Ethanol stimulates shape change in human platelets by activation of phosphoinositide-specific phospholipase C

Rubin, Raphael; Ponnappa, Biddanda C.; Thomas, Andrew P.; Hoek, Jan B.

doi:10.1016/0003-9861(88)90472-9

Cited by 42 publications

(21 citation statements)

References 39 publications

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“…Ethanol could also stimulate PKC by several other mechanisms. Ethanol elevates intracellular Ca2+ in PC 12 cells (Rabe and Weight, 1988), hepatocytes (Hoek et al, 1987), and platelets (Rubin et al, 1988). The basis for this effect in PC12 cells is not known, but in platelets (Rubin et al, 1988) and hepatocytes (Hoek et al, 1987) ethanol transiently stimulates phosphati-dylinositol4,5-bisphosphate hydrolysis.…”

Section: Discussionmentioning

confidence: 99%

“…Ethanol elevates intracellular Ca2+ in PC 12 cells (Rabe and Weight, 1988), hepatocytes (Hoek et al, 1987), and platelets (Rubin et al, 1988). The basis for this effect in PC12 cells is not known, but in platelets (Rubin et al, 1988) and hepatocytes (Hoek et al, 1987) ethanol transiently stimulates phosphati-dylinositol4,5-bisphosphate hydrolysis. Hydrolysis of phosphatidylinositol 4,5-bisphosphate generates inositol 1,4,5-tnsphosphate, which releases stored intracellular Caz+ into the cytosol, and diacylglycerol, which activates PKC (Berridge and Irvine, 1984).…”

Section: Discussionmentioning

confidence: 99%

“…Hydrolysis of phosphatidylinositol 4,5-bisphosphate generates inositol 1,4,5-tnsphosphate, which releases stored intracellular Caz+ into the cytosol, and diacylglycerol, which activates PKC (Berridge and Irvine, 1984). Consequently, in platelets, ethanol induces the phosphorylation of a 40-kDa protein that is a known substrate for PKC (Rubin et al, 1988). Therefore, in some cell types, ethanol enhances PKC activation by stimulating phosphatidylinositol 4,5-bisphosphate hydrolysis and diacylglycerol formation.…”

Section: Discussionmentioning

confidence: 99%

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Protein Kinase C Participates in Up‐Regulation of Dihydropyridine‐Sensitive Calcium Channels by Ethanol

Messing

Sneade

Savidge

1990

Journal of Neurochemistry

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Exposure to ethanol for several days increases the expression of dihydropyridine-sensitive, voltage-dependent Ca2+ channels in brain and in the neural cell line PC12. Since protein phosphorylation is a major mechanism by which ion channels are regulated, we used protein kinase inhibitors to investigate whether ethanol-induced up-regulation of Ca2+ channels involves activation of a protein kinase. Sphingosine and polymixin B, which inhibit protein kinase C and calmodulin-dependent kinases, prevented the enhancement of 45Ca2+ uptake induced by exposure of PC12 cells to ethanol for 4 days. In addition, sphingosine blocked the ability of ethanol to increase the number of [3H]dihydropyridine binding sites in PC12 cell membranes. Sphingosine's effect was prevented by simultaneous exposure to phorbol 12,13-dibutyrate, a potent activator of protein kinase C. Therefore, protein kinase C appears to be involved in the up-regulation of dihydropyridine-sensitive Ca2+ channels during prolonged exposure to ethanol.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Protein Kinase C Participates in Up‐Regulation of Dihydropyridine‐Sensitive Calcium Channels by Ethanol

Messing

Sneade

Savidge

1990

Journal of Neurochemistry

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“…In nonembryonic cells, ethanol releases intracellular Ca 2+ through its interaction with a G protein, which activates PLC to generate IP 3 [22,23]. Although ethanol can directly stimulate G-protein induction of PLC activity and increase the rate of PLC activation at submaximal levels of GTP--y-S [24,25], PLC can be activated through receptors coupled to either a G protein or tyrosine kinase ( Fig.…”

Section: Introductionmentioning

confidence: 99%

Regulation of Blastocoele Formation by Intracellular Calcium Release is Mediated through a Phospholipase C-Dependent Pathway in Mice1

Stachecki¹,

Armant²

1996

Biology of Reproduction

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Calcium signaling plays a critical role in the regulation of mouse preimplantation development, in part through the activation of calmodulin. Calcium transients in mouse morulae appear to be generated predominantly through the production of inositol 1,4,5-trisphosphate (IP3) by phospholipase C (PLC). IP3 receptors predominate in mouse embryos as regulators of calcium release. Exposure to the PLC inhibitors ET-18-OCH3 or U73122 resulted in a dose-dependent, reversible inhibition of cavitation, while the inactive analogue U73343 did not alter the rate of cavitation, as compared to that in controls. U73122 inhibited the release of calcium from intracellular stores after exposure to ethanol or lysophosphatidic acid, suggesting that PLC is required for blastocoele formation in the mouse and that calcium signaling may be PLC-dependent. In addition to IP3, PLC activation generates diacylglycerol, which stimulates protein kinase C (PKC) and could also alter the rate of embryonic development. However, activation of PKC with phorbol ester or synthetic diacylglycerol was not sufficient to accelerate development, although embryo culture in medium containing PKC inhibitors did delay cavitation. Exposure to a PKC inhibitor during ethanol-induced calcium signaling did not attenuate the ensuing acceleration of cavitation. These results demonstrate that a PLC-mediated signaling pathway is required for blastocoele formation and that the generation of IP3, but not diacylglycerol, is critical for accelerating preimplantation development.

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“…The dose of ethanol was set after previous studies using human platelets (Rubin, 1989;Rubin et al 1988;Wakabayashi and Marumo, 2002), in which the major inhibitory effects of ethanol in vitro on platelet activation are generally observed in the order of 100 mM (Wakabayashi and Marumo, 2002). Such higher concentrations of ethanol are unphysiological, but are required for inhibiting platelet aggregation in vitro possibly because ethanol has combined effects in vivo with other inhibitors of platelet response such as increasing serum level of prostacyclin or adenosine (Rubin and Rand, 1994).…”

Section: Measurement Of Platelet Aggregation and [Ca 21 ] Imentioning

confidence: 99%

Inhibition of PAR4 Signaling Mediates Ethanol‐Induced Attenuation of Platelet Function In Vitro

Kasuda

Sakurai

Shima

et al. 2006

Alcoholism Clin & Exp Res

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Ethanol stimulates shape change in human platelets by activation of phosphoinositide-specific phospholipase C

Cited by 42 publications

References 39 publications

Protein Kinase C Participates in Up‐Regulation of Dihydropyridine‐Sensitive Calcium Channels by Ethanol

Protein Kinase C Participates in Up‐Regulation of Dihydropyridine‐Sensitive Calcium Channels by Ethanol

Regulation of Blastocoele Formation by Intracellular Calcium Release is Mediated through a Phospholipase C-Dependent Pathway in Mice1

Inhibition of PAR4 Signaling Mediates Ethanol‐Induced Attenuation of Platelet Function In Vitro

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