Transient inositol (1,4,5) trisphosphate accumulation under vasopressin stimulation in WRK1 cells: correlation with intracellular calcium mobilization

doi:10.1016/0006-291X(89)92201-8

Biochemical and Biophysical Research Communications

Volume 159, Issue 3, 31 March 1989, Pages 953-960

https://doi.org/10.1016/0006-291X(89)92201-8 Get rights and content

Abstract

In the rat mammary tumoral cell line (WRK1 cells), vasopressin was previously described to stimulate a phospholipase C. In this study, we have analysed the effect of vasopressin both on intracellular calcium mobilization and on the accumulation of inositol phosphates. Maximal concentration of vasopressin simultaneously induces an accumulation of Ins(1,4,5)P3 and a rise of intracellular calcium concentration. Both these two phenomena are transient and exhibit similar kinetics. A sustained accumulation of InsP2, Ins(1,3,4)P3 and InsP are observed later. Yet no stimulation of InsP4 can be objectified. These results indicate that Ins(1,4,5)P3 is the major inositol phosphate involved in intracellular calcium mobilization.

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1995, Insect Biochemistry and Molecular Biology
Inositol 1-monophosphate (Ins₍₁₎)P1), and together inositol 1,4-bisphosphate (Ins_1,4)P2) and inositol 4-monophosphate (Ins₍₄₎P1) were rapidly (5s) generated in the presence of low concentrations of neuroparsin (NP), likely by hydrolysis of phosphatidylinositol monophosphate (PIP) and phosphatidylinositol (PI) substrates with a phospholipase C (PLC). High concentrations of NP activated another membrane effector which hydrolyzed phosphatidylinositol 4,5-bisphosphate (PIP2) and produced inositol 1,4,5-trisphosphate which is either dephosphorylated in Ins₍₄₎P1 or phosphorylated in inositol 1,3,4,5-tetrakisphosphate, then rapidly dephosphorylated in inositol 1,3,4-trisphosphate and finally in Ins₍₁₎P1. Both PLC are Ca²⁺-dependent. Their existence possibly reflects the involvement of two distinct transduction mechanisms for the antidiuretic signal of NP according to its concentration. Beyond a previous action of NP demonstrated on the opening of L-type Ca²⁺ channels, experiments show the early participation of other types of Ca²⁺ channels.
Arachidonic acid and prostaglandin E<inf>2</inf> stimulate phospholipase C activity in the rectum of the African locust, Locusta migratoria migratorioides
1995, Journal of Insect Physiology
Arachidonic acid (20:4n-6) and its metabolite PGE₂ stimulated fluid reabsorption in the African locust rectum and enhanced phospholipase C (PLC) activity, resulting in an increase in inositol phosphate production (primarily that of inositol 1,4,5-trisphosphate). This effect resulted in an elevation in cytosolic free Ca²⁺ concentrations in epithelial cells via the opening of L-type channels, a mechanism showed by neuroparsin, an antidiuretic neuronal hormone. The effects of 20:4n-6 and PGE₂ were abolished after treatment with polymyxin B, a protein kinase C (PKC) inhibitor. Thus, these data are consistent with a stimulation of PKC by 20:4n-6 and PGE₂ inducing, in turn, a regulation of the neuroparsin-induced PLC activity. The presence of 20:4n-6 (which separated in preliminary experiments from locust rectal phospholipids) as free fatty acid, should result from phospholipase A₂ activity was demonstrated in the experiments.
Action of linoleic acid on phospholipase C activity at the rectal level of the African locust under the control of protein kinase C
1995, Comparative Biochemistry and Physiology. Part C: Comparative
Linoleic acid (18:2n-6), linolenic acid and eicosatrienoic acid stimulated fluid reabsorption in locust rectum. Only 18:2n-6 was able to enhance phospholipase C activity, inositol_(1,4,5) trisphosphate production and to increase cytosolic free Ca²⁺ concentrations in epithelial cells via the opening of L-type Ca²⁺ channels. These effects resemble those exerted by neuroparsin, an antidiuretic neuronal hormone extracted from the storage lobes of the locust corpora cardiaca. As for neuroparsin, the effects of 18:2n-6 were abolished after pre-treatment with the protein kinase C inhibitor, polymyxin B. The results were consistent with a regulation of neuroparsin-sensitive phospholipase C activity by 18:2n-6 under control of protein kinase C, possibly by increasing membrane fluidity. Cyclooxygenase inhibitors attenuated the effects of 18:2n-6. This demonstrated that the results should be produced via the metabolites of 18:2n-6 HODEs rather than the PUFA itself.
Increase in inositol tris-, pentakis- and hexakisphosphates by high K<sup>+</sup> stimulation in cultured rat cerebellar granule cells
1993, Brain Research
Effects of high K⁺ stimulation on inositol polyphosphate accumulations and intracellular free calcium concentration ([Ca²⁺]_i) were investigated in cultured rat cerebellar granule cells. When the [³H]inositol-labelled cells were stimulated with KCl, concentration-dependent accumulations of [³H]Ins(1,4,5)P₃, [³H]InsP₅ and [³H]InsP₆ were observed. Nifedipine (3 μM), a calcium channel antagonist, inhibited the high (KCl, 90 mM) K⁺-induced accumulations of these inositol polyphosphates. In Ca²⁺-depleted and EGTA-containing (0.1 mM) medium, the high K⁺-induced inositol polyphosphate accumulation were completely inhibited. Similar results were also observed in the case of [Ca²⁺]_i. These results suggest that the rise in [Ca²⁺]_i caused by activation of voltage-dependent calcium channels plays an important roles in the high K⁺-induced accumulation of [³H]Ins(1,4,5)P₃, [³H]InsP₅ and [³H]InsP₆ in cultured rat cerebellar granule cells.
Characteristics of inositol polyphosphate metabolism in cultured adrenal chromaffin cells
1993, Progress in Neuropsychopharmacology and Biological Psychiatry
Sasakawa, Nobuyuki, Toshio Nakaki and Ryuichi Kato: Characteristics of Inositol polyphosphate Metabolism in cultured adrenal chromaffin cells. Prog. NeuroPsychopharmacol. & Biol. Psychiat. 1993, : 17(5): 825–834.
- 1.
  1. Nicotine, high K⁺ and maitotoxin caused the inositol polyphosphate accumulation concomitant with ⁴⁵Ca²⁺ uptake.
- 2.
  2. Angiotensin II (Ang II) and ATP induced the inositol polyphosphate accumulation without ⁴⁵Ca²⁺ uptake.
- 3.
  3. Nifedipine-treatment and Ca²⁺-deprivation inhibited the high K⁺-induced inositol polyphosphate accumulation but failed to inhibit the Ang II-induced inositol polyphosphate accumulation.
- 4.
  4. 12-O-tetradecanoylphorbol-13-acetate inhibited the Ang II-induced inositol polyphosphate accumulation but failed to inhibit the high K⁺-induced one
- 5.
  5. These results suggest that the formation of inositol polyphosphates may be regulated by two mechanisms i.e. Ca²⁺ uptake-dependent mechanisms represented by high K⁺, and Ca²⁺ uptake-independent mechanisms represented by Ang II.
Pharmacological characterization of inositol 1,4,5,-trisphosphate binding sites: relation to Ca<sup>2+</sup> release
1992, European Journal of Pharmacology: Molecular Pharmacology
Two subcellular fractions, one enriched in plasma membranes and the other in endoplasmic reticulum membranes, were obtained from WRK₁ cells using a combination of differential centrifugations and percoll gradient fractionation. Specific inositol 1,4,5-triphosphate (Ins(1,4,5)P₃) binding sites were detected in these two preparations. Endoplasmic reticulum membranes exhibited a binding capacity which was about 5-fold higher than that of plasma membranes. Dose-dependent Ins(1,4,5)P₃ binding was determined. Experimental data obtained with endoplasmic reticulum membranes could be adequately fitted with a two-site model (a high-affinity binding site with K_d and B_max values of 0.7 ± 0.15 nM and 12.9 ± 5 fmol/mg protein and a low-affinity binding site with K_d and B_max values of 44.2 ± 14.6 nM and 143 ± 43 fmol/mg protein). Both the high- and low-affinity binding sites were selective for Ins(1,4,5)P₃. Besides Ins(1,4,5)P₃, Ins(1,3,4,5)P₄ also discriminated between the two populations of sites while heparin interacted with the high- and low-affinity binding sites with the same affinity. Ins(1,4,5)P₃-induced calcium release from endoplasmic reticulum vesicles was determined by monitoring the calcium concentration in the extravesicular compartment with fura-2. Under experimental conditions where the degradation of Ins(1,4,5)P₃ was reduced (incubation at 0°C), a high-affinity Ins(1,4,5)P₃-induced calcium release (apparent K_act around 20 nM) could be demonstrated. These results suggest that in WRK₁ cells, the endoplasmic reticulum is a major site for Ins(1,4,5)P₃ action and that the high-affinity binding sites located on the endoplasmic reticulum membranes may contribute to the physiological regulation of the cytosolic free calcium concentration.

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Transient inositol (1,4,5) trisphosphate accumulation under vasopressin stimulation in WRK1 cells: correlation with intracellular calcium mobilization

Abstract

J. Biol. Chem

Biochimie

J. Biol. Chem

J. Biol. Chem

Biochem. Biophys. Res. Commun

J. Biol. Chem

J. Biol. Chem

FEBS Lett

J. Biol. Chem

Ann. Rev. Biochem

Nature

Nature

Biochem. J

Biochem. J

Transient inositol (1,4,5) trisphosphate accumulation under vasopressin stimulation in WRK₁ cells: correlation with intracellular calcium mobilization