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 language | English |
|---|---|
| Pages (from-to) | 717-723 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 133 |
| Issue number | 2 |
| DOIs | |
| State | Published - 17 Dec 1985 |
Fingerprint
Cite this
}
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 journal › Article
TY - JOUR
T1 - Calcium/phospholipid-dependent protein kinase and its relationship to antidiuretic hormone in toad urinary bladder epithelium
AU - Yorio, Thomas
AU - Quist, Eugene
AU - Masaracchia, Ruthann A.
PY - 1985/12/17
Y1 - 1985/12/17
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0022396269&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(85)90963-5
DO - 10.1016/0006-291X(85)90963-5
M3 - Article
C2 - 3002355
AN - SCOPUS:0022396269
VL - 133
SP - 717
EP - 723
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -