Calcium/phospholipid-dependent protein kinase and its relationship to antidiuretic hormone in toad urinary bladder epithelium

Thomas Yorio, Eugene Quist, Ruthann A. Masaracchia

Research output: Contribution to journalArticle

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Abstract

The hydro-osmotic response of the toad urinary bladder to antidiuretic hormone (ADH) and cyclic AMP was inhibited by phorbol myristate acetate (PMA) and 4β- phorbol dideconate (4β-PDD), activators of protein kinase C (PKC). The inactive epimer of 4β-PDD, 4α-PDD, had no effect on the ADH response. The osmotic transfer of water in the absence of ADH was unaffected by PMA. PKC activity, localized in the soluble fraction of isolated toad bladder cells, was activated by PMA. ADH initially inhibited and subsequently stimulated 32Pi incorporation into phosphatidic acid (PA) and phosphatidylinositol (PI). Carbachol, which inhibits ADH-induced water flow, also stimulated 32P incorporation into PA and PI. It is suggested that phosphoinositide breakdown to diacylglycerol may activate PKC which functions to attenuate the hormone-mediated permeability response.

Original languageEnglish
Pages (from-to)717-723
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume133
Issue number2
DOIs
StatePublished - 17 Dec 1985

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Vasopressins
Anura
Protein Kinase C
Urinary Bladder
Epithelium
Tetradecanoylphorbol Acetate
Phosphatidylinositols
Phosphatidic Acids
Water
Diglycerides
Carbachol
Cyclic AMP
Permeability
Hormones
phorbol

Cite this

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abstract = "The hydro-osmotic response of the toad urinary bladder to antidiuretic hormone (ADH) and cyclic AMP was inhibited by phorbol myristate acetate (PMA) and 4β- phorbol dideconate (4β-PDD), activators of protein kinase C (PKC). The inactive epimer of 4β-PDD, 4α-PDD, had no effect on the ADH response. The osmotic transfer of water in the absence of ADH was unaffected by PMA. PKC activity, localized in the soluble fraction of isolated toad bladder cells, was activated by PMA. ADH initially inhibited and subsequently stimulated 32Pi incorporation into phosphatidic acid (PA) and phosphatidylinositol (PI). Carbachol, which inhibits ADH-induced water flow, also stimulated 32P incorporation into PA and PI. It is suggested that phosphoinositide breakdown to diacylglycerol may activate PKC which functions to attenuate the hormone-mediated permeability response.",
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Calcium/phospholipid-dependent protein kinase and its relationship to antidiuretic hormone in toad urinary bladder epithelium. / Yorio, Thomas; Quist, Eugene; Masaracchia, Ruthann A.

In: Biochemical and Biophysical Research Communications, Vol. 133, No. 2, 17.12.1985, p. 717-723.

Research output: Contribution to journalArticle

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