Osmotic activation of the Na+ H+ antiport in protein kinase C-depleted lymphocytes

Sergio Grinstein, Esther Mack, Gordon B. Mills

    Research output: Contribution to journalArticle

    32 Scopus citations

    Abstract

    The Na+ H+ antiport of rat thymic lymphocytes is activated when protein kinase C is stimulated by phorbol esters. A similar activation of the antiport is obtained when the cells are treated with hypertonic solutions. We tested the possibility that protein kinase C also mediates the osmotic activation of Na+ H+ exchange. Protein kinase C was depleted by preincubation of thymocytes for 24 hr in the presence of high concentrations of phorbol ester. Disappearance of the enzyme was assessed by direct measurement of phosphotransferase activity, and by the loss of biological responses to phorbol esters. The Na+ H+ antiport in protein kinase C-depleted cells was not stimulated by addition of phorbol ester, but responded normally to hypertonic treatment. The results indicate that the osmotic activation of countertransport does not require stimulation of protein kinase C.

    Original languageEnglish (US)
    Pages (from-to)8-13
    Number of pages6
    JournalBiochemical and Biophysical Research Communications
    Volume134
    Issue number1
    DOIs
    StatePublished - Jan 14 1986

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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