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Hormone-induced rise in cytosolic Ca2+ in axolotl hepatocytes: extracellular origin and control by cAMP

Hormone-induced rise in cytosolic Ca2+ in axolotl hepatocytes: extracellular origin and control... THE REGULATION OF GLYCOGEN BREAKDOWN in mammalian liver by a-adrenergic agonists and vasoactive peptides (vasopressin, angiotensin II) has been extensively studied (12). In rat liver these hormones mobilize from intracellular stores associated with the endoplasmic reticulum (9, 20, 23). The effect of the vasoactive peptide [Arg8]vasopressin (AVP), which has the highest - mobilizing potency, is mediated via V1 receptors coupled to phospholipase C, generating the second messenger inositol 1,4,5trisphosphate [ Ins( 1,4,5) P3] and diacylglycerol (2, 7). The V1 receptor has been identified in rat liver, vascular smooth muscle, and platelets (29). Further classification into V1, and V1b subtypes has been proposed following the observation of pharmacological differences between receptors in vascular smooth muscle and pituitary gland (19). Recently, Howl et al. (15) reported that AVP (V,,) receptors were only present in a very low abundance in human liver. In other tissues, for example, renal tubules, AVP stimulates adenylate cyclase and formation of adenosine 3’,5’-cyclic monophosphate (), and receptors coupled to this system have been classified as the V2 subtype (29). In the rat liver the V2 receptor is absent (18). Hormones such as glucagon, or P-adrenergic agonists like isoprenaline, act via the formation of . How0363-6143/93 $2.00 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Hormone-induced rise in cytosolic Ca2+ in axolotl hepatocytes: extracellular origin and control by cAMP

J. W. Kleineke and P. A. Janssens
AJP - Cell Physiology , Volume 265: C1281 – Nov 1, 1993
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Publisher
The American Physiological Society
Copyright
Copyright © 1993 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
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Abstract

THE REGULATION OF GLYCOGEN BREAKDOWN in mammalian liver by a-adrenergic agonists and vasoactive peptides (vasopressin, angiotensin II) has been extensively studied (12). In rat liver these hormones mobilize from intracellular stores associated with the endoplasmic reticulum (9, 20, 23). The effect of the vasoactive peptide [Arg8]vasopressin (AVP), which has the highest - mobilizing potency, is mediated via V1 receptors coupled to phospholipase C, generating the second messenger inositol 1,4,5trisphosphate [ Ins( 1,4,5) P3] and diacylglycerol (2, 7). The V1 receptor has been identified in rat liver, vascular smooth muscle, and platelets (29). Further classification into V1, and V1b subtypes has been proposed following the observation of pharmacological differences between receptors in vascular smooth muscle and pituitary gland (19). Recently, Howl et al. (15) reported that AVP (V,,) receptors were only present in a very low abundance in human liver. In other tissues, for example, renal tubules, AVP stimulates adenylate cyclase and formation of adenosine 3’,5’-cyclic monophosphate (), and receptors coupled to this system have been classified as the V2 subtype (29). In the rat liver the V2 receptor is absent (18). Hormones such as glucagon, or P-adrenergic agonists like isoprenaline, act via the formation of . How0363-6143/93 $2.00

Journal

AJP - Cell Physiology – The American Physiological Society

Published: Nov 1, 1993

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