Relevant bibliographies by topics / (Pa˜dag.)

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Academic literature on the topic '(Pa˜dag.)'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "(Pa˜dag.)"

1

CLEJAN, Sanda, Conrad MALLIA, David VINSON, Robert DOTSON, and Barbara S. BECKMAN. "Erythropoietin stimulates G-protein-coupled phospholipase D in haematopoietic target cells." Biochemical Journal 314, no. 3 (March 15, 1996): 853–60. http://dx.doi.org/10.1042/bj3140853.

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A murine haematopoietic stem-cell line, B6SUt.EP, responsive to erythropoietin (EPO), has been found to exhibit both early and late changes in diacylglycerol (DAG) and phosphatidic acid (PA) as measured by HPLC and TLC. DAG levels peaked at 5 s with a 28.1% increase compared with control levels (from 17.3 to 22.2 pmol/106 cells) with a later peak at 30 min (84.2% increase from 17.3 to 31.9 pmol). These changes were concentration-dependent from 0.025 to 10 units/ml EPO (5 s, EC50 = 0.82 unit/ml; 30 min, EC50 = 0.10 unit/ml). In addition, PA levels increased 752.3% compared with control levels (from 8.6 to 64.7 μg/106 cells) with an early peak at 20 s, as measured by both HPLC and TLC (5 s, EC50 = 0.07 unit/ml). G-protein regulation was investigated by studying the effects of the non-hydrolysable GTP analogue guanosine 5´-[γ-thio]triphosphate (GTP[S]) on PA synthesis. The addition of GTP[S] (10 μM) in permeabilized cells increased PA content from 6.3 μg to 48.6 μg per 106 cells. In the presence of EPO and GTP[S], PA levels increased to 64.8 μg. An antagonist of G-proteins, guanosine 5´-[β-thio]diphosphate (GDP[S]), had no effect on control levels of PA (5.9 μg/106 cells) but blocked the effect of EPO on PA (30.6 μg/106 cells). Thus, EPO stimulated both lipid second messengers, DAG and PA. Our results demonstrate DAG kinetics to be biphasic, as observed with a high concentration of EPO, or monophasic, as observed with low concentrations of EPO. The PA accumulation preceding that of DAG in the slower and sustaining phase suggests that PA was not derived from DAG. This was confirmed by the stimulation of PA (without ATP) by GTP[S], effectively excluding phosphorylation of DAG by DAG kinase in the formation of PA. In addition, phospholipase D (PLD) activation was demonstrated with a maximal increase in phosphatidylethanol at 5 min, suggesting that EPO increases PA via a guanine nucleotide-binding protein coupled to PLD. The temporal relationship of the evolution of PA and DAG is further strengthened by experiments with ethanol and propranolol as inhibitors of the DAG/PA phosphohydrolase reaction and R59022 as an inhibitor of the DAG kinase reaction.
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2

Ganesan, Suriakarthiga, Brittney N. Shabits, and Vanina Zaremberg. "Tracking Diacylglycerol and Phosphatidic Acid Pools in Budding Yeast." Lipid Insights 8s1 (January 2015): LPI.S31781. http://dx.doi.org/10.4137/lpi.s31781.

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Phosphatidic acid (PA) and diacylglycerol (DAG) are key signaling molecules and important precursors for the biosynthesis of all glycerolipids found in eukaryotes. Research conducted in the model organism Saccharomyces cerevisiae has been at the forefront of the identification of the enzymes involved in the metabolism and transport of PA and DAG. Both these lipids can alter the local physical properties of membranes by introducing negative curvature, but the anionic nature of the phosphomonoester headgroup in PA sets it apart from DAG. As a result, the mechanisms underlying PA and DAG interaction with other lipids and proteins are notoriously different. This is apparent from the analysis of the protein domains responsible for recognition and binding to each of these lipids. We review the current evidence obtained using the PA-binding proteins and domains fused to fluorescent proteins for in vivo tracking of PA pools in yeast. In addition, we present original results for visualization of DAG pools in yeast using the C1 domain from mammalian PKCδ. An emerging first cellular map of the distribution of PA and DAG pools in actively growing yeast is discussed.
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3

Song, J. G., L. M. Pfeffer, and D. A. Foster. "v-Src increases diacylglycerol levels via a type D phospholipase-mediated hydrolysis of phosphatidylcholine." Molecular and Cellular Biology 11, no. 10 (October 1991): 4903–8. http://dx.doi.org/10.1128/mcb.11.10.4903.

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Activating the protein-tyrosine kinase of v-Src in BALB/c 3T3 cells results in rapid increases in the intracellular second messenger, diacylglycerol (DAG). v-Src-induced increases in radiolabeled DAG were most readily detected when phospholipids were prelabeled with myristic acid, which is incorporated predominantly into phosphatidylcholine. Consistent with this observation, v-Src increased the level of intracellular choline. No increase in DAG was observed when cells were prelabeled with arachidonic acid, which is incorporated predominantly into phosphatidylinositol. Inhibiting phosphatidic acid (PA) phosphatase, which hydrolyzes PA to DAG, blocked v-Src-induced DAG production and enhanced PA production, implicating a type D phospholipase. Consistent with the involvement of a type D phospholipase, v-Src increased transphosphatidylation activity, which is characteristic of type D phospholipases. Thus, v-Src-induced increases in DAG most likely result from the activation of a type D phospholipase/PA phosphatase-mediated signaling pathway.
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4

Song, J. G., L. M. Pfeffer, and D. A. Foster. "v-Src increases diacylglycerol levels via a type D phospholipase-mediated hydrolysis of phosphatidylcholine." Molecular and Cellular Biology 11, no. 10 (October 1991): 4903–8. http://dx.doi.org/10.1128/mcb.11.10.4903-4908.1991.

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Activating the protein-tyrosine kinase of v-Src in BALB/c 3T3 cells results in rapid increases in the intracellular second messenger, diacylglycerol (DAG). v-Src-induced increases in radiolabeled DAG were most readily detected when phospholipids were prelabeled with myristic acid, which is incorporated predominantly into phosphatidylcholine. Consistent with this observation, v-Src increased the level of intracellular choline. No increase in DAG was observed when cells were prelabeled with arachidonic acid, which is incorporated predominantly into phosphatidylinositol. Inhibiting phosphatidic acid (PA) phosphatase, which hydrolyzes PA to DAG, blocked v-Src-induced DAG production and enhanced PA production, implicating a type D phospholipase. Consistent with the involvement of a type D phospholipase, v-Src increased transphosphatidylation activity, which is characteristic of type D phospholipases. Thus, v-Src-induced increases in DAG most likely result from the activation of a type D phospholipase/PA phosphatase-mediated signaling pathway.
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5

Farese, R. V., D. R. Cooper, T. S. Konda, G. Nair, M. L. Standaert, J. S. Davis, and R. J. Pollet. "Mechanisms whereby insulin increases diacylglycerol in BC3H-1 myocytes." Biochemical Journal 256, no. 1 (November 15, 1988): 175–84. http://dx.doi.org/10.1042/bj2560175.

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We previously suggested that insulin increases diacylglycerol (DAG) in BC3H-1 myocytes, both by increases in synthesis de novo of phosphatidic acid (PA) and by hydrolysis of non-inositol-containing phospholipids, such as phosphatidylcholine (PC) and phosphatidylethanolamine (PE). We have now evaluated these insulin effects more thoroughly, and several potential mechanisms for their induction. In studies of the effect on PA synthesis de novo, insulin stimulated [2-3H]glycerol incorporation into PA, DAG, PC/PE and total glycerolipids of BC3H-1 myocytes, regardless of whether insulin was added simultaneously with, or after 2 h or 3 or 10 days of prelabelling with, [2-3H]glycerol. In prelabelled cells, time-related changes in [2-3H]glycerol labelling of DAG correlated well with increases in DAG content: both were maximal in 30-60 s and persisted for 20-30 min. [2-3H]Glycerol labelling of glycerol 3-phosphate, on the other hand, was decreased by insulin, presumably reflecting increased utilization for PA synthesis. Glycerol 3-phosphate concentrations were 0.36 and 0.38 mM before and 1 min after insulin treatment, and insulin effects could not be explained by increases in glycerol 3-phosphate specific radioactivity. In addition to that of [2-3H]glycerol, insulin increased [U-14C]glucose and [1,2,3-3H]glycerol incorporation into DAG and other glycerolipids. Effects of insulin on [2-3H]glycerol incorporation into DAG and other glycerolipids were half-maximal and maximal at 2 nM- and 20 nM-insulin respectively, and were not dependent on glucose concentration in the medium, extracellular Ca2+ or protein synthesis. Despite good correlation between [3H]DAG and DAG content, calculated increases in DAG content from glycerol 3-phosphate specific radioactivity (i.e. via the pathway of PA synthesis de novo) could account for only 15-30% of the observed increases in DAG content. In addition to increases in [3H]glycerol labelling of PC/PE, insulin rapidly (within 30 s) increased PC/PE labelling by [3H]arachidonic acid, [3H]myristic acid, and [14C]choline. Phenylephrine, ionophore A23187 and phorbol esters did not increase [2-3H]glycerol incorporation into DAG or other glycerolipids in 2-h-prelabelling experiments; thus activation of the phospholipase C which hydrolyses phosphatidylinositol, its mono- and bis-phosphate, Ca2+ mobilization, and protein kinase C activation, appear to be ruled out as mechanisms to explain the insulin effect on synthesis de novo of PA, DAG and PC.(ABSTRACT TRUNCATED AT 400 WORDS)
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6

BECKMAN, Barbara S., Conrad MALLIA, and Sanda CLEJAN. "Molecular species of phospholipids in a murine stem-cell line responsive to erythropoietin." Biochemical Journal 314, no. 3 (March 15, 1996): 861–67. http://dx.doi.org/10.1042/bj3140861.

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The generation of the lipid signalling molecules, diacylglycerol (DAG) and phosphatidic acid (PA), has been implicated in the transduction events essential for proliferation of murine B6SUt.EP stem cells responsive to erythropoietin (EPO). Some of the responses were rapid and transient while others were slower and sustained. In an attempt to better understand the biphasic nature of DAG and PA appearance in response to EPO, an analysis of the molecular species of DAG, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylinositol (PI), and PA in control and EPO-treated B6SUt.EP cells was made by HPLC and TLC. Fifteen to eighteen species were identified, which were increased non-uniformly by 0.2 unit/ml EPO. Greater increases (×6) were observed in 16:0,20:4 and 18:0,20:4 DAGs than in other species. The molecular species profiles of the stimulated DAGs were compared with the profiles of molecular species contained in the phospholipids. Comparison of the increase in DAG species caused by EPO with the molecular species present in PC and PI showed both PI and PC as the source of the fast DAG accumulation and only PC as the source of the slow DAG accumulation. PE was involved in both phases. We found a consistent formation of ethanolamine over time, in larger amounts than choline, providing strong evidence that, in addition to PC, PE is a major substrate. In addition, changes in molecular species of PA in response to EPO suggest that PI cannot account for the mass of PA formed during the first 30 s incubation with EPO, nor for PA formed during 30 min with EPO. It is concluded that the majority of PA was formed by a direct action of phospholipase D on PC.
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7

Farah, Carole A., Ikue Nagakura, Daniel Weatherill, Xiaotang Fan, and Wayne S. Sossin. "Physiological Role for Phosphatidic Acid in the Translocation of the Novel Protein Kinase C Apl II in Aplysia Neurons." Molecular and Cellular Biology 28, no. 15 (May 27, 2008): 4719–33. http://dx.doi.org/10.1128/mcb.00178-08.

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ABSTRACT In Aplysia californica, the serotonin-mediated translocation of protein kinase C (PKC) Apl II to neuronal membranes is important for synaptic plasticity. The orthologue of PKC Apl II, PKCε, has been reported to require phosphatidic acid (PA) in conjunction with diacylglycerol (DAG) for translocation. We find that PKC Apl II can be synergistically translocated to membranes by the combination of DAG and PA. We identify a mutation in the C1b domain (arginine 273 to histidine; PKC Apl II-R273H) that removes the effects of exogenous PA. In Aplysia neurons, the inhibition of endogenous PA production by 1-butanol inhibited the physiological translocation of PKC Apl II by serotonin in the cell body and at the synapse but not the translocation of PKC Apl II-R273H. The translocation of PKC Apl II-R273H in the absence of PA was explained by two additional effects of this mutation: (i) the mutation removed C2 domain-mediated inhibition, and (ii) the mutation decreased the concentration of DAG required for PKC Apl II translocation. We present a model in which, under physiological conditions, PA is important to activate the novel PKC Apl II both by synergizing with DAG and removing C2 domain-mediated inhibition.
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8

Peterson, M. W., and M. E. Walter. "Calcium-activated phosphatidylcholine-specific phospholipase C and D in MDCK epithelial cells." American Journal of Physiology-Cell Physiology 263, no. 6 (December 1, 1992): C1216—C1224. http://dx.doi.org/10.1152/ajpcell.1992.263.6.c1216.

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Calcium ionophore exposure generates diglycerides (DAG) from phosphatidylcholine (PC) hydrolysis in Madin-Darby canine kidney (MDCK) epithelial cells. This study compares calcium ionophore-activated PC hydrolysis with the previously described phorbol ester-stimulated PC hydrolysis pathway using MDCK cells labeled with [14C]-linoleic acid. Lipid species were measured using thin-layer chromatography. DAG resulted in part from PC hydrolysis because DAG increased in cells labeled with [palmitoyl-2-14C]phosphatidylcholine. Neither protein kinase C (PKC) inhibitors nor PKC depletion affected the ionomycin (IONO)-induced increase in DAG. Ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid prevented the increased DAG after IONO but not after phorbol 12,13-dibutyrate (PDBu) exposure. The EGTA effect was reversed by adding excess calcium but was not reversed by adding excess Mg2+. IONO exposure also increased phosphatidic acid (PA) production. The PA was produced by phospholipase D (PLD) because phosphatidylethanol was produced when IONO was added to the cells in the presence of ethanol. Although increasing concentrations of ethanol resulted in progressively less PA, it had no effect on increased DAG after IONO exposure at any time point tested. These data are consistent with both increased phospholipase C (PLC) and increased PLD activity following ionomycin. In contrast to IONO exposure, ethanol completely prevented the increase in DAG after PDBu exposure, consistent with DAG produced by PLD activation. These results demonstrate that calcium activates both PC-specific PLC and PLD in MDCK cells and that the calcium-activated pathway is independent of the previously described PKC activation pathways.
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9

Gharbi, Severine I., Esther Rincón, Antonia Avila-Flores, Pedro Torres-Ayuso, María Almena, María Angeles Cobos, Juan Pablo Albar, and Isabel Mérida. "Diacylglycerol kinase ζ controls diacylglycerol metabolism at the immunological synapse." Molecular Biology of the Cell 22, no. 22 (November 15, 2011): 4406–14. http://dx.doi.org/10.1091/mbc.e11-03-0247.

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Diacylglycerol (DAG) generation at the T cell immunological synapse (IS) determines the correct activation of antigen-specific immune responses. DAG kinases (DGKs) α and ζ act as negative regulators of DAG-mediated signals by catalyzing DAG conversion to phosphatidic acid (PA). Nonetheless, the specific input of each enzyme and their spatial regulation during IS formation remain uncharacterized. Here we report recruitment of endogenous DGKα and DGKζ to the T cell receptor (TCR) complex following TCR/CD28 engagement. Specific DGK gene silencing shows that PA production at the activated complex depends mainly on DGKζ, indicating functional differences between these proteins. DGKζ kinase activity at the TCR is enhanced by phorbol-12-myristate-13-acetate cotreatment, suggesting DAG-mediated regulation of DGKζ responsiveness. We used GFP-DGKζ and -DGKα chimeras to assess translocation dynamics during IS formation. Only GFP-DGKζ translocated rapidly to the plasma membrane at early stages of IS formation, independent of enzyme activity. Finally, use of a fluorescent DAG sensor confirmed rapid, sustained DAG accumulation at the IS and allowed us to directly correlate membrane translocation of active DGKζ with DAG consumption at the IS. This study highlights a DGKζ-specific function for local DAG metabolism at the IS and offers new clues to its mode of regulation.
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10

Harrris, W. E., and S. L. Bursten. "Lipid A stimulates phospholipase D activity in rat mesangial cells via a G-protein." Biochemical Journal 281, no. 3 (February 1, 1992): 675–82. http://dx.doi.org/10.1042/bj2810675.

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Stimulation of mesangial cells (MC) with the bacterial endotoxin Lipid A activated two enzymes involved in lipid metabolism. First, a phospholipase D hydrolyses phosphatidylethanolamine (PE) to phosphatidic acid (PA), followed by dephosphorylation of PA to 1,2-diacylglycerol (DAG) by PA phosphohydrolase. MC or microsomes from these cells were pre-labelled with [3H]glycerol. A 30-60 s stimulation with 10-100 ng of Lipid A/ml caused a decrease in [3H]glycerol in PE and increased radioactive glycerol in PA. The enzyme responsible for this hydrolysis preferred PE containing unsaturated acyl side chains. DAG was formed from PA within the first 1 min after Lipid A stimulation. Microsomes incubated with 25 mM-NaF to inhibit phospholipase C and to stimulate GTP-binding proteins also caused PE to be converted into PA. The [3H]glycerol and acyl mass of phosphatidylcholine, phosphatidylserine and phosphatidylinositol did not change with either Lipid A or NaF. Addition of guanosine 5′-[gamma-thio]triphosphate to MC microsomes caused the rapid decrease in proportion of PE and increase in PA, followed by an increase in DAG unsaturated acyl mass. These data suggest the concurrent G-protein-dependent activation by Lipid A of a PE-directed phospholipase D and a PA phosphohydrolase.
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Books on the topic "(Pa˜dag.)"

1

Dag yig rig paʼi gab pa mṅon phyuṅ. [Zi-liṅ]: Mtsho-sṅon mi rigs dpe skrun khaṅ, 1999.

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Dag yig mkhas pa dgaʼ skyed rtsa ʼgrel. 6th ed. Lanzhou: Kan-suʼu mi rigs dpe skrun khaṅ, 1990.

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Ṅag-dbaṅ-chos-kyi-rgya-mtsho, Dpal-khaṅ. Dag yig ṅag sgron rtsa ba daṅ deʼi ʼgrel pa. [Lhasa]: Bod-ljoṅs mi dmaṅs dpe skrun khaṅ, 1990.

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Nagarjuna, Siddha. Ācārya Nāgārjunapraṇītaḥ Dharmasaṅgrahaḥ =: ʼPhags-pa Klu-sgrub kyis mdzad paʼi Chos yaṅ dag par bsdus pa. Sāranātha, Vārāṇasī: Kendrīya Ucca Tibbatī-Śikshā-Saṃsthāna, 1988.

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Nagarjuna, Siddha. Ācārya Nāgārjunapraṇītaḥ Dharmasaṅgrahaḥ =: ʾPhags-pa Klu-sgrub kyis mdzad paʾi Chos yaṅ dag par bsdus pa. Sāranātha, Vārāṇasī: Kendrīya Ucca Tibbatī-Śikshā-Saṃsthāna, 1988.

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Śa-li-ho-tra and Śa-li-ho-tra. Draṅ sroṅ chen po Śa-li-ho-tras yaṅ dag bar bsdus paʼi rtaʼi tsheʼi rig byed mthaʼ dag rjes su bstan pa źes bya ba rgyas pa bzugs so. [Lhasa]: Bod-ljoṅs mi dmaṅs dpe skrun khaṅ, 1987.

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chos kyi grags pa dpal bzang po. Sku gsum ngo sprod kyi rnam par bshad pa mdo rgyud bstan pa mthaʼ dag gi ae waṃ phyag rgya. Sarnath, Varanasi: Wā-ṇa Badzra-bidyā Dpe-mdzod-khang, 2013.

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Theg pa chen poʼi ñams len mtha dag gi gnas bsdus pa blo sbyoṅ don bdun maʼi rgya cher ʼgrel. Dharamsala: Institute of Buddhist Dialectics, 1997.

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1527-1592, Padma-dkar-po ʼBrug-chen IV, ed. Dbu ma yaṅ dag par brjod pa daṅ Dbu maʼi gźuṅ gsum gsal byed. 2nd ed. Sarnath, Varanasi: Kargyud Relief & Protection Committee, Central Institute of Higher Tibetan Studies, 2000.

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1777, Gsar-tshaṅ Sbra b., ed. Brda sprod ñi śu bdun pa rtsa ʾgrel daṅ Brda dag blo gsal ʾjug ṅogs bźugs. [Chengdu]: Si-khron mi rigs dpe skrun khaṅ, 1989.

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Book chapters on the topic "(Pa˜dag.)"

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Maurer, Petra. "Blo-bzang bstan-pa'i rgyal-mtshan: Byang chub sems mnga' ba'i bya mgrin sngon zla ba'i rtogs pa brjod pa 'khor ba mtha' dag la snying po med par mthong ba rnams kyi rna rgyan." In Kindlers Literatur Lexikon (KLL), 1–2. Stuttgart: J.B. Metzler, 2020. http://dx.doi.org/10.1007/978-3-476-05728-0_10955-1.

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Conference papers on the topic "(Pa˜dag.)"

1

SIMON, M. F., H. CHAP, and L. DOUSTE-BLAZY. "EFFECTS OF SIN 1 ON PLATELET ACTIVATION INDUCED BY THROMBIN IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643423.

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The mechanism of platelet activation is well known. The interaction of agonist such as thrombin, on specific membrane receptor induces phosphatidylinositol-specific phospholipase C activation, with a concomitant formation of two second messengers (from PIP2): inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 is able to induce a rapid discharge of Ca2+ from internal stores and Ca2+ influx through plasma membrane by unidentified Ca2+ channels linked to receptor activation. The increase of cytoplasmic free calcium concentration leads to the activation of the calcium calmodulin dependent myosine light chain kinase which phosphoryla-tes 20 kD proteins (myosine light chain). DAG is a potent activator of protein kinase C, which phosphorylates 40 kD proteins. These different pathways act in synergism.Sin 1 is a platelet aggregating inhibitor. This compound is an active metabolite of molsidomine, which activates platelet guany-late cyclase, inducing a rapid rise in cyclic GMP level. The precise role of cyclic GMP in platelet activation is not yet known. In order to study the mechanism of action of this drug, we tried to determine the effect of Sin 1 on the different steps described above. We measured Ca2+ fluxes and phospholipase C activation in thrombin (0,5 U/ml) stimulated platelets in the presence of different doses of Sin 1 (10™7-10™3M). Serotonin secretion was inhibited by 30 % with Sin 1 (10™4M-10™5m). A parallel inhibition of phospholipase C was detected by measurement of [32P)-PA level. Platelets loaded with Quin 2 and stimulated by thrombin showed a 70 % inhibition of external Ca2+ influx as soon as a concentration of 10™7M of Sin 1 was added. A study on platelet loaded with [45Ca2+) and Quin 2 confirmed these results. On the contrary, discharge of internal Ca2+ store seemed to be unaffected.In conclusion, the major effect of Sin 1 on platelet phospholipase C pathway is an inhibition of Ca2+ influx through plasma membrane. Some further experiments are necessary to shown whether this inhibition is correlated with cyclic GMP formation (the major effect of Sin 1) and try to establish a relation between this inhibition and that exerted on phospholipase C.Sin 1 was a generous gift of Hoechst.
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