Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 20 October 1978:
Vol. 202. no. 4365, pp. 313 - 315
DOI: 10.1126/science.308698

Articles

Science, Vol 202, Issue 4365, 313-315
Copyright © 1978 by American Association for the Advancement of Science


articles

Tumor-promoting phorbol esters inhibit binding of epidermal growth factor to cellular receptors

LS Lee and IB Weinstein

Tumor-promoting phorbol esters and related plant macrocyclic diterpenes inhibit the binding of epidermal growth factor to its receptors on HeLa cells. This effect shows marked structural specificity and correlates with other biological effects of these compounds on mouse skin and in cell culture systems. The active compounds inhibited binding of 125I-labeled epidermal growth factor with a 50 per-cent effective dose in the range of 10(-8) to 10(-9) M. Inhibition appears to be due to a decrease in the number of available epidermal growth factor receptors rather than a change in receptor affinity. These results suggest that certain biologic effects of tumor promoters may result from alterations in the function of cell surface receptors involved in growth regulation.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Growth Hormone Alters Epidermal Growth Factor Receptor Binding Affinity via Activation of Extracellular Signal-Regulated Kinases in 3T3-F442A Cells.
Y. Huang, Y. Chang, X. Wang, J. Jiang, and S. J. Frank (2004)
Endocrinology 145, 3297-3306
   Abstract »    Full Text »    PDF »
Distinct Cytoplasmic Domains of the Growth Hormone Receptor Are Required for Glucocorticoid- and Phorbol Ester-induced Decreases in Growth Hormone (GH) Binding. THESE DOMAINS ARE DIFFERENT FROM THAT REPORTED FOR GH-INDUCED RECEPTOR INTERNALIZATION.
A. P.J. King, M.-J. Tseng, C. D. Logsdon, N. Billestrup, and C. Carter-Su (1996)
J. Biol. Chem. 271, 18088-18094
   Abstract »    Full Text »    PDF »
Neu Differentiation Factor Inhibits EGF Binding.
D. Karunagaran, E. Tzahar, N. Liu, D. Wen, and Y. Yarden (1995)
J. Biol. Chem. 270, 9982-9990
   Abstract »    Full Text »    PDF »
Bromine residue at hydrophilic region influences biological activity of aplysiatoxin, a tumor promoter.
K Shimomura, M. Mullinix, T Kakunaga, H Fujiki, and T Sugimura (1983)
Science 222, 1242-1244
   Abstract »    PDF »
Tumor-promoting phorbol esters stimulate hematopoietic colony formation in vitro.
R. Stuart and J. Hamilton (1980)
Science 208, 402-404
   Abstract »    PDF »
Regulation of the Ligand Binding Activity of the Human Very Low Density Lipoprotein Receptor by Protein Kinase C-dependent Phosphorylation.
R. Sakthivel, J.-C. Zhang, D. K. Strickland, M. Gafvels, and K. R. McCrae (2001)
J. Biol. Chem. 276, 555-562
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)