts. Each of these activities was specifically inhibited by antibodies to different regions of the v-sis gene product. Moreover, viral infection of a variety of cell types revealed a strict correlation between those cells possessing PDGF receptors and those susceptible to transformation by SSV. These findings provide evidence that SSV-transforming activity is mediated by the interaction of a virus-coded mitogen with PDGF receptors.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Cell Surface Retention Sequence Binding Protein-1 Interacts with the v-sis Gene Product and Platelet-derived Growth Factor beta -Type Receptor in Simian Sarcoma Virus-transformed Cells.
C. Boensch, S. S. Huang, D. T. Connolly, and J. S. Huang (1999)
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Comparison of biological properties and transforming potential of human PDGF-A and PDGF-B chains.
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The role of individual cysteine residues in the structure and function of the v-sis gene product.
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Oncogenic Potential of the Human Platelet-derived Growth Factor Transcriptional Unit.
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