Regulation of phosphoinositide breakdown by guanine nucleotides

Litosch, Irene; Fain, John N.

doi:10.1016/0024-3205(86)90529-1

Cited by 162 publications

(64 citation statements)

References 58 publications

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“…The mechanism whereby PTH and its receptor couple to both adenylate cyclase and phospholipase C also remains to be elucidated. Receptor coupling to adenylate cyclase is through the guanine nucleotide binding protein (G, reference 50). The -alpha subunit of G, confers the stimulatory effect, but the betagamma subunit may induce an inhibitory effect on another guanine nucleotide binding protein (Gi).…”

Section: Resultsmentioning

confidence: 99%

Stimulation of inositol trisphosphate and diacylglycerol production in renal tubular cells by parathyroid hormone.

Hruska¹,

Moskowitz²,

Esbrit³

et al. 1987

J. Clin. Invest.

232

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Section: Resultsmentioning

confidence: 99%

Stimulation of inositol trisphosphate and diacylglycerol production in renal tubular cells by parathyroid hormone.

Hruska¹,

Moskowitz²,

Esbrit³

et al. 1987

J. Clin. Invest.

232

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“…shown to serve as a substrate for pertussis toxin-catalyzed ADP-ribosylation in many (30,31) but not all (32,33) systems. In contrast to EGF-stimulated PLC activity in the A43 1 cell line, which is not inhibited by pertussis toxin (34), the G protein described herein is pertussis toxin sensitive (Fig.…”

Section: Discussionmentioning

confidence: 99%

Epidermal growth factor-stimulated phosphoinositide hydrolysis in cultured rat inner medullary collecting tubule cells. Regulation by G protein, calcium, and protein kinase C.

Teitelbaum

Strasheim²,

Berl³

1990

J. Clin. Invest.

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Epidermal growth factor (EGF) exhibits specific saturable binding to cultured rat inner medullary collecting tubule cells and stimulates inositol trisphosphate (IP3) production by these cells in a dose-dependent fashion. EGF-stimulated IP3 production is enhanced by GTP-ys or AJF4 and is inhibited by GDPBs or pertussis toxin. Alterations in extracellular Ca2" have no effect on either basal or EGF-stimulated IP3 production. Similarly, treatment with EGTA which decreases cytosolic Ca" is without effect. In contrast, treatment with ionomycin which increases cytosolic Ca2" has no effect on basal IP3 production but enhances the response to EGF. Activation of protein kinase C inhibits IP3 production in response to either EGF or AIF4. These studies demonstrate the occurrence of EGF-stimulated phospholipase C activity in the rat inner medullary collecting duct. Stimulation by EGF is transduced by a pertussis toxinsensitive G protein, unaffected by alterations in extracellular Ca2+, insensitive to a decrement in cytosolic Ca`., enhanced by an increase in cytosolic Ca2+, and inhibited by protein kinase C. (J. Clin.

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“…In the last few years, ample functional evidence has been presented that receptor-mediated activation of phospholipase C by hormones and neurotransmitters involves the intermediate action of guanine nucleotide-binding proteins (Gproteins) [8][9][10], located at the inner surface of the plasma membrane. The nature of the phospholipase C-coupling G-protein(s) has not been identified so far.…”

Section: Introductionmentioning

confidence: 99%

Stimulation and inhibition of human platelet membrane high‐affinity GTPase by neomycin

Herrmann¹,

Jakobs²

1988

FEBS Letters

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The effect of the inositol phospholipid-binding antibiotic neomycin was studied on high-affinity GTPase in human platelet membranes. At low concentrations (up to 1 mM), neomycin by itself stimulated a high-affinity GTPas¢. This GTPase stimulation was additive with that caused by the hormonal factors, prostaglandin E 1 and epinephrine, but not with thrombin. At concentrations higher than 1 raM, neomycin reduced control GTPas¢ activity and eliminated the stimulation caused by thrombin. The data suggest that neomycin by a presently unknown mechanism can regulate activity states of signal transducing GTP-binding proteins.

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Regulation of phosphoinositide breakdown by guanine nucleotides

Cited by 162 publications

References 58 publications

Stimulation of inositol trisphosphate and diacylglycerol production in renal tubular cells by parathyroid hormone.

Stimulation of inositol trisphosphate and diacylglycerol production in renal tubular cells by parathyroid hormone.

Epidermal growth factor-stimulated phosphoinositide hydrolysis in cultured rat inner medullary collecting tubule cells. Regulation by G protein, calcium, and protein kinase C.

Stimulation and inhibition of human platelet membrane high‐affinity GTPase by neomycin

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