Intracellular receptors for inositol 1,4,5-trisphosphate in angiotensin II target tissues

G. Guillemette, T. Balla, A. J. Baukal, A. Spät, K. J. Catt

Research output: Contribution to journalArticle

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Abstract

Many cells (including angiotensin II target cells) respond to external stimuli with accelerated hydrolysis of phosphatidylinositol 4,5-bisphosphate, generating 1,2-diacylglycerol and inositol 1,4,5-trisphosphate, a rapidly diffusible and potent Ca2+-mobilizing factor. Following its production at the plasma membrane level, inositol 1,4,5-trisphosphate is believed to interact with specific sites in the endoplasmic reticulum and triggers the release of stored Ca2+. Specific receptor sites for inositol 1,4,5-trisphosphate were recently identified in the bovine adrenal cortex and have been further characterized in the adrenal cortex and other target tissues. The inositol 1,4,5-trisphosphate-binding sites are saturable and present in low concentration (104 ± 48 fmol/mg protein) and exhibit high affinity for inositol 1,4,5-trisphosphate (K(d) 1.7 ± 0.6 nM). Their ligand specificity is illustrated by their low affinity for inositol 1,4-bisphosphate (K(d) ~ 10-7 M), inositol 1-phosphate and phytic acid (K(d) ~ 10-4 M), fructose 1,6-bisphosphate and 2,3-bisphosphoglycerate (K(d) ~ 10-3 M), with no detectable affinity for inositol 1-phosphate and myo-inositol. These binding sites are distinct from the degradative enzyme, inositol trisphosphate phosphatase, which has a much lower affinity for inositol trisphosphate (K(m) = 17 μM). Furthermore, submicromolar concentrations of inositol 1,4,5-trisphosphate evoked a rapid release of Ca2+ from nonmitochondrial ATP-dependent storage sites in the adrenal cortex. Specific and saturable binding sites for inositol 1,4,5-trisphosphate were also observed in the anterior pituitary (K(d) = 0.87 ± 0.31 nM, B(max) = 14.8 ± 9.0 fmol/mg protein) and in the liver (K(d) = 1.66 ± 0.7 nM, B(max) = 147 ± 24 fmol/mg protein). These data suggest that the binding sites described in this study are specific receptors through which inositol 1,4,5-trisphosphate mobilizes Ca2+ in target tissues for angiontensin II and other calcium-dependent hormones.

Original languageEnglish
Pages (from-to)1010-1015
Number of pages6
JournalJournal of Biological Chemistry
Volume262
Issue number3
Publication statusPublished - 1987

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Inositol 1,4,5-Trisphosphate Receptors
Inositol 1,4,5-Trisphosphate
Angiotensin II
Tissue
Adrenal Cortex
Binding Sites
Inositol
2,3-Diphosphoglycerate
Phytic Acid
Proteins
Phosphatidylinositols
Endoplasmic Reticulum
Cell membranes
Phosphoric Monoester Hydrolases
Liver
Hydrolysis
Adenosine Triphosphate
Cell Membrane
Hormones
Ligands

ASJC Scopus subject areas

  • Biochemistry

Cite this

Guillemette, G., Balla, T., Baukal, A. J., Spät, A., & Catt, K. J. (1987). Intracellular receptors for inositol 1,4,5-trisphosphate in angiotensin II target tissues. Journal of Biological Chemistry, 262(3), 1010-1015.

Intracellular receptors for inositol 1,4,5-trisphosphate in angiotensin II target tissues. / Guillemette, G.; Balla, T.; Baukal, A. J.; Spät, A.; Catt, K. J.

In: Journal of Biological Chemistry, Vol. 262, No. 3, 1987, p. 1010-1015.

Research output: Contribution to journalArticle

Guillemette, G, Balla, T, Baukal, AJ, Spät, A & Catt, KJ 1987, 'Intracellular receptors for inositol 1,4,5-trisphosphate in angiotensin II target tissues', Journal of Biological Chemistry, vol. 262, no. 3, pp. 1010-1015.
Guillemette, G. ; Balla, T. ; Baukal, A. J. ; Spät, A. ; Catt, K. J. / Intracellular receptors for inositol 1,4,5-trisphosphate in angiotensin II target tissues. In: Journal of Biological Chemistry. 1987 ; Vol. 262, No. 3. pp. 1010-1015.
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abstract = "Many cells (including angiotensin II target cells) respond to external stimuli with accelerated hydrolysis of phosphatidylinositol 4,5-bisphosphate, generating 1,2-diacylglycerol and inositol 1,4,5-trisphosphate, a rapidly diffusible and potent Ca2+-mobilizing factor. Following its production at the plasma membrane level, inositol 1,4,5-trisphosphate is believed to interact with specific sites in the endoplasmic reticulum and triggers the release of stored Ca2+. Specific receptor sites for inositol 1,4,5-trisphosphate were recently identified in the bovine adrenal cortex and have been further characterized in the adrenal cortex and other target tissues. The inositol 1,4,5-trisphosphate-binding sites are saturable and present in low concentration (104 ± 48 fmol/mg protein) and exhibit high affinity for inositol 1,4,5-trisphosphate (K(d) 1.7 ± 0.6 nM). Their ligand specificity is illustrated by their low affinity for inositol 1,4-bisphosphate (K(d) ~ 10-7 M), inositol 1-phosphate and phytic acid (K(d) ~ 10-4 M), fructose 1,6-bisphosphate and 2,3-bisphosphoglycerate (K(d) ~ 10-3 M), with no detectable affinity for inositol 1-phosphate and myo-inositol. These binding sites are distinct from the degradative enzyme, inositol trisphosphate phosphatase, which has a much lower affinity for inositol trisphosphate (K(m) = 17 μM). Furthermore, submicromolar concentrations of inositol 1,4,5-trisphosphate evoked a rapid release of Ca2+ from nonmitochondrial ATP-dependent storage sites in the adrenal cortex. Specific and saturable binding sites for inositol 1,4,5-trisphosphate were also observed in the anterior pituitary (K(d) = 0.87 ± 0.31 nM, B(max) = 14.8 ± 9.0 fmol/mg protein) and in the liver (K(d) = 1.66 ± 0.7 nM, B(max) = 147 ± 24 fmol/mg protein). These data suggest that the binding sites described in this study are specific receptors through which inositol 1,4,5-trisphosphate mobilizes Ca2+ in target tissues for angiontensin II and other calcium-dependent hormones.",
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AU - Catt, K. J.

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N2 - Many cells (including angiotensin II target cells) respond to external stimuli with accelerated hydrolysis of phosphatidylinositol 4,5-bisphosphate, generating 1,2-diacylglycerol and inositol 1,4,5-trisphosphate, a rapidly diffusible and potent Ca2+-mobilizing factor. Following its production at the plasma membrane level, inositol 1,4,5-trisphosphate is believed to interact with specific sites in the endoplasmic reticulum and triggers the release of stored Ca2+. Specific receptor sites for inositol 1,4,5-trisphosphate were recently identified in the bovine adrenal cortex and have been further characterized in the adrenal cortex and other target tissues. The inositol 1,4,5-trisphosphate-binding sites are saturable and present in low concentration (104 ± 48 fmol/mg protein) and exhibit high affinity for inositol 1,4,5-trisphosphate (K(d) 1.7 ± 0.6 nM). Their ligand specificity is illustrated by their low affinity for inositol 1,4-bisphosphate (K(d) ~ 10-7 M), inositol 1-phosphate and phytic acid (K(d) ~ 10-4 M), fructose 1,6-bisphosphate and 2,3-bisphosphoglycerate (K(d) ~ 10-3 M), with no detectable affinity for inositol 1-phosphate and myo-inositol. These binding sites are distinct from the degradative enzyme, inositol trisphosphate phosphatase, which has a much lower affinity for inositol trisphosphate (K(m) = 17 μM). Furthermore, submicromolar concentrations of inositol 1,4,5-trisphosphate evoked a rapid release of Ca2+ from nonmitochondrial ATP-dependent storage sites in the adrenal cortex. Specific and saturable binding sites for inositol 1,4,5-trisphosphate were also observed in the anterior pituitary (K(d) = 0.87 ± 0.31 nM, B(max) = 14.8 ± 9.0 fmol/mg protein) and in the liver (K(d) = 1.66 ± 0.7 nM, B(max) = 147 ± 24 fmol/mg protein). These data suggest that the binding sites described in this study are specific receptors through which inositol 1,4,5-trisphosphate mobilizes Ca2+ in target tissues for angiontensin II and other calcium-dependent hormones.

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