Regulation of histamine H1 receptor-mediated phosphoinositide hydrolysis by histamine and phorbol esters in DDT1 MF-2 cells

Matthew S. Cowlen, Michael R. Barnes, Myron L. Toews

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The regulation of histamine-stimulated phosphoinositide turnover by histamine and phorbol esters was examined in intact DDT1 MF-2 cells grown in suspension culture. Histamine increased the incorporation of 32P into phosphatidylinositol (PI) in these cells, and this stimulation was inhibited by the H1 antagonist diphenhydramine but not by the H2 antagonist cimetidine. Pretreatment of cells with histamine or with phorbol 12-myristate 13-acetate (PMA) or other activators of protein kinase C induced a marked decrease in the subsequent stimulation by histamine. PMA, but not histamine, also decreased the ability of epinephrine to stimulate PI labelling through α1-adrenoceptors. Thus, histamine appears to induce homologous desensitization of histamine H1 receptor-mediated PI turnover, whereas direct activation of protein kinase C in the absence of receptor occupancy by agonist induces nonspecific heterologous desensitization of both histamine H1- and α1-adrenoceptor-mediated responses.

Original languageEnglish (US)
Pages (from-to)105-112
Number of pages8
JournalEuropean Journal of Pharmacology: Molecular Pharmacology
Issue number2-3
StatePublished - Mar 13 1990
Externally publishedYes


  • Desensitization
  • Histamine receptors
  • Phosphoinositide hydrolysis
  • Protein kinase C

ASJC Scopus subject areas

  • Pharmacology


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