Recombinant human mullerian inhibiting substance inhibits epidermal growth factor receptor tyrosine kinase

F. G. Cigarroa, J. P. Coughlin, P. K. Donahoe, M. F. White, N. Uitvlugt, D. T. MacLaughlin

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Autophosphorylation of the epidermal growth factor (EGF) receptor in A-431 cells and plasma membrane fractions was inhibited by partially purified recombinant human Mullerian Inhibiting Substance (MIS). Immunoprecipitation of the EFG receptor using anti-EGF receptor or anti-phosphotyrosine antibodies, and phosphoamino acid analysis of this receptor, demonstrated that MIS specifically inhibited EGF-induced tyrosine phosphorylation. Inhibition of EGF receptor autophosphorylation by MIS in membrane preparations was not affected by increasing concentrations of EGF, manganese or [γ32)P] ATP. Thus, it is unlikely that MIS competes for EGF binding sites or sequesters substrate. Immunoabsorption of MIS with anti-human MIS antibody blocked the MIS inhibition of EGF receptor autophosphorylation, indicating that the inhibition was due to MIS. Our data suggest that MIS regulates the activity of the EGF receptor tyrosine kinase in A-431 cells.

Original languageEnglish (US)
Pages (from-to)179-191
Number of pages13
JournalGrowth Factors
Volume1
Issue number2
DOIs
StatePublished - Jan 1 1989
Externally publishedYes

Keywords

  • Epidermal growth factor receptor
  • Human Mullerian Inhibiting Substance
  • Tyrosine kinase

ASJC Scopus subject areas

  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

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