Epidermal Growth Factor Activates Phosphoinositide Turnover and Protein Kinase C in BALB/MK Keratinocytes

Jorge Moscat, Christopher J. Molloy, Timothy P. Fleming, Stuart A. Aaronson

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

BALB/MK is a nontransformed epithelial cell line derived from primary BALB/c mouse keratinocytes that requires epidermal growth factor (EGF) for growth. Using a defined-medium culture system, we investigated the role of physiological concentrations of EGF on phosphoinositide metabolism in these cells. The results show that EGF rapidly activates phospholipase-C mediated phosphoinositide metabolism resulting in the generation of the second messengers inositol 1,4,5-trisphosphate and diacylglyc-erol. These metabolites control intracellular Ca2+ levels and activate protein kinase C, respectively. Protein kinase C activation in response to EGF was evidenced by the phosphorylation of the acidic 80 kilodalton endogenous protein substrate (p80) specific for this kinase. In contrast, insulin, which acts in concert with EGF to cause BALB/MK cell proliferation, had no effect on phosphoinositide metabolism nor led to any additional stimulation when added in combination with EGF. Taken together, our results show that rapid alterations in phosphoinositide metabolism and protein kinase C activation are associated with the normal mitogenic response of keratinocytes to EGF.

Original languageEnglish (US)
Pages (from-to)799-805
Number of pages7
JournalMolecular Endocrinology
Volume2
Issue number9
DOIs
StatePublished - Sep 1988
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Endocrinology

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