Relevant bibliographies by topics / Phospholipase C

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Phospholipase C'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "Phospholipase C"

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Hawrylak, K., and R. A. Stinson. "Phospholipase C and phosphatidylinositol phospholipase C." Clinical Chemistry 33, no. 2 (February 1, 1987): 337. http://dx.doi.org/10.1093/clinchem/33.2.337.

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Bollag, Wendy B. "Role of phospholipases in adrenal steroidogenesis." Journal of Endocrinology 229, no. 1 (April 2016): R29—R41. http://dx.doi.org/10.1530/joe-16-0007.

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Phospholipases are lipid-metabolizing enzymes that hydrolyze phospholipids. In some cases, their activity results in remodeling of lipids and/or allows the synthesis of other lipids. In other cases, however, and of interest to the topic of adrenal steroidogenesis, phospholipases produce second messengers that modify the function of a cell. In this review, the enzymatic reactions, products, and effectors of three phospholipases, phospholipase C, phospholipase D, and phospholipase A2, are discussed. Although much data have been obtained concerning the role of phospholipases C and D in regulating adrenal steroid hormone production, there are still many gaps in our knowledge. Furthermore, little is known about the involvement of phospholipase A2, perhaps, in part, because this enzyme comprises a large family of related enzymes that are differentially regulated and with different functions. This review presents the evidence supporting the role of each of these phospholipases in steroidogenesis in the adrenal cortex.
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Dhand, Rajiv, Jared Young, Andelle Teng, Subbiah Krishnasamy, and Nicholas J. Gross. "Is dipalmitoylphosphatidylcholine a substrate for convertase?" American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 1 (January 1, 2000): L19—L24. http://dx.doi.org/10.1152/ajplung.2000.278.1.l19.

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Convertase has homology with carboxylesterases, but its substrate(s) is not known. Accordingly, we determined whether dipalmitoylphosphatidylcholine (DPPC), the major phospholipid in surfactant, was a substrate for convertase. We measured [3H]choline release during cycling of the heavy subtype containing [3H]choline-labeled DPPC with convertase, phospholipases A2, B, C, and D, liver esterase, and elastase. Cycling with liver esterase or peanut or cabbage phospholipase D produced the characteristic profile of heavy and light peaks observed on cycling with convertase. In contrast, phospholipases A2, B, and C and yeast phospholipase D produced a broad band of radioactivity across the gradient without distinct peaks. [3H]choline was released when natural surfactant containing [3H]choline-labeled DPPC was cycled with yeast phospholipase D but not with convertase or peanut and cabbage phospholipases D. Similarly, yeast phospholipase D hydrolyzed [3H]choline from [3H]choline-labeled DPPC after incubation in vitro, whereas convertase, liver esterase, or peanut and cabbage phospholipases D did not. Thus convertase, liver esterase, and plant phospholipases D did not hydrolyze choline from DPPC either on cycling or during incubation with enzyme in vitro. In conclusion, conversion of heavy to light subtype of surfactant by convertase may require a phospholipase D type hydrolysis of phospholipids, but the substrate in this reaction is not DPPC.
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LITTLE, CLIVE. "Phospholipase C." Biochemical Society Transactions 17, no. 2 (April 1, 1989): 271–73. http://dx.doi.org/10.1042/bst0170271.

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Karasawa, Tadahiro, Xingmin Wang, Tsuneo Maegawa, Yoshio Michiwa, Hiroyuki Kita, Koichi Miwa, and Shinichi Nakamura. "Clostridium sordellii Phospholipase C: Gene Cloning and Comparison of Enzymatic and Biological Activities with Those of Clostridium perfringens and Clostridium bifermentans Phospholipase C." Infection and Immunity 71, no. 2 (February 2003): 641–46. http://dx.doi.org/10.1128/iai.71.2.641-646.2003.

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ABSTRACT The gene encoding Clostridium sordellii phospholipase C (Csp) was cloned and expressed as a histidine-tagged (His-tag) protein, and the protein was purified to compare its enzymatic and biological activities with those of Clostridium perfringens phospholipase C (Cpa) and Clostridium bifermentans phospholipase C (Cbp). Csp was found to consist of 371 amino acid residues in the mature form and to be more homologous to Cbp than to Cpa. The egg yolk phospholipid hydrolysis activity of the His-tag Csp was about one-third of that of His-tag Cpa, but the hemolytic activity was less than 1% of that of His-tag Cpa. His-tag Csp was nontoxic to mice. Immunization of mice with His-tag Cbp or His-tag Csp did not provide effective protection against the lethal activity of His-tag Cpa. These results indicate that Csp possesses similar molecular properties to Cbp and suggest that comparative analysis of toxic and nontoxic clostridial phospholipases is helpful for characterization of the toxic properties of clostridial phospholipases.
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Teitelbaum, I. "Hormone signaling systems in inner medullary collecting ducts." American Journal of Physiology-Renal Physiology 263, no. 6 (December 1, 1992): F985—F990. http://dx.doi.org/10.1152/ajprenal.1992.263.6.f985.

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The inner medullary collecting duct is a complex tissue that exhibits a variety of hormone signaling systems. These include the following: adenylyl cyclase activity stimulated by vasopressin (AVP), beta-adrenergic agonists, or prostanoids and inhibited by alpha 2-adrenergic agents or adenosine; guanylate cyclase activity in response to atrial natriuretic peptide (ANP); phospholipase C activity stimulated by ANP, AVP, bradykinin, endothelin, epidermal growth factor (EGF), and muscarinic cholinergic agents; and phospholipase A2 activity stimulated by AVP, bradykinin, EGF, and endothelin. The signal transduction mechanisms for each of these hormone signaling systems is succinctly reviewed, and the interactions between different signaling pathways are discussed. Central to this interaction is the mutually inhibitory relationship between activation of adenylyl cyclase and phospholipases. Increasing cellular adenosine 3',5'-cyclic monophosphate content impairs activation of phospholipases A2 and C; conversely, stimulation of phospholipase C impairs AVP-stimulated adenylyl cyclase activity via activation of protein kinase C.
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Ghannoum, Mahmoud A. "Potential Role of Phospholipases in Virulence and Fungal Pathogenesis." Clinical Microbiology Reviews 13, no. 1 (January 1, 2000): 122–43. http://dx.doi.org/10.1128/cmr.13.1.122.

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SUMMARY Microbial pathogens use a number of genetic strategies to invade the host and cause infection. These common themes are found throughout microbial systems. Secretion of enzymes, such as phospholipase, has been proposed as one of these themes that are used by bacteria, parasites, and pathogenic fungi. The role of extracellular phospholipase as a potential virulence factor in pathogenic fungi, including Candida albicans, Cryptococcus neoformans, and Aspergillus, has gained credence recently. In this review, data implicating phospholipase as a virulence factor in C. albicans, Candida glabrata, C. neoformans, and A. fumigatus are presented. A detailed description of the molecular and biochemical approaches used to more definitively delineate the role of phospholipase in the virulence of C. albicans is also covered. These approaches resulted in cloning of three genes encoding candidal phospholipases (caPLP1, caPLB2, and PLD). By using targeted gene disruption, C. albicans null mutants that failed to secrete phospholipase B, encoded by caPLB1, were constructed. When these isogenic strain pairs were tested in two clinically relevant murine models of candidiasis, deletion of caPLB1 was shown to lead to attenuation of candidal virulence. Importantly, immunogold electron microscopy studies showed that C. albicans secretes this enzyme during the infectious process. These data indicate that phospholipase B is essential for candidal virulence. Although the mechanism(s) through which phospholipase modulates fungal virulence is still under investigations, early data suggest that direct host cell damage and lysis are the main mechanisms contributing to fungal virulence. Since the importance of phospholipases in fungal virulence is already known, the next challenge will be to utilize these lytic enzymes as therapeutic and diagnostic targets.
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Heo, Yunseok, Inhwan Lee, Sunjin Moon, Ji-Hye Yun, Eun Yu Kim, Sam-Yong Park, Jae-Hyun Park, Woo Taek Kim, and Weontae Lee. "Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain." Molecules 27, no. 7 (April 2, 2022): 2317. http://dx.doi.org/10.3390/molecules27072317.

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Phospholipase is an enzyme that hydrolyzes various phospholipid substrates at specific ester bonds and plays important roles such as membrane remodeling, as digestive enzymes, and the regulation of cellular mechanism. Phospholipase proteins are divided into following the four major groups according to the ester bonds they cleave off: phospholipase A1 (PLA1), phospholipase A2 (PLA2), phospholipase C (PLC), and phospholipase D (PLD). Among the four phospholipase groups, PLA1 has been less studied than the other phospholipases. Here, we report the first molecular structures of plant PLA1s: AtDSEL and CaPLA1 derived from Arabidopsis thaliana and Capsicum annuum, respectively. AtDSEL and CaPLA1 are novel PLA1s in that they form homodimers since PLAs are generally in the form of a monomer. The dimerization domain at the C-terminal of the AtDSEL and CaPLA1 makes hydrophobic interactions between each monomer, respectively. The C-terminal domain is also present in PLA1s of other plants, but not in PLAs of mammals and fungi. An activity assay of AtDSEL toward various lipid substrates demonstrates that AtDSEL is specialized for the cleavage of sn-1 acyl chains. This report reveals a new domain that exists only in plant PLA1s and suggests that the domain is essential for homodimerization.
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Kadamur, Ganesh, and Elliott M. Ross. "Mammalian Phospholipase C." Annual Review of Physiology 75, no. 1 (February 10, 2013): 127–54. http://dx.doi.org/10.1146/annurev-physiol-030212-183750.

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Alvarez-Breckenridge, Christopher A., Kristin A. Waite, and Charis Eng. "PTEN regulates phospholipase D and phospholipase C." Human Molecular Genetics 16, no. 10 (April 3, 2007): 1157–63. http://dx.doi.org/10.1093/hmg/ddm063.

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Dissertations / Theses on the topic "Phospholipase C"

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Zhou, Yixing Harden T. Kendall. "Cloning and characterization of a novel phospholipase C enzyme, human phospholipase C eta2." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2007. http://dc.lib.unc.edu/u?/etd,1271.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2007.
Title from electronic title page (viewed Mar. 26, 2008). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Pharmacology." Discipline: Pharmacology; Department/School: Medicine.
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Lin, Gialih Hoffmann. "Stereochemistry and mechanism of phospholipase A2 and phosphatidylinositide-specific phospholipase C /." The Ohio State University, 1989. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487672245900381.

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Tong, Yun. "Phosphoinositide-phospholipase C in diabetic cardiomyopathy." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape17/PQDD_0001/MQ32268.pdf.

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Zhao, Li. "Mechanistic studies on phosphatidylinositol-specific phospholipase C." Connect to this title online, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1047485476.

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Thesis (Ph. D.)--Ohio State University, 2003.
Title from first page of PDF file. Document formatted into pages; contains xix, 135 p.; also includes graphics (some col.) Includes bibliographical references (p. 128-135). Available online via OhioLINK's ETD Center
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Donahue, Vicki S. "Phospholipase c activity in retinal pigment epithelium." Virtual Press, 1997. http://liblink.bsu.edu/uhtbin/catkey/1041916.

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The role of the retinal pigment epithelial cells on the viability and renewal of photoreceptors has been well demonstrated in the Royal College of Surgeons (RCS) strain of rat. These rats are characterized by an inherited time-dependent degeneration of their photoreceptors. This degeneration is apparently due to the inability of the retinal pigment epithelial cells to adequately ingest fragments of photoreceptor membrane that are shed during the course of photoreceptor membrane renewal. The buildup of photoreceptor material in the interphotoreceptor space ultimately leads to the degeneration of photoreceptors in these animals. With regard to the pigment epithelial cells, neither the mechanism mediating the ingestion process in normal rats nor the nature of the defect of this process in RCS rats is understood.It is the goal of this proposed research to assay for the presence of phospholipase C in retinal pigment epithelial (RPE) cells and to determine possible modulators of the enzyme in an attempt to associate this with the process of phagocytosis.
Department of Biology
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Clark, Graeme Christopher. "Characterisation and exploitation of clostridial phospholipase C." Thesis, Birkbeck (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.406120.

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Blank, Jonathan Louis. "The phospholipase C specific for the phosphoinositides." Thesis, University of Nottingham, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252943.

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Meldrum, Eric. "Isolation and characterization of mammalian phospholipase C." Thesis, Open University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.258438.

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Chrétien, Louise. "Régulation de l'activité de la phospholipase C par les récepteurs AT [indice] 1 de l'angiotensine II et B [indice] 2 de la bradykinine." Sherbrooke : Université de Sherbrooke, 1998.

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Nazih, Hassan. "Hdl3, plaquettes et seconds messagers : caracterisation et regulation du systeme de transduction." Lille 2, 1993. http://www.theses.fr/1993LIL2P261.

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Books on the topic "Phospholipase C"

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Tobin, A. B. The Phospholipase C pathway: Its regulation and desenisitization. Austin, TX: R.G. Landes, 1996.

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

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Perera, Nevin Martin. Phospholipase C activation is implicated in the responses of yeast to several stresses. Birmingham: University of Birmingham, 2002.

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Brind, Robert Ian. The characterisation of Plc1: A phospholipase C enzyme identified in the fission yeast Schizosaccharomyces pombe. [s.l.]: typescript, 2000.

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Idestrup, Chris. P2Y-and P2U-purinoceptor activation cause intracellualr CA2+ release in dorsal spinal astrocytes via the phospholipase C[BETA]/IP3 pathway. Ottawa: National Library of Canada, 1996.

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Slaaby, Rita. Cloning and characterisation of a phosphoinositide-specific phospholipase C in Schizosaccharomyces pombe and isolation and characterisation of pheromone induced cell cycle arrest mutants in Schizosaccharomyces pombe. Birmingham: University of Birmingham, 1996.

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N, Fain John, ed. Lipid metabolism in signalling systems. San Diego: Academic Press, Inc., 1993.

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N, Fain John, ed. Lipid metabolism in signaling systems. San Diego: Academic Press, 1993.

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Weingart, Christine L. A phospholipase C produced by Burkholderia cepacia. 1997.

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Weingart, Christine L. A phospholipase C produced by Burkholderia cepacia. 1997.

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Book chapters on the topic "Phospholipase C"

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Lackner, K. J., and D. Peetz. "Phospholipase C." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_2425-1.

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Lackner, K. J., and D. Peetz. "Phospholipase C." In Springer Reference Medizin, 1880. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2425.

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Vines, Charlotte M. "Phospholipase C." In Advances in Experimental Medicine and Biology, 235–54. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-2888-2_10.

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Schomburg, Dietmar, and Margit Salzmann. "Phospholipase C." In Enzyme Handbook 3, 543–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_115.

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Bill, Colin A., and Charlotte M. Vines. "Phospholipase C." In Advances in Experimental Medicine and Biology, 215–42. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12457-1_9.

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Cuatrecasas, Pedro. "Some Novel Phospholipase C Activities." In Cellular and Molecular Aspects of Inflammation, 405–12. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5487-1_20.

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Rhee, Sue Goo, and Yun Soo Bae. "Regulation of Phospholipase C isozymes." In Interacting Protein Domains, 87–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60848-3_14.

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Schomburg, Dietmar, and Dörte Stephan. "Variant-surface-glycoprotein phospholipase C." In Enzyme Handbook 15, 167–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58948-5_39.

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Pejchar, Přemysl, Günther F. E. Scherer, and Jan Martinec. "Assaying Nonspecific Phospholipase C Activity." In Methods in Molecular Biology, 193–203. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-401-2_18.

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Schinner, Franz, Richard Öhlinger, and Ellen Kandeler. "Bestimmung der Phospholipase C-Aktivität." In Bodenbiologische Arbeitsmethoden, 168–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-97284-3_39.

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Conference papers on the topic "Phospholipase C"

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Deykin, D., and R. M. Karmer. "DIRECT STIMULATIONOF CA2+-ACTIVATED HUMAN PLATELET PHOSPHOLIPASE A2 BY DIACYLGLYCEROL." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644673.

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These studies examined the effect of diacylglycerol on Ca2+-dependent phospholipase A2 from human platelets. Phospholipase A2 was solubilized and partially purified to a stable form in the presence of octylglucoside and its enzymatic activity determined using sonicated arachidonoyl phosphatidylcholine (PC) as substrate. (Kramer RM, et al: BBA 878:394, 1986) Phospholipase A2 activity was increased when dioleoylglycerc_ was incorporated into the substrate arachidonoyl-PC. In the presence of 1 uM (29 mol %) sn-1,2-dioleoylglycerol the enzymatic activity was stimulated 4.1-fold. Exogenously added sn-l-oleoyl-2-acetoylglycerol also enhanced phospholipase A2 activity, producing a maximal stimulation of 1.6-fold at a concentration of 25 uM. Comparative studies conducted with pancreatic, bee-venom and snake venom phospholipase A2 showed that the activity of these extracellular phospholipases towards the arachidonoyl-PC substrate was also increased by diacylglycerol, but the stimulation was less than observed for platelet phospholipase A2. We conclude that in stimulated platelets Ca2+-activated phospholipase A2 may be regulated by newly generated diacylglycerols, not only via protein kinase C-mediated events, but also directly through conformational changes imposed by the diglycerides on cellular membrane phospholipids.
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Lapetina, Eduardo G. "THE ROLE OF INOSITIDES, PHOSPHOLIPASE C AND G-PROTEINS IN RECEPTOR TRANSDUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644775.

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It is now widely recognized that the activation of phospholipase C by specific agonists leads to the formation of two second messengers: (1) inositol trisphosphate, which releases Ca2+ from the endoplasmic reticulum to the cytosol and (2) 1,2- diacylglycerol, which stimulates protein kinase C. In the past few years, GTP-binding proteins have been associated with the regulation of phospholipase C. However, the identity of the GTP-binding protein involved and the type of association with phospholipase C is not yet known. It is now recognized that there are two types of phospholipase C enzymes: (a) a soluble enzyme that has been characterized in several tissues and does not preferentially hydrolyze polyphospholinositides and (b) membrane-bound enzymes that are coupled to the receptors, specifically hydrolyzing polyphosphoinositides and activated by membrane guanine nucleotide-binding proteins. Recent reports have tried to assess the involvement of GTP-binding proteins in the agonist-induced stimulation of phospholipase C, and various related aspects have been reported. These are concerned with: (a) detection of various GTP-binding proteins in platelets, (b) the effects of known inhibitors of GTP-binding proteins such as GDPgS or pertussis toxin on the agonist-induced stimulation of phospholipase C, (c) the direct effects of stimulators of GTP-binding proteins such as GTP, GTP-analogs and fluoride on phospholipase C activity, (d) the possible association of GTP-binding proteins to cytosolic phospholipase C that would then lead to degradation of the membrane-bound inositides and (e) cytosolic phospholipase C response to the activation of cell surface receptors. The emerging information has had contradictory conclusions. (1) Pretreatment of saponin-permeabilized platelets with pertussis toxin has been shown to enhance and to inhibit the thrombin-induced activation of phospholipase C. Therefore, it is not clear if a G protein that is affected by pertussis toxin in a manner similar to Gi or Go plays a central role in activation of phospholipase C. (2) Studies on the effect of GDPβ;S are also conflicting indicating that there may be GTP-independent and/or -dependent pathways for the activation of phosphoinositide hydrolysis. (3) A cytosolic phospholipase C is activated by GTP, and it has been advanced that this activity might trigger the hydrolysis of membrane-bound inositides. A cytosolic GTP-binding protein might be involved in this action, and it is speculated that an α-subunit might be released to the cytoplasm by a receptor-coupled mechanism to activate phospholipase C. However, no direct evidence exists to support this conclusion. Moreover, the exact contribution of phospholipase C from the membranes or the cytosol to inositide hydrolysis in response to cellular agonists and the relationship of those activites to membrane-bound or soluble GTP-binding proteins are unknown. Our results indicate that the stimulation of phospholipase C in platelets by GDPβS and thrombin are affected differently by GDPβS. GDPgSinhibits the formation of inositol phosphates produced by GTPγS but not that induced by thrombin. Thrombin, therefore, can directly stimulate phospholipase C without the involvement of a “stimulatory” GTP-binding protein, such as Gs, for the agonist stimulation of adenylate cyclase. However, an “inhibitory” GTP-binding protein might have some influence on thrombin-stimulated phospholipase C, since in the presence of GDPγS thrombin produces a more profound stimulation of phospholipase C.This “inhibitory” GTP-binding protein might be ADP-ribosylated by pertussis toxin because pertussis toxin can also enhance thrombin action on phospholipase C activity. Therefore, phospholipase C that responds to thrombin could be different from the one that responds to GTPγS. Cytosolic phospholipase C can be activated by GTP or GTP analogs, and the one that responds to thrombin should be coupled to the receptors present in the plasma membrane. The initial action of thrombin is to directly activate the plasma membrane-bound phospholipase C and the mechanism of this activation is probably related to the proteolytic action of thrombin or the activation of platelet proteases by thrombin. In agreement with this, trypsin can also directly activate platelet phospholipase C and, subsequently, GTPyS produces further activation of phospholipase C. If these two mechanisms are operative in platelets, the inhibition of cytosolic phospholipase C by GDPβS would allow a larger fraction of inositides for degradation of the thrombin-stimulated phospholipase C, as our results show.
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Outlaw, Kennedy, Isaac J. Fisher, Kaushik Muralidharan, and Angeline Lyon. "Structural and Functional Characterization of Phospholipase C β3." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.249970.

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Nakashima, S., T. Tohmatsu, H. Hattori, A. Suganuma, and Y. Nozawa. "EVIDENCE FOR INVOLVEMENT OF GTP-BINDING PROTEIN IN ARACKIDONIC ACID RELEASE BY PHOSPHOLIPASE A2 IN PERMEABILIZED HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644631.

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Platelet activation is accompanied by the active metabolism of membrane phospholipids. Phosphoinositide breakdown by phospholipase C generates second messengers; inositol trisphosphate and diacylglycerol. Recently, it is suggested that GTP-binding protein is linked to the activation of phospholipase C as is true for adenylate cyclase. Although it is known that the receptor stimulation by agonists leads to generation of arachidonic acid, its molecular mechanism has not yet been clear. However, several studies in neutrophils and mast cells using pertussis toxin, have shown the possibility that a GTP-binding protein may act as an intermediary unit component between the receptor and phospholipase A2. The present study was therefore designed to examine the effect of GTP and its analogue GTPγS on the arachidonic acid release in saponin-permeabilized human platelets. GTP or GTPγS alone caused a small but significant liberation of arachidonic acid in permeabilized cells but not in intact cells. GTP or GTPγS was found to enhance thrombin-induced [3H]arachidonic acid release in saponi n-permeabi li zed human platelets. The release of arachidonic acid has been ascribed to activity of phospholipase A2 and/or to sequential action of phospholipase C and diacylglycerol lipase. Inhibitors of phospholipase C (neomycin)/ diacylglycerol lipase (RHC 80267) pathway of arachidonate liberation did not reduce the level of the [3H]arachidonic acid release. The loss of [3H]arachidonate radioactivity from phosphatidylcholine was almost complementary to the increment of released [3H]arachidonic acid, suggesting thrombin-induced hydrolysis of phosphatidylcholine by phospholipase A2. Although phospholipase A2 usually are described as having a requirement for calcium, the effect of GTPγS was more evident at lower calcium concentrations (buffer>0.1 mM>1.0 mM). These data thus indicate that release of arachidonic acid by phospholipase A2 in saponin-treated platelets is closely linked to GTP-binding protein which may decrease the calcium requirement for phospholipase A2 activation.
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Crouch, Michael F., and Eduardo G. Lapetina. "PHOSPHOLIPASE A2 ACTIVATION BY A MECHANISM SEPARATE TO THAT RESPONSIBLE FOR PHOSPHOLIPASE C STIMULATION IN ALPHA-THROMBIN-STIMULATED HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644470.

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The ability of cell surface receptor occupation to increase the activity of phospholipase A2 has been thought to be due to the prior activation of phospholipase C and an increase in the intracellular Ca2+ concentration. However, recent evidence from our and other laboratories has suggested that this may not be the case, but rather stimulation of phospholipase A2 may be under the control of separate receptor-activated events. We have investigated this further by comparing the ability of prostacyclin (PGI2) and epinephrine to alter platelet responses to thrombin and examining the resulting phospholipase A2 activities.Alpha-thrombin stimulated aggregation of human platelets, the formation of inositol phosphates and phosphatidic acid, mobilizaton of Ca2+ from internal stores and Ca2+ influx, protein phosporylation (47 kDa and 20 kDa) and arachidonic acid (AA) release. Each of these responses was partially inhibited by prostacyclin (PGI2) except that of AA release, which was abolished. In combination with epinephrine and PGI2, alpha-thrombin-induced aggregation, phosphatidic acid formation and protein phosphorylation were restored, but the release of AA only reached 50% of its control value. Epinephrine alone had no effect on any of these responses, either in the presence or absence of PGI2. Thus, alpha-thrombin-induced activation of phospholipase A2 is more sensitive to the effects of PGI2 than is phospholipase C, and supports the possibility that there are distinct control mechanisms for receptor activation of these enzymes. We are presently examining the role of Gs in the inhibition by PGI2 of platelet phospholipase A2 and of Gi in the thrombin stimulation of this enzyme
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Merkuleva, Iu A., D. N. Shcherbakov, and A. A. Bondar. "Development of recombinant phosphatidylcholine-specific phospholipase C from Bacillus thuringiensis." In ACTUAL PROBLEMS OF ORGANIC CHEMISTRY AND BIOTECHNOLOGY (OCBT2020): Proceedings of the International Scientific Conference. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0069626.

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Zhou, Mingjie, Cailan Zhang, and Richard P. Haugland. "Choline oxidase: a useful tool for high-throughput assays of acetylcholinesterase, phospholipase D, phosphatidylcholine-specific phospholipase C, and sphingomyelinase." In BiOS 2000 The International Symposium on Biomedical Optics, edited by Patrick A. Limbach, John C. Owicki, Ramesh Raghavachari, and Weihong Tan. SPIE, 2000. http://dx.doi.org/10.1117/12.380507.

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Scarlata, Suzanne, Loren Runnels, and Mario Rebecchi. "Detection of phospholipase C-β 2 activation by G-protein subunits." In BiOS '98 International Biomedical Optics Symposium, edited by Joseph R. Lakowicz and J. B. Alexander Ross. SPIE, 1998. http://dx.doi.org/10.1117/12.307051.

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Bijli, Kaiser M., Fabeha Fazal, Alan Smrcka, and Arshad Rahman. "Critical Role Of Phospholipase C Epsilon In Lipopolysaccharide-Induced Lung Inflammation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4189.

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Brass, L. F., D. R. Manning, and M. J. Woolkalis. "G PROTEIN REGULATORS OF PHOSPHOLIPASE C AND ADENYLATE CYCLASE IN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644630.

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The hydrolysis of polyphosphoinositides (PI) by phospholipase C during platelet activation produces two key intracellular messengers, inositol triphosphate and diacylglycerol. This process is thought to be regulated by a guanine nucleotide binding protein referred to as Gp. Although the evidence that Gp exists is compelling, to date it has not been isolated. Uncertainty about its identity has been compounded by variations between tissues in the susceptibility of Gp to pertussis toxin and by reconstitution studies which show that pertussis toxin-inhibited PI hydrolysis can be restored by purified Gi, the pertussis toxin-sensitive G protein which inhibits adenylate cyclase. Therefore, it remains unclear whether Gp represents a new G protein or a second role for Gj. When platelets permeabilized with saponin were incubated with pertussis toxin and 32P-NAD, a single 42 kDa protein was 32P-ADP-ribosylated which co-migrated with the purified a subunit of Gi. Preincubating the platelets with an agonist inhibited labeling of this protein by dissociating the G protein into subunits. The extent of inhibition correlated with the number of toxin-sensitive functions caused by the agonist. Labeling was abolished by thrombin, which inhibited cAMP formation and caused toxin-inhibitable PI hydrolysis. Labeling was partially inhibited by vasopressin and platelet activating factor, which caused toxin-inhibitable PI hydrolysis, but had no effect on cAMP formation and by epinephrine, which inhibited cAMP formation, but did not cause PI hydrolysis. Labeling was unaffected by the TxA2 analog U46619, which neither caused toxin-sensitive PI hydrolysis nor inhibited cAMP formation. These observations suggest that the 42 kDa band may contain a subunits from both Gp and Gi and, in fact, 2D electrophoresis resolved the 42 kDa protein band into two proteins with distinct pi. However, those agonists linked functionally only to Gp or only to Gi decreased the labeling of both proteins. Therefore, our data suggest (1) that Gj and Gp are the same protein and (2) that whether a aiven platelet agonist affects adenylate cyclase or phospholipase C or both depends upon factors extrinsic to the G protein.
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Reports on the topic "Phospholipase C"

1

Luberto, Chiara. Identification of the Elusive Mammalian Enzyme Phosphatidylcholine-Specific Phospholipase C. Fort Belvoir, VA: Defense Technical Information Center, July 2014. http://dx.doi.org/10.21236/ada611640.

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