Relevant bibliographies by topics / Phospholipase C gamma 2 [PLC 2]

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  2. Dissertations / Theses
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  4. Conference papers

Academic literature on the topic 'Phospholipase C gamma 2 [PLC 2]'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Phospholipase C gamma 2 [PLC 2]"

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Sultzman, L., C. Ellis, L. L. Lin, T. Pawson, and J. Knopf. "Platelet-derived growth factor increases the in vivo activity of phospholipase C-gamma 1 and phospholipase C-gamma 2." Molecular and Cellular Biology 11, no. 4 (1991): 2018–25. http://dx.doi.org/10.1128/mcb.11.4.2018.

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Upon binding to its cell surface receptor, platelet-derived growth factor (PDGF) causes the tyrosine phosphorylation of phospholipase C-gamma 1 (PLC-gamma 1) and stimulates the production of diacylglycerol and inositol 1,4,5-triphosphate. We showed that following stimulation by PDGF, rat-2 cells overexpressing PLC-gamma 1 display an increase in the levels of both tyrosine-phosphorylated PLC-gamma 1 and inositol phosphates compared with the parental rat-2 cells. This increased responsiveness to PDGF is a direct effect of PLC-gamma 1 overexpression, as a cell line expressing similar levels of an enzymatically inactive point mutant of PLC-gamma 1, PLC-gamma 1 335Q, did not show elevated inositol phosphate production in response to PDGF. Hematopoietic cells express PLC-gamma 2, a PLC isoform that is closely related to PLC-gamma 1. When rat-2 cells overexpressing PLC-gamma 2 were treated with PDGF, an increase in both the tyrosine phosphorylation and the in vivo activity of PLC-gamma 2 was observed. Aluminum fluoride (AIF4-), a universal activator of PLC linked to G-proteins, did not produce an increase in the levels of inositol phosphates in either of the overexpressing cell lines compared with parental rat-2 cells, demonstrating that PLC-gamma isoforms respond specifically to a receptor with tyrosine kinase activity.
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Sultzman, L., C. Ellis, L. L. Lin, T. Pawson, and J. Knopf. "Platelet-derived growth factor increases the in vivo activity of phospholipase C-gamma 1 and phospholipase C-gamma 2." Molecular and Cellular Biology 11, no. 4 (1991): 2018–25. http://dx.doi.org/10.1128/mcb.11.4.2018-2025.1991.

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Upon binding to its cell surface receptor, platelet-derived growth factor (PDGF) causes the tyrosine phosphorylation of phospholipase C-gamma 1 (PLC-gamma 1) and stimulates the production of diacylglycerol and inositol 1,4,5-triphosphate. We showed that following stimulation by PDGF, rat-2 cells overexpressing PLC-gamma 1 display an increase in the levels of both tyrosine-phosphorylated PLC-gamma 1 and inositol phosphates compared with the parental rat-2 cells. This increased responsiveness to PDGF is a direct effect of PLC-gamma 1 overexpression, as a cell line expressing similar levels of an enzymatically inactive point mutant of PLC-gamma 1, PLC-gamma 1 335Q, did not show elevated inositol phosphate production in response to PDGF. Hematopoietic cells express PLC-gamma 2, a PLC isoform that is closely related to PLC-gamma 1. When rat-2 cells overexpressing PLC-gamma 2 were treated with PDGF, an increase in both the tyrosine phosphorylation and the in vivo activity of PLC-gamma 2 was observed. Aluminum fluoride (AIF4-), a universal activator of PLC linked to G-proteins, did not produce an increase in the levels of inositol phosphates in either of the overexpressing cell lines compared with parental rat-2 cells, demonstrating that PLC-gamma isoforms respond specifically to a receptor with tyrosine kinase activity.
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Shirai, Y., K. Kashiwagi, N. Sakai, and N. Saito. "Phospholipase A(2) and its products are involved in the purinergic receptor-mediated translocation of protein kinase C in CHO-K1 cells." Journal of Cell Science 113, no. 8 (2000): 1335–43. http://dx.doi.org/10.1242/jcs.113.8.1335.

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The signal transduction involved in the purinergic stimuli-induced activation of protein kinase C (PKC) in CHO-K1 cells was investigated. Purinergic stimuli such as adenosine triphosphate and uridine triphosphate induced a transient translocation of PKC epsilon, gamma, and delta from the cytoplasm to the plasma membrane. These translocations were blocked by an inhibitor of phosphatidylinositol-specific phospholipase C (PLC), but not by an inhibitor of phosphatidylcholine-specific PLC. A diacylglycerol (DAG) analogue also induced reversible translocations of PKC gamma, epsilon, and delta from the cytoplasm to the plasma membrane, while the calcium ionophore A23187 caused a similar translocation of only the gamma subtype. These results confirm that the hydrolysis of phosphatidylinositol-2-phosphate by PLC and the subsequent generation of DAG and increase in Ca(2+)are involved in the purinergic stimuli-induced translocation of PKC. A DAG antagonist, 1-o-hexadecyl-2-o-acetyl-glycerol, blocked the DAG analogue-induced translocations of all PKC subtypes tested but failed to inhibit the purinergic stimuli-induced translocations of PKC epsilon and gamma. The DAG antagonist could not block the ATP- and UTP-induced translocation of PKC epsilon even in the absence of extracellular Ca(2+). Co-application of the DAG antagonist and a phospholipase A(2) (PLA(2)) inhibitor such as aristolochic acid, arachidonyltrifluoromethyl ketone, or bromoenol lactone inhibited the purinergic receptor-mediated translocation of PKC epsilon although each PLA(2) inhibitor alone did not block the translocation. In contrast to the epsilon subtype, ATP-induced translocation of PKC gamma was observed in the presence of both the PLA(2) inhibitor and the DAG antagonist. However, it is noteworthy that re-translocation of PKC gamma was hastened by the PLA(2) inhibitor. Furthermore products of PLA(2), such as lysophospholipids and fatty acids, induced the translocation of PKC gamma and epsilon in a dose dependent manner, but not delta. These results indicate that, in addition to PLC and DAG, PLA(2) and its products are involved in the purinergic stimuli-induced translocation of PKC epsilon and gamma in CHO-K1 cells. Each subtype of PKC in CHO-K1 cell is individually activated in response to a purinergic stimulation.
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Takata, M., Y. Homma, and T. Kurosaki. "Requirement of phospholipase C-gamma 2 activation in surface immunoglobulin M-induced B cell apoptosis." Journal of Experimental Medicine 182, no. 4 (1995): 907–14. http://dx.doi.org/10.1084/jem.182.4.907.

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Surface IgM (sIgM) stimulation induces the tyrosine phosphorylation of multiple cellular substrates, including phospholipase C (PLC)-gamma 2, which is involved in the activation of phosphatidylinositol pathway. DT40 B cells underwent apoptotic cell death when activated through sIgM, a phenomenon that is related to elimination of self-reactive B cells. To examine the roles of PLC-gamma 2 in sIgM signaling, we have generated DT40 cells deficient in PLC-gamma 2 Cross-linking of sIgM on PLC-gamma 2-deficient cells evoked neither inositol 1,4,5-trisphosphate nor calcium mobilization. In PLC-gamma 2- or Syk-deficient DT40 cells, the induction of apoptosis was blocked, but was still observed in Lyn-deficient cells. Src homology 2 domains of PLC-gamma 2 were essential for both its activation and sIgM-induced apoptosis. Since tyrosine phosphorylation of PLC-gamma 2 is mediated by Syk, these results indicate that activation of PLC-gamma 2 through Syk is required for sIgM-induced apoptosis.
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Tappia, Paramjit S., Raymond R. Padua, Vincenzo Panagia та Elissavet Kardami. "Fibroblast growth factor-2 stimulates phospholipase Cβ in adult cardiomyocytes". Biochemistry and Cell Biology 77, № 6 (1999): 569–75. http://dx.doi.org/10.1139/o99-059.

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Although fibroblast growth factor-2 (FGF-2) plays an important role in cardioprotection and growth, little is known about the signals triggered by it in the adult heart. We therefore examined FGF-2-induced effects on phosphoinositide-specific phospholipase C (PI-PLC) isozymes, which produce second messengers linked to the inotropic and hypertrophic response of the myocardium. FGF-2, administered by retrograde perfusion to the isolated heart, induced an increase in inositol-1,4,5-trisphosphate levels in the cytosol, as well as an increase in total PI-PLC activity associated with sarcolemmal and cytosolic fractions. Furthermore FGF-2 induced a time-dependent elevation in cardiomyocyte membrane-associated PLC gamma1 and PLC β1 activities, assayed in immunoprecipitated fractions, and moreover, increased the membrane levels of PLC β1 and PLC β3. Activation of PLC β is suggestive of FGF-2-induced cross-talk between FGF-receptor tyrosine kinase and G-protein-coupled signaling in adult cardiomyocytes and underscores the importance of FGF-2 in cardiac physiology.Key words: FGF-2, signal transduction, PLC gamma, PLC β, cardiomyocytes.
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Lee, SB, AK Rao, KH Lee, X. Yang, YS Bae, and SG Rhee. "Decreased expression of phospholipase C-beta 2 isozyme in human platelets with impaired function." Blood 88, no. 5 (1996): 1684–91. http://dx.doi.org/10.1182/blood.v88.5.1684.1684.

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Abstract Platelets from a patient with a mild inherited bleeding disorder and abnormal platelet aggregation and secretion show reduced generation of inositol 1,4,5-trisphosphate, mobilization of intracellular Ca2+, and phosphorylation of pleckstrin in response to several G protein mediated agonists, suggesting a possible defect at the level of phospholipase C (PLC) activation (see accompanying report). A procedure was developed that allows quantitation of platelet PLC isozymes. After fractionation of platelet extracts by high-performance liquid chromatography, 7 out of 10 known PLC isoforms were detected by immunoblot analysis. The amount of these isoforms in normal platelets decreased in the order PLC- gamma 2 > PLC-beta 2 > PLC-beta 3 > PLC-beta 1 > PLC-gamma 1 > PLC- delta 1 > PLC-beta 4. Compared with normal platelets, platelets from the patient contained approximately one-third the amount of PLC-beta 2, whereas PLC-beta 4 was increased threefold. These results suggest that the impaired platelet function in the patient in response to multiple G protein mediated agonists is attributable to a deficiency of PLC-beta 2. They document for the first time a specific PLC isozyme deficiency in human platelets and provide an unique opportunity to understand the role of different PLC isozymes in normal platelet function.
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Lee, SB, AK Rao, KH Lee, X. Yang, YS Bae, and SG Rhee. "Decreased expression of phospholipase C-beta 2 isozyme in human platelets with impaired function." Blood 88, no. 5 (1996): 1684–91. http://dx.doi.org/10.1182/blood.v88.5.1684.bloodjournal8851684.

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Platelets from a patient with a mild inherited bleeding disorder and abnormal platelet aggregation and secretion show reduced generation of inositol 1,4,5-trisphosphate, mobilization of intracellular Ca2+, and phosphorylation of pleckstrin in response to several G protein mediated agonists, suggesting a possible defect at the level of phospholipase C (PLC) activation (see accompanying report). A procedure was developed that allows quantitation of platelet PLC isozymes. After fractionation of platelet extracts by high-performance liquid chromatography, 7 out of 10 known PLC isoforms were detected by immunoblot analysis. The amount of these isoforms in normal platelets decreased in the order PLC- gamma 2 > PLC-beta 2 > PLC-beta 3 > PLC-beta 1 > PLC-gamma 1 > PLC- delta 1 > PLC-beta 4. Compared with normal platelets, platelets from the patient contained approximately one-third the amount of PLC-beta 2, whereas PLC-beta 4 was increased threefold. These results suggest that the impaired platelet function in the patient in response to multiple G protein mediated agonists is attributable to a deficiency of PLC-beta 2. They document for the first time a specific PLC isozyme deficiency in human platelets and provide an unique opportunity to understand the role of different PLC isozymes in normal platelet function.
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8

Arkinstall, S., M. Payton, and K. Maundrell. "Activation of phospholipase C gamma in Schizosaccharomyces pombe by coexpression of receptor or nonreceptor tyrosine kinases." Molecular and Cellular Biology 15, no. 3 (1995): 1431–38. http://dx.doi.org/10.1128/mcb.15.3.1431.

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The fission yeast Schizosaccharomyces pombe has no detectable endogenous receptor tyrosine kinases or associated signalling apparatus, and we have used this cell system to reconstitute mammalian platelet-derived growth factor beta (PDGF beta) receptor-linked activation of phospholipase C gamma 2 (PLC gamma 2). The PDGF beta receptor migrates as a glycosylated protein of 165 kDa associated exclusively with membrane fractions. No tyrosine autophosphorylation was detected when PDGF beta was expressed alone. PLC gamma 2 appears as a 140-kDa protein distributed between particulate and soluble fractions which exhibits characteristic selectivity for phosphatidylinositol 4,5-bisphosphate and is sensitive to powerful activation by Ca2+. When coexpressed, both PDGF beta and PLC gamma 2 undergo tyrosine phosphorylation, and this is accompanied by a > 26-fold increase in [3H]inositol 4,5-biphosphate ([3H]IP2) and [3H]inositol 1,4,5-triphosphate [3H]IP3 production. Treatment with the tyrosine phosphatase inhibitor pervanadate further increased PLC gamma 2 tyrosine phosphorylation as well as [3H]IP2 and [3H]IP3 generation. Phosphorylated PLC gamma 2 was found predominantly in membrane fractions. To test a nonreceptor tyrosine kinase, we then expressed the human proto-oncogene c-src together with its negative regulator Csk. These were immunodetectable as bands at 60 kDa (c-Src) and 50 kDa (Csk) and distributed between membrane and cytosolic fractions. When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively. Csk expressed alone with PLC gamma 2 was ineffective. Similar PLC gamma 2 activation was observed upon in vitro mixing with the extracts expressing either c-Src or the PDGF beta receptor. In summary, this is the first report of a reconstitution of mammalian tyrosine kinase-linked effector activation in yeast cells and also the first demonstration of direct PLC gamma 2 activation by the proto-oncogene c-src. These observations indicate that S. pombe provides a powerful cell system in which to study critical molecular interactions and activities underlying receptor and nonreceptor tyrosine kinase-dependent cell signaling.
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Bolt, M. J. G., B. M. Bissonnette, R. K. Wali, S. C. Hartmann, T. A. Brasitus, and M. D. Sitrin. "Characterization of phosphoinositide-specific phospholipase C in rat colonocyte membranes." Biochemical Journal 292, no. 1 (1993): 271–76. http://dx.doi.org/10.1042/bj2920271.

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The phosphoinositide signal transduction pathway mediates important processes in intestinal physiology, yet the key enzyme, phosphoinositide-specific phospholipase C (PI-PLC), is not well-characterized in the colon. PI-PLC activity was examined in rat colonic membranes using exogenous [3H]phosphatidylinositol 4,5-bisphosphate (PIP2) as substrate, and beta-glycerophosphate to suppress degradation of substrate or product. The activity of membrane PI-PLC increased 6-fold with the addition of alamethicin, and a further 2-3-fold enhancement was observed with 10 microM guanosine 5′-[gamma-thio]triphosphate (GTP[S]), suggesting the involvement of G-protein(s). The effect of GTP[S] appeared to be specific, as up to 100 microM adenosine 5′-[gamma-thio]-triphosphate failed to stimulate PI-PLC activity, and guanosine 5′-[beta-thio]diphosphate inhibited activity. The response of membrane PI-PLC to Ca2+ was biphasic, while > 0.5 mM Mg2+ was inhibitory with or without GTP[S]. Comparable total PI-PLC activities and responses to GTP[S] and Ca2+ were observed in purified brush-border and basolateral membranes. Western immunoblots probed with monoclonal antibodies to PLC isoenzymes PLC-beta 1, -gamma 1 and -delta 1 demonstrated that these antipodal plasma membranes contain predominantly the PLC-delta 1 isoform, with small amounts of PLC-gamma 1 present but no detectable PLC-beta 1. PLC-gamma 1 was the major isoform detected in cytosol.
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Homma, Y., Y. Emori, F. Shibasaki, K. Suzuki та T. Takenawa. "Isolation and characterization of a γ-type phosphoinositide-specific phospholipase C (PLC-γ2)". Biochemical Journal 269, № 1 (1990): 13–18. http://dx.doi.org/10.1042/bj2690013.

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A novel bovine spleen phosphoinositide-specific phospholipase C (PLC) has been identified with respect to immunoreactivity with four independent antibodies against each of the PLC isoenzymes, and purified to near homogeneity by sequential column chromatography. Spleen contains three of the isoenzymes: two different gamma-types [gamma 1 and gamma 2, originally named as PLC-gamma [Rhee, Suh, Ryu & Lee (1989) Science 244, 546-550] and PLC-IV [Emori, Homma, Sorimachi, Kawasaki, Nakanishi, Suzuki & Takenawa (1989) J. Biol. Chem. 264, 21885-21890] respectively] and delta-type of the enzyme, but PLC-gamma 1 is separated from the PLC-gamma 2 pool by the first DEAE-cellulose column chromatography. Subsequently, PLC-delta is dissociated on the third heparin-Sepharose column chromatography. The purified enzyme has a molecular mass of 145 kDa on SDS/polyacrylamide-gel electrophoresis and a specific activity of 12.8 mumol/min per mg with phosphatidylinositol 4,5-bisphosphate as substrate. This enzyme activity is dependent on Ca2+ for hydrolysis of all these phosphoinositides. None of the other phospholipids examined could be its substrate at any concentration of Ca2+. The optimal pH of the enzyme is slightly acidic (pH 5.0-6.5).
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Dissertations / Theses on the topic "Phospholipase C gamma 2 [PLC 2]"

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Caraux, Anouk. "Le grand chemin des cellules natural killer : développement et fonctions chez la souris." Paris 6, 2005. http://www.theses.fr/2005PA066082.

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Bühler, Anja [Verfasser]. "Molecular mechanisms regulating phospholipase C-gamma 2 activity / Anja Bühler." Ulm : Universität Ulm. Fakultät für Naturwissenschaften, 2016. http://d-nb.info/1094889202/34.

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Gross, Barabara Sylvie. "Regulation of phospholipase C-←#gamma#2 in human platelets activated by collagen." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298782.

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Thérier, Julien. "Régulation de la voie des Mitogen-Activated Protein Kinase ERK1/2 par la phospholipase C gamma dans le signal du Macrophage-Colony Stimulating Factor." Lyon 1, 2005. http://www.theses.fr/2005LYO10121.

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Le M-CSF régule l'établissement du lignage monocytaire/macrophagique en assurant la survie, la prolifération mais aussi la différenciation des progéniteurs myéloïdes en cellules très spécialisées : les macrophages. Ce contrôle nécessite la transduction d'un signal intracellulaire impliquant de nombreuses molécules. Parmi celles-ci, les MAPK ERK1/2 présentent une cinétique d'activation caractéristique : une première vague de phosphorylation rapide et transitoire puis une seconde vague tardive et soutenue essentielle à la différenciation macrophagique. J'ai montré au cours de cette étude que la phospholipase C régule spécifiquement cette seconde vague d'activation des kinases ERK1/2 par l'intermédiaire de Ras. Ce processus, indépendant du diacylglycérol, fait intervenir de façon prépondérante l'augmentation du taux de calcium intracellulaire. Ces résultats constituent un mécanisme d'activation original faisant potentiellement intervenir les kinases Src ou les complexes Gab2/SHP2
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Waksmunski, Andrea Rose. "From Variants to Pathways: Interrogating the Genetic Architecture of Age-Related Macular Degeneration." Case Western Reserve University School of Graduate Studies / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=case1586371907365746.

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Piechulek, Thomas. "Isoenzym-spezifische Stimulation der Phospholipase C-g2 [C-Gamma 2] durch Rac-GTPasen /." 2005. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=014794211&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Christow, Carolin [Verfasser]. "Strukturelle Voraussetzungen der Rac2-vermittelten Aktivierung der Phospholipase C-γ2 [C-gamma-2] / vorgelegt von Carolin Christow". 2010. http://d-nb.info/1010106015/34.

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Weber, Frank Udo [Verfasser]. "Physiko-chemische und strukturelle Voraussetzungen für die Rho-GTPase-vermittelte Aktivierung der Phospholipase Cγ2 [C-gamma 2] im zellfreien System / vorgelegt von Frank Udo Weber". 2010. http://d-nb.info/1010745093/34.

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Barzik, Melanie [Verfasser]. "Struktur- und Funktionsuntersuchungen an der Phosphatidylinositol-spezifischen Phospholipase C (PI-PLC) aus Listeria monocytogenes und der Ena-VASP-Homologie-1-(EVH1)-Domäne des murinen Vesl-2 / von Melanie Barzik." 2002. http://d-nb.info/965237273/34.

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Books on the topic "Phospholipase C gamma 2 [PLC 2]"

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Brazil, Derek P. Regulation of phospholipase C-[beta]2 by G protein [beta] [gamma] subunits. University College Dublin, 1996.

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Conference papers on the topic "Phospholipase C gamma 2 [PLC 2]"

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Labow, R. S., E. Meek, G. A. Adams, and G. Rock. "AGGREGATION RESPONSE OF PLATELETS DURING INHIBITION OF PHOSPHOLIPASE A2." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644542.

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Arachidonic acid (AA) is liberated from platelet membrane phospholipids during stimulation and promotes cellular aggregation through the synthesis of thromboxane A2. Two pathways; phospholipase A2 (PLA2) or phospholipase C (PLC) followed by the action of acylglycerolipases, are thought to be activated during platelet stimulation and supply the necessary AA. We have reported that mono (2-ethylhexyl)phthalate (MEHP), a physiological metabolite of the plasticizer di(2-ethylhexyl)-phthalate (DEHP), commonly used in a variety of medical devices and storage containers, inhibits PLA2, but not PLC in platelet lysates. The effects of MEHP on intact platelets were studied. PLA2 activity in intact platelets or lysates was assayed by incubating them with 2-14C-arachidonyl-phosphatidylcholine and measuring formation of free 14C-arachidonic acid in 10 min. Platelet lysates hydrolyzed 10% of the substrate while 2.6% was hydrolyzed by intact platelets. The amount of MEHP needed to inhibit 14C-AA liberation was 0.35 mM for platelet lysates and 0.7 mM for intact platelets. Platelet aggregation induced by collagen was inhibited by MEHP (1 mM), although responses to adenosine diphosphate, AA and ionophore were unaffected. Identical effects on platelet aggregation were found when indomethacin (0.1 mM) was added. Higher concentrations of MEHP blocked platelet aggregation induced by adenosine diphosphate or AA but not ionophore or synergistic pairs of these stimuli, indicating a more generalized membrane disruption at higher MEHP concentrations. These results suggest that MEHP acts in a similar manner to indomethacin to block PLA2-mediated liberation of arachidonate during platelet aggregation(supported by MRC and NHRDP, Canada)
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Sandset, P. M., P. A. Sirnes, U. Abildgaard, and M. Petterson. "PREACTIVATION AND INHIBITION OF EXTRINSIC COAGULATION PATHWAY IN ACUTE CORONARY DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643024.

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It has recently been shown that plasma from individuals with a high risk score for developing AMI shows an abnormal depression of factor VII (EVII) coagulant activity after treatment with phospholipase C (PLC), (Dalaker, K.& Prydz, H., Br . J . Haematol. 61,315, 1985) revealing the presence of “preactivated” FVII in complex with lipid. We have studied this phenomenon in patients in a coronary unit, by serial determinations of Normotest (NT) + PLC pretreatment (which correlates with FVII clotting) assay ± PLC) and EVII amidolytic assay (EVIIram) (OswaldsBn et al., Tromb.Haemostas. 54,26,1985). The newly described inhibitor of FVII-Tissue thromboplastin (EPI) was also measured. Mean patient values day 2 are listed:More than 20% depression of NT by PLC treatment was found in 2/14 controls, 9/19 AMI patients, 3/17 angina patients and 2/15 patients with other heart disease. The EVII:am values correlated better with NT (r = 0.81) than with PLC+NT (r=0.62). It has been suggested that FVII:am correlates with the molar concentration of FVII. If correct, our data precludes two chain FVII as contributing much to preactivation. EPI values were in the high normal range for all three groups of heart patients. The individual variation in EPI values was great, particularly in AMI patients. Apparently, EPI did not correlate to any of the FVII assays. Three patients with more then 50% reduced NT after PLC had EPI values 67, 149, and 130%. In conclusion, lipid activation was frequent in AMI patients, and was not related to EPI activity.
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Authi, K. S., B. J. Evenden та N. Crawford. "ACTION OF GTPγS [GUANOSINE 5∲-0-(3-THIOPHOSPHATE)] ON SAPONIN-PERMEABILISED PLATELETS: INVOLVEMENT OF 'G' PROTEINS IN PLATELET ACTIVATION". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644514.

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Certain ligand-receptor interactions at cell surfaces lead to the phospholipase-C (PLC) hydrolysis of phosphatidyl inositol (4.5) bisphosphate (PIP2). The products serve as intracellular second messengers, e.g. inositol (1.4.5) trisphosphate (IP3) releases Ca2+ from intracellular stores and diacylglycerol activates protein kinase-C. From studies using GTP and analogues (e.g. GTPγS) there is evidence of a key role for a guanine nucleotide binding protein(s) as a link between receptors and PIP2 hydrolysis. We report the actions of GTPγS on washed human platelets permeabilised with saponin (12-14 μg/ml) to allow penetration of low MWt polar substances. The responses to GTPγS are dose dependent (range 9-60 μM) and at 60 μM the agent induces shape change, aggregation and the secretion of 50% of previously incorporated [14C]-5HT. No effect of GTPγS is seen with intact cells. Shape change occurs 25-30 sec after GTPγS; aggregation and secretion is complete after 3 min. When GTP was used (up to 135 μM) with similarly permeabilised platelets no responses were initiated. Phosphatidylinositol turnover was monitored using 32P-labelling before permeabilisation. The addition of 90 μM GTPγS resulted in a 143 ± 23% (n=4) increase in 32P-phosphatidic acid (PA) with respect to the basal levels of “saponised control” cells. These findings suggest that GTPγS stimulates PLC activity through a ‘G’ protein interaction. The GDP analogue (GDPβS) produced no activation responses in saponised platelets but inhibited responses induced by GTPγS in a dose dependent manner (0-480 μM, max inhibition 480 μM). At 960 μM, GDPβS totally inhibited aggregation and secretion initiated by low doses of thrombin (0.1 U/ml) and collagen (1 μg/ml). Identical inhibition by GDPβS of thrombin and collagen-induced activation of intact platelets was observed indicating membrane penetration of this analogue. Shape change effects were not inhibited by GDPSS. The inhibitory effects of GDPSS towards thrombin and collagen induced secretion could be progressively overcome at higher doses of thrombin (0.2 U/ml - 2 U/ml) and collagen (5 μg/ml - 60 μg/ml) suggesting that at higher concentrations these agonists may exert effects through 'G' protein-independent mechanisms.
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