Role of protein kinase c in duodenal mucosal bicarbonate secretion in the guinea pig

H. S. Odes, R. Reimer, R. Muallem, M. Schwenk, W. Beil, K. F. Sewing

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Since duodenal bicarbonate secretion (DBS) is increased by m-cholinoceptor agonists, it was postulated that protein kinase C (PKC) has a role in this secretion. This premise was examined in guinea pigs, using 12-O-tetradecanoyl-phorbol 13-acetate (TPA) to stimulate bicarbonate production in the perfused duodenum in vivo, and to activate PKC in isolated duodenal enterocytes. TPA (10−7 mol·kg−1) infused intravenously stimulated active DBS from basal values of 3.64 ± 0.66 to 8.73 ± 1.59 μmol·cm−1 10 min−1. This effect was completely blocked by verapamil (4 × 10−7 mol·kg−1). PKC activity in duodenal enterocytes in the basal state was most abundant in the cytosolic fraction (2,221 ± 444 U/mg protein) and very low in the particulate fraction (227 ± 51 U/mg protein). TPA (10−7 mol·kg−1) caused a time-dependent translocation of the cytosolic, lipid-dependent activity of PKC into the particulate fraction. The effect was maximal at 5 min incubation and was reversed by 30 min. In the particulate fraction, this activity was no longer lipid-dependent, but could be stimulated by Ca2+ alone. These data support the hypothesis that translocation of PKC may contribute to DBS.

Original languageEnglish
Pages (from-to)60-65
Number of pages6
Issue number1
StatePublished - 1 Jan 1996


  • 12-O-Tetradecanoyl-phorbol 13-acetate
  • Duodenal bicarbonate secretion
  • Protein kinase C

ASJC Scopus subject areas

  • Pharmacology


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