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

Sergio Grinstein, Esther Mack, Gordon Mills

Research output: Contribution to journalArticle

32 Citations (Scopus)

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
Externally publishedYes

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Lymphocytes
Ion Transport
Protein Kinase C
Phorbol Esters
Chemical activation
Hypertonic Solutions
Thymocytes
Rats
Ion exchange
Phosphotransferases
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Osmotic activation of the Na+ H+ antiport in protein kinase C-depleted lymphocytes. / Grinstein, Sergio; Mack, Esther; Mills, Gordon.

In: Biochemical and Biophysical Research Communications, Vol. 134, No. 1, 14.01.1986, p. 8-13.

Research output: Contribution to journalArticle

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