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Journal articles on the topic 'Phospholipase C'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Bollag, Wendy B. "Role of phospholipases in adrenal steroidogenesis." Journal of Endocrinology 229, no. 1 (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

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2

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

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3

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 (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

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4

Karasawa, Tadahiro, Xingmin Wang, Tsuneo Maegawa, et al. "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 (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% o

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5

Teitelbaum, I. "Hormone signaling systems in inner medullary collecting ducts." American Journal of Physiology-Renal Physiology 263, no. 6 (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 sig

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6

Ghannoum, Mahmoud A. "Potential Role of Phospholipases in Virulence and Fungal Pathogenesis." Clinical Microbiology Reviews 13, no. 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 glabr

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7

LITTLE, CLIVE. "Phospholipase C." Biochemical Society Transactions 17, no. 2 (1989): 271–73. http://dx.doi.org/10.1042/bst0170271.

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8

Heo, Yunseok, Inhwan Lee, Sunjin Moon, et al. "Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain." Molecules 27, no. 7 (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

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9

Tanabe, Kumiko, Osamu Kozawa, Hiroyuki Matsuno, Masayuki Niwa, Shuji Dohi, and Toshihiko Uematsu. "Effect of Propofol on Arachidonate Cascade by Vasopressin in Aortic Smooth Muscle Cells." Anesthesiology 90, no. 1 (1999): 215–24. http://dx.doi.org/10.1097/00000542-199901000-00028.

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Background The mechanisms underlying the vascular effects of propofol are not fully understood. Vasopressin, a potent vasoactive peptide, stimulates the arachidonate cascade and the synthesis of prostacyclin (PGI2; the main metabolite of the cascade in vascular smooth muscle cells). Arachidonic acid (AA) release by phospholipases is the rate-limiting step in the cascade. We investigated the mechanisms underlying vasopressin-induced AA release and the effect of propofol on PGI2 synthesis in a rat aortic smooth muscle cell line: A10 cells. Methods In cultured A10 cells pretreated with propofol,

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10

Inamori, K., N. Sagawa, M. Hasegawa, H. Itoh, J. Yano, and T. Mori. "Activation of phospholipase D in cultured human amnion cells." Reproduction, Fertility and Development 7, no. 6 (1995): 1591. http://dx.doi.org/10.1071/rd9951591.

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The regulation of phospholipase D (PLD) activity in the human amniotic membrane was examined using primary cultures of amnion cells. Cultured amnion cells were labelled with [3H]oleic acid, and PLD activity was determined as the amount of [3H]phosphatidylethanol (PEt) produced during incubation in the presence of 0.1% ethanol. PLD activity in cultured amnion cells was activated by addition of arginine vasopressin and oxytocin. PLD activity was also stimulated by treatment was arachidonic acid, the product of phospholipase A2 (PLA2), and phospholipase C (PLC). These results indicate that PLD in

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11

D'Eça Júnior, Aurean, Anderson França Silva, Fernanda Costa Rosa, Sílvio Gomes Monteiro, Patrícia de Maria Silva Figueiredo, and Cristina de Andrade Monteiro. "In vitro differential activity of phospholipases and acid proteinases of clinical isolates of Candida." Revista da Sociedade Brasileira de Medicina Tropical 44, no. 3 (2011): 334–38. http://dx.doi.org/10.1590/s0037-86822011005000036.

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INTRODUCTION: Candida yeasts are commensals; however, if the balance of normal flora is disrupted or the immune defenses are compromised, Candida species can cause disease manifestations. Several attributes contribute to the virulence and pathogenicity of Candida, including the production of extracellular hydrolytic enzymes, particularly phospholipase and proteinase. This study aimed to investigate the in vitro activity of phospholipases and acid proteinases in clinical isolates of Candida spp. METHODS: Eighty-two isolates from hospitalized patients collected from various sites of origin were

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Umemura, Atsushi, Hideo Mabe, Hajime Nagai, and Fumihiko sugino. "Action of phospholipases A2 and C on free fatty acid release during complete ischemia in rat neocortex." Journal of Neurosurgery 76, no. 4 (1992): 648–51. http://dx.doi.org/10.3171/jns.1992.76.4.0648.

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✓ The levels of brain free fatty acids rapidly increase after the onset of ischemia. The purpose of this study was to investigate the action of phospholipases A2 and C during complete ischemia based on the effects of a phospholipase C inhibitor (phenylmethylsulfonyl fluoride) and the N-methyl-D-aspartate antagonist MK-801 on the release of free fatty acids in rat neocortex. Complete brain ischemia was induced in rats with cardiac arrest by intracardiac injection of KC1. Free fatty acid levels in the neocortex were measured 0, 2, 4, and 8 minutes after cardiac arrest. Phenylmethylsulfonyl fluor

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13

Kadamur, Ganesh, and Elliott M. Ross. "Mammalian Phospholipase C." Annual Review of Physiology 75, no. 1 (2013): 127–54. http://dx.doi.org/10.1146/annurev-physiol-030212-183750.

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14

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

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15

Kunze, Donika, Inga Melzer, Désirée Bennett, et al. "Functional analysis of the phospholipase C gene CaPLC1 and two unusual phospholipase C genes, CaPLC2 and CaPLC3, of Candida albicans." Microbiology 151, no. 10 (2005): 3381–94. http://dx.doi.org/10.1099/mic.0.28353-0.

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Phospholipases C are known to be important regulators of cellular processes but may also act as virulence factors of pathogenic microbes. At least three genes in the genome of the human-pathogenic fungus Candida albicans encode phospholipases with conserved phospholipase C (Plc) motifs. None of the deduced protein sequences contain N-terminal signal peptides, suggesting that these phospholipases are not secreted. In contrast to its orthologue in Sacharomyces cerevisiae, CaPLC1 seems to be an essential gene. However, a conditional mutant with reduced transcript levels of CaPLC1 had phenotypes s

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Cross, M. J., M. N. Hodgkin, S. Roberts, E. Landgren, M. J. Wakelam, and L. Claesson-Welsh. "Tyrosine 766 in the fibroblast growth factor receptor-1 is required for FGF-stimulation of phospholipase C, phospholipase D, phospholipase A(2), phosphoinositide 3-kinase and cytoskeletal reorganisation in porcine aortic endothelial cells." Journal of Cell Science 113, no. 4 (2000): 643–51. http://dx.doi.org/10.1242/jcs.113.4.643.

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Fibroblast growth factor-mediated signalling was studied in porcine aortic endothelial cells expressing either wild-type fibroblast growth factor receptor-1 or a mutant receptor (Y766F) unable to bind phospholipase C-(γ). Stimulation of cells expressing the wild-type receptor resulted in activation of phospholipases C, D and A(2) and increased phosphoinositide 3-kinase activity. Stimulation of the wild-type receptor also resulted in stress fibre formation and a cellular shape change. Cells expressing the Y766F mutant receptor failed to stimulate phospholipase C, D and A(2) as well as phosphoin

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17

González-Mendoza, Víctor M., M. E. Sánchez-Sandoval, Lizbeth A. Castro-Concha, and S. M. Teresa Hernández-Sotomayor. "Phospholipases C and D and Their Role in Biotic and Abiotic Stresses." Plants 10, no. 5 (2021): 921. http://dx.doi.org/10.3390/plants10050921.

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Plants, as sessile organisms, have adapted a fine sensing system to monitor environmental changes, therefore allowing the regulation of their responses. As the interaction between plants and environmental changes begins at the surface, these changes are detected by components in the plasma membrane, where a molecule receptor generates a lipid signaling cascade via enzymes, such as phospholipases (PLs). Phospholipids are the key structural components of plasma membranes and signaling cascades. They exist in a wide range of species and in different proportions, with conversion processes that inv

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18

BERTELLO, Laura E., Maria Júlia M. ALVES, Walter COLLI, and Rosa M. de LEDERKREMER. "Evidence for phospholipases from Trypanosoma cruzi active on phosphatidylinositol and inositolphosphoceramide." Biochemical Journal 345, no. 1 (1999): 77–84. http://dx.doi.org/10.1042/bj3450077.

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The lipid moiety in the glycosylphosphatidylinositol anchors of glycoproteins of Trypanosoma cruzi consists of an alkylacylglycerol, a lysoalkylglycerol or a ceramide. Previously, we showed that the inositolphosphoceramides (IPCs) are the major components in the precursor inositolphospholipids of epimastigote and trypomastigote forms. Using 3H-labelled subfractions of IPC, phosphatidylinositol (PI) and glycoinositolphospholipids (GIPLs) as substrates with a cell-free system, we now demonstrate the association of at least five enzyme activities with the trypanosomal membranous particulate mater

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19

Cockcroft, S., and J. Stutchfield. "The receptors for ATP and fMetLeuPhe are independently coupled to phospholipases C and A2 via G-protein(s). Relationship between phospholipase C and A2 activation and exocytosis in HL60 cells and human neutrophils." Biochemical Journal 263, no. 3 (1989): 715–23. http://dx.doi.org/10.1042/bj2630715.

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The relationship between phospholipase A2 and C activation and secretion was investigated in intact human neutrophils and differentiated HL60 cells. Activation by either ATP or fMetLeuPhe leads to [3H]arachidonic acid release into the external medium from prelabelled cells. This response was inhibited when the cells were pretreated with pertussis toxin. When the [3H]arachidonic acid-labelled cells were stimulated with fMetLeuPhe, ATP or Ca2+ ionophore A23187, and the lipids analysed by t.l.c., the increase in free fatty acid was accompanied by decreases in label from phosphatidylinositol and p

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20

Sharom, Frances J., Gary L. McNeil, John R. Glover, and Sandra Seier. "Modulation of the cleavage of glycosylphosphatidylinositol-anchored proteins by specific bacterial phospholipases." Biochemistry and Cell Biology 74, no. 5 (1996): 701–13. http://dx.doi.org/10.1139/o96-077.

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Many enzymes are tethered to the extracellular face of the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. These proteins can be released in soluble form by the action of GPI-specific phospholipases. Little is currently known about the factors modulating this release. We investigated the effects of several experimental variables on the cleavage of the GPI-anchored proteins 5′-nucleotidase, acetylcholinesterase, and alkaline phosphatase by phospholipases from Bacillus thuringiensis and Staphylococcus aureus. Phospholipase activity was not inhibited by isotonic salt and was relat

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21

Watkins, D. C., C. M. Moxham, A. J. Morris та C. C. Malbon. "Suppression of Giα2 enhances phospholipase C signalling". Biochemical Journal 299, № 3 (1994): 593–96. http://dx.doi.org/10.1042/bj2990593.

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G-proteins mediate transmembrane signalling from a populous group of cell-surface receptors to a smaller group of effectors that includes adenylate cyclase, various ion channels and phospholipase C. Stem cells (F9 teratocarcinoma) or rat osteosarcoma 17/2.8 cells in which Gi alpha 2 expression is abolished by antisense RNA display markedly elevated basal inositol 1,4,5-trisphosphate accumulation and a potentiated phospholipase C response to stimulatory hormones. Expression of the Q205L mutant of Gi alpha 2, which is constitutively active, was found to block persistently hormonally stimulated p

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22

Liu, M., J. Xu, J. Liu, M. E. Kraw, A. K. Tanswell, and M. Post. "Mechanical strain-enhanced fetal lung cell proliferation is mediated by phospholipase C and D and protein kinase C." American Journal of Physiology-Lung Cellular and Molecular Physiology 268, no. 5 (1995): L729—L738. http://dx.doi.org/10.1152/ajplung.1995.268.5.l729.

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The signaling pathways by which intermittent strain (60 cycles/min, 15 min/h) regulates proliferation of mixed fetal rat lung cell in vitro have been investigated. Adenosine 3',5'-cyclic monophosphate (cAMP) content and cAMP-dependent protein kinase (PKA) activity were not affected by strain. The stimulatory effect of strain on DNA synthesis was also not influenced by the cyclic nucleotide-dependent protein kinase inhibitors H-8 or HA-1004, the adenylate cyclase inhibitor SQ-22536, or a PKA inhibitor and cAMP antagonist, adenosine 3',5'-cyclic monophosphothioate (Rp-cAMPS). In contrast, intrac

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Bomalaski, John S., Fusao Hirata, and Mike A. Clark. "Aspirin inhibits phospholipase C." Biochemical and Biophysical Research Communications 139, no. 1 (1986): 115–21. http://dx.doi.org/10.1016/s0006-291x(86)80087-0.

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24

Wahl, Matthew, and Graham Carpenter. "Selective phospholipase C activation." BioEssays 13, no. 3 (1991): 107–13. http://dx.doi.org/10.1002/bies.950130303.

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25

Fisher, Isaac J., Kaushik Muralidharan, Kennedy Outlaw, and Elisabeth Garland-Kuntz. "Resolving phospholipase C regulation." Acta Crystallographica Section A Foundations and Advances 79, a1 (2023): a22. http://dx.doi.org/10.1107/s2053273323099771.

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26

Bominaar, A. A., and P. J. Van Haastert. "Chemotactic antagonists of cAMP inhibit Dictyostelium phospholipase C." Journal of Cell Science 104, no. 1 (1993): 181–85. http://dx.doi.org/10.1242/jcs.104.1.181.

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In Dictyostelium discoideum extracellular cAMP induces chemotaxis via a transmembrane signal transduction cascade consisting of surface cAMP receptors, G-proteins and effector enzymes including adenylyl cyclase, guanylyl cyclase and phospholipase C. Previously it was demonstrated that some cAMP derivatives such as 3′-deoxy-3′-aminoadenosine 3′:5′-monophosphate (3′NH-cAMP) bind to the receptor and induce normal activation of adenylyl cyclase and guanylyl cyclase. However these analogues do not induce chemotaxis, probably because the signal is transduced in an inappropriate manner. We have now s

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27

Kolesnikov, Y. S., S. V. Kretynin, V. S. Kravets, and Y. K. Bukhonska. "Phosphatidic acid formation and signaling in plant cells." Ukrainian Biochemical Journal 96, no. 1 (2024): 5–21. http://dx.doi.org/10.15407/ubj96.01.005.

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This review conteins updated information on the structure, localization and regulation of phosphatidic acid (PA)-producing enzymes phospholipase D, phosphoinositide-specific and non-specific phospholipases C and diacylglycerol kinases is analyzed. The specific role of PA and PA-producing enzymes in plant stress signaling is discussed.

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28

Krjukova, Jelena, Tomas Holmqvist, Alexander S. Danis, Karl E. O. Åkerman, and Jyrki P. Kukkonen. "Phospholipase C activator m -3M3FBS affects Ca2+ homeostasis independently of phospholipase C activation." British Journal of Pharmacology 143, no. 1 (2004): 3–7. http://dx.doi.org/10.1038/sj.bjp.0705911.

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29

Kiss, Zoltan, and Nandor Garamszegi. "Protein kinase C-dependent stimulation of phospholipase D in phospholipase C-treated fibroblasts." Lipids 28, no. 6 (1993): 479–81. http://dx.doi.org/10.1007/bf02536077.

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30

Badiani, K., and G. Arthur. "Evidence for receptor and G-protein regulation of a phosphatidylethanolamine-hydrolysing phospholipase A1 in guinea-pig heart microsomes: stimulation of phospholipase A1 activity by DL-isoprenaline and guanine nucleotides." Biochemical Journal 312, no. 3 (1995): 805–9. http://dx.doi.org/10.1042/bj3120805.

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While evidence has been presented for the receptor-mediated activation of phospholipases A2, C and D, the activation of phospholipase A1 subsequent to receptor activation has not been established. Phospholipase A1-catalysed hydrolysis of 1-palmitoyl-2-linoleoyl-glycerophosphoethanolamine (GPE) by guinea-pig heart microsomes was stimulated 40-60% by isoprenaline. This isoprenaline-mediated increase in activity was blocked by propranolol and butoxamine, a specific beta 2-adrenergic antagonist, but not by atenolol, a specific beta 1-adrenergic antagonist. Neither clonidine nor phenylephrine, alph

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Nakamura, Yuki, and Anh H. Ngo. "Correction to: Non-specific phospholipase C (NPC): an emerging class of phospholipase C in plant growth and development." Journal of Plant Research 134, no. 2 (2021): 365. http://dx.doi.org/10.1007/s10265-020-01251-7.

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32

Lahkar, Vicky, Lahari Saikia, Saurav J. Patgiri, Reema Nath, and Partha Pratim Das. "Estimation of biofilm, proteinase & phospholipase production of the Candida species isolated from the oropharyngeal samples in HIV-infected patients." Indian Journal of Medical Research 145, no. 5 (2017): 635–40. https://doi.org/10.4103/ijmr.ijmr_1773_14.

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Background & objectives: Candida, the most common opportunistic infection in acquired immunodeficiency syndrome (AIDS), attributes its pathogenicity to its virulence factors, mainly the biofilms, the proteinases and the phospholipases. There is a significant interplay of these factors during the HIV infection. This study was aimed to estimate the biofilm, proteinase and phospholipase production in Candida species isolated from the oropharyngeal samples in the HIV-infected patients. Methods: A total of 126 consecutive HIV-positive patients were screened for Candida growth using oropharyngea

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Goñi, Félix M., and Alicia Alonso. "Membrane Fusion Induced by Phospholipase C and Sphingomyelinases." Bioscience Reports 20, no. 6 (2000): 443–63. http://dx.doi.org/10.1023/a:1010450702670.

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In the past decade lipid vesicle fusion induced by either bacterial PC-preferring phospholipase C, phosphatidylinositol-specific phospholipase C, sphingomyelinase, or a combination of phospholipase C and sphingomyelinase has been demonstrated. In the present paper, the experimental evidence is reviewed, and discussed in terms of the underlying molecular mechanisms of fusion, and of the possible physiological relevance of these findings.

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Mahadevappa, V. G., and Frank Sicilia. "Mobilization of arachidonic acid in thrombin-stimulated human platelets." Biochemistry and Cell Biology 68, no. 2 (1990): 520–27. http://dx.doi.org/10.1139/o90-074.

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In the present work we investigated the effect of serine esterase inhibitors such as 2-nitro-4-carboxyphenyl N,N-diphenylcarbamate (NCDC) and phenylmethylsulfonyl fluoride (PMSF), as well as the effect of mepacrine on thrombin-induced mobilization of arachidonic acid (AA) in human platelets. The inhibitor NCDC (0.6 mM) completely abolished the thrombin-induced activation of phospholipase C, phospholipase A2, and transacylase enzymes, whereas the pretreatment of platelets with PMSF (2 mM) resulted in a highly selective inhibition of phospholipase A2 and transacylase activities, with no marked e

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Purkiss, J. R., and M. R. Boarder. "Stimulation of phosphatidate synthesis in endothelial cells in response to P2-receptor activation. Evidence for phospholipase C and phospholipase D involvement, phosphatidate and diacylglycerol interconversion and the role of protein kinase C." Biochemical Journal 287, no. 1 (1992): 31–36. http://dx.doi.org/10.1042/bj2870031.

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To investigate the stimulation of phosphatidic acid formation in bovine aortic endothelial cells by P2-purinergic agonists, we labelled AG4762 cells with [32P]P1 and stimulated in the presence of butanol. Under these conditions phospholipase D generated [32P]phosphatidylbutanol, whereas the [32P]phosphatidic acid from phospholipase C and diacylglycerol kinase was unchanged. The action of various purinergic agonists on both [32P]phosphatidic acid and [32P]phosphatidylbutanol was consistent with the presence of a P2Y receptor. The stimulation of phospholipase D was dependent on extracellular Ca2

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36

Ganendren, Ranjini, Fred Widmer, Vatsala Singhal, Christabel Wilson, Tania Sorrell, and Lesley Wright. "In Vitro Antifungal Activities of Inhibitors of Phospholipases from the Fungal Pathogen Cryptococcus neoformans." Antimicrobial Agents and Chemotherapy 48, no. 5 (2004): 1561–69. http://dx.doi.org/10.1128/aac.48.5.1561-1569.2004.

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ABSTRACT Secreted phospholipase B is a proven virulence factor for the pathogenic fungus Cryptococcus neoformans and exhibits three phospholipase activities in the one protein. These are phospholipase B (PLB), lysophospholipase (LPL), and lysophospholipase transacylase (LPTA). Our aim was to investigate the feasibility of using this enzyme as a target for antifungal therapy. We determined in C. neoformans var. grubii strain H99 that 82% of PLB activity was secreted but that 64% of LPL activity and 70% of LPTA activity were cell associated. Cell-associated activities (cytosolic and membrane) we

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Rice, K. L., P. G. Duane, G. Mielke, A. A. Sinha, and D. E. Niewoehner. "Calcium ionophores injure alveolar epithelial cells: relation to phospholipase activity." American Journal of Physiology-Lung Cellular and Molecular Physiology 259, no. 6 (1990): L439—L450. http://dx.doi.org/10.1152/ajplung.1990.259.6.l439.

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Phospholipases and certain of their hydrolytic products are toxic to alveolar epithelial cells. Since many intracellular phospholipases are Ca2+ dependent, we postulated that elevating cytosolic Ca2+ with ionophores might cause epithelial injury via phospholipase activation. Isolated perfused hamster lungs exposed to an Ca2+ ionophore A23187 develop functional evidence of severe epithelial injury. Ultrastructural studies show widespread lysis of type I epithelial cells, with only minimal abnormalities in other lung cells, including the microvascular endothelium. Analysis of whole lung lipid ex

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Ortiz-Placín, Cándido, Alba Castillejo-Rufo, Matías Estarás, and Antonio González. "Membrane Lipid Derivatives: Roles of Arachidonic Acid and Its Metabolites in Pancreatic Physiology and Pathophysiology." Molecules 28, no. 11 (2023): 4316. http://dx.doi.org/10.3390/molecules28114316.

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One of the most important constituents of the cell membrane is arachidonic acid. Lipids forming part of the cellular membrane can be metabolized in a variety of cellular types of the body by a family of enzymes termed phospholipases: phospholipase A2, phospholipase C and phospholipase D. Phospholipase A2 is considered the most important enzyme type for the release of arachidonic acid. The latter is subsequently subjected to metabolization via different enzymes. Three enzymatic pathways, involving the enzymes cyclooxygenase, lipoxygenase and cytochrome P450, transform the lipid derivative into

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Rubin, R., and J. B. Hoek. "Alcohol-induced stimulation of phospholipase C in human platelets requires G-protein activation." Biochemical Journal 254, no. 1 (1988): 147–53. http://dx.doi.org/10.1042/bj2540147.

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In previous studies we have demonstrated that ethanol activates hormone-sensitive phospholipase C in intact human platelets, resulting in the mobilization of intracellular Ca2+ and platelet shape change. The present study aims to localize further this effect of ethanol by examining its interaction with the regulation of phospholipase C in a permeabilized cell system. In platelets permeabilized with a minimal concentration (18 micrograms/ml) of saponin, ethanol by itself did not activate phospholipase C. However, ethanol potentiated the activation of phospholipase C in response to the non-hydro

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Rupwate, Sunny D., and Ram Rajasekharan. "Plant phosphoinositide-specific phospholipase C." Plant Signaling & Behavior 7, no. 10 (2012): 1281–83. http://dx.doi.org/10.4161/psb.21436.

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41

Goñi, Félix M., José L. Nieva, Gorka Basañez, Gerardo Fidelio, and Alicia Alonso. "Phospholipase-C-promoted liposome fusion." Biochemical Society Transactions 22, no. 3 (1994): 839–44. http://dx.doi.org/10.1042/bst0220839.

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Williams, Roger L. "Mammalian phosphoinositide-specific phospholipase C." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1441, no. 2-3 (1999): 255–67. http://dx.doi.org/10.1016/s1388-1981(99)00150-x.

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Cocco, Lucio, Alberto M. Martelli, R. Stewart Gilmour, Sue Goo Rhee, and Francesco A. Manzoli. "Nuclear phospholipase C and signaling." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1530, no. 1 (2001): 1–14. http://dx.doi.org/10.1016/s1388-1981(00)00169-4.

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Jones, Gwenith, and Graham Carpenter. "Regulation of phospholipase C isozymes." Progress in Growth Factor Research 4, no. 2 (1992): 97–106. http://dx.doi.org/10.1016/0955-2235(92)90025-d.

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Eberhard, David A., and Ronald W. Holz. "Intracellular Ca2+ activates phospholipase C." Trends in Neurosciences 11, no. 12 (1988): 517–20. http://dx.doi.org/10.1016/0166-2236(88)90174-9.

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Kostadinova, S. "Phospholipase C fromPseudomonas FluorescensStrain B." Biotechnology & Biotechnological Equipment 11, no. 3-4 (1997): 38–42. http://dx.doi.org/10.1080/13102818.1997.10818951.

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Horowitz, Lisa F., Wiebke Hirdes, Byung-Chang Suh, Donald W. Hilgemann, Ken Mackie, and Bertil Hille. "Phospholipase C in Living Cells." Journal of General Physiology 126, no. 3 (2005): 243–62. http://dx.doi.org/10.1085/jgp.200509309.

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We have further tested the hypothesis that receptor-mediated modulation of KCNQ channels involves depletion of phosphatidylinositol 4,5-bisphosphate (PIP2) by phosphoinositide-specific phospholipase C (PLC). We used four parallel assays to characterize the agonist-induced PLC response of cells (tsA or CHO cells) expressing M1 muscarinic receptors: translocation of two fluorescent probes for membrane lipids, release of calcium from intracellular stores, and chemical measurement of acidic lipids. Occupation of M1 receptors activates PLC and consumes cellular PIP2 in less than a minute and also p

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Tsutsumi, T., T. Kobayashi, M. Miyashita, S. Watanabe, Y. Homma, and H. Okuyama. "A Lysophosphoinositide-Specific Phospholipase C Distinct from Other Phospholipase C Families in Rat Brain." Archives of Biochemistry and Biophysics 317, no. 2 (1995): 331–36. http://dx.doi.org/10.1006/abbi.1995.1171.

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Singer, William D., H. Alex Brown, and, and Paul C. Sternweis. "REGULATION OF EUKARYOTIC PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C AND PHOSPHOLIPASE D." Annual Review of Biochemistry 66, no. 1 (1997): 475–509. http://dx.doi.org/10.1146/annurev.biochem.66.1.475.

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Wang, Z. "Phospholipase C- 1: A Phospholipase and Guanine Nucleotide Exchange Factor." Molecular Interventions 2, no. 6 (2002): 352–55. http://dx.doi.org/10.1124/mi.2.6.352.

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