Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2

Reynolds, Laure J.; Hughes, Lori L.; Louis, Andrew I.; Kramer, Ruth M.; Dennis, Edward A.

doi:10.1016/0005-2760(93)90229-3

Cited by 158 publications

(110 citation statements)

References 46 publications

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“…These results, together with the previous observation by Leslie (1 991), who detected lysophospholipase and phospholipase A, activities of arachidonoyl-preferential phospholipase A, in the mouse macrophage cell line RAW 264.7, strongly indicate that so-called cPLAz may generally mediate both phospholipase A, and lysophospholipase activities. A similar observation was recently reported by Reynolds et al (1993). Due to its high phospholipase A2 and lysophospholipase activities, cPLA, shows a resemblance to the phospholipase-B-type enzymes.…”

Section: Discussionsupporting

confidence: 88%

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A₂

Fujimori

Kudo

Fujita

et al. 1993

European Journal of Biochemistry

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Evidence has accumulated to suggest that a wide variety of mammalian cells and tissues express a cytosolic phospholipase A, with arachidonoyl preference (cPLA,). Purified rabbit platelet-derived cPLA,, as well as the human recombinant enzyme originally identified in the monocytic leukemic cell line U937, exhibit significant lysophospholipase activity. Several series of experiments indicated that a single protein mediated both activities. Treatment of the purified enzyme with p-bromophenacylbromide or an anti-(rabbit platelet cPLA,) monoclonal antibody, RHY-5, suppressed the activity of phospholipase A, without any appreciable effect on lysophospholipase activity, suggesting that the domain(s) required for phospholipase A, activity may be located separately from that for lysophospholipase activity. Lysophospholipase activity was appreciably detected above the critical micellar concentration of the substrate. Ly sophosphatidylcholine was also hydrolyzed efficiently when it was incorporated into liposomes made of dialkylphosphatidylcholine. The hydrolysis of lysophospholipid was dependent on the fatty acid bound at the sn, position; the relative rates of hydrolysis of 1 -oleoyllysophosphatidylcholine, 1-palmitoyllysophosphatidylcholine, and l-stearoyllysophosphatidylcholine were 23, 8, and 1, respectively. A similar order of reactivity was observed with lysophospholipid incorporated into dialkylphosphatidylcholine liposomes. cPLAz may function not only as an arachidonate liberation enzyme but also as an enzyme responsible for degradation of certain molecular species of lysophospholipids formed in membranes.

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Section: Discussionsupporting

confidence: 88%

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A₂

Fujimori

Kudo

Fujita

et al. 1993

European Journal of Biochemistry

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“…In contrast, Plb3p has lower lysophospholipase than phospholipase A activity. In this respect, Plb3p resembles mammalian cytosolic phospholipase A 2 , which also has lysophospholipase activity (32,33).…”

Section: Discussionmentioning

confidence: 99%

Characterization and Function in Vivo of Two Novel Phospholipases B/Lysophospholipases fromSaccharomyces cerevisiae

Merkel

Fido

Mayr

et al. 1999

Journal of Biological Chemistry

102

118

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The yeast genome contains two genes, designated as PLB2 and PLB3, that are 67% and 62% identical, respectively, to PLB1, which codes for a phospholipase B/lysophospholipase in yeast (Lee, S. K., Patton, J. L., Fido, M., Hines, L. K., Kohlwein, S. D., Paltauf, F., Henry, S. A., and Levin, D. E. (1994) J. Biol. Chem. 269, 19725-19730). Deletion and overexpression studies and in vivo and in vitro activity measurements suggest that both genes indeed code for phospholipases B/lysophospholipases. In cell free extracts of a plb1 plb2 plb3 triple mutant, no phospholipase B activity was detectable. Upon overexpression of PLB2 in a plb1 plb3 mutant background, phospholipase B activity was detectable in the plasma membrane, periplasmic space extracts and the culture supernatant. Similar to Plb1p, Plb2p appears to accept all major phospholipid classes, with a preference for acidic phospholipids including phosphatidylinositol 3,4-bisphosphate and phosphatidic acid. Consistent with a function as an extracellular lysophospholipase, PLB2 overexpression conferred resistance to lyso-phosphatidylcholine. Deletion of Plb2p function had no effect on glycerophosphoinositol or glycerophosphocholine release in vivo, in contrast to a deletion of Plb3p function, which resulted in a 50% reduction of phosphatidylinositol breakdown and glycerophosphoinositol release from the cells. In vitro, Plb3p hydrolyzes only phosphatidylinositol and phosphatidylserine and, to a lesser extent, their lysoanalogs. Plb3p activity in a plb1 plb2 mutant background was observed in periplasmic space extracts. Both Plb3p and Plb2p display transacylase activity in vitro, in the presence or absence, respectively, of detergent.Phospholipases B catalyze the hydrolytic cleavage of both acylester bonds of glycerophospholipids. Products of phospholipase B activity are fatty acids and water-soluble glycerophosphodiesters. In yeast, soluble degradation products are released to some extent into the culture medium, and are thus an indicator of cellular phospholipase B activity. The only acylester-hydrolyzing enzyme from yeast characterized so far at the molecular level is a phospholipase B encoded by the PLB1 gene (1). The highly glycosylated enzyme of about 220 kDa (73 kDa for the protein part, predicted from the sequence) is enriched in the yeast plasma membrane but was also found in the periplasmic space and in the culture supernatant. The lysophospholipase activity of Plb1p greatly exceeds the activity catalyzing the first step of hydrolysis; thus, lyso-phospholipids do not accumulate as intermediate products of Plb1p activity (2-4). In addition, this enzyme has transacylase activity, catalyzing the synthesis of phosphatidylcholine (PtdCho) 1 from two molecules of lyso-phosphatidylcholine. The physiological function of yeast phospholipase B is still unclear; neither disruption of the PLB1 gene nor its overexpression result in detectable growth phenotypes. However, the amount of glycerophosphocholine (GroPCho) and glycerophosphoethanolamine released into the culture su...

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“…Established PLA2 inhibitors like manoalide (Jacobson et al, 1990) and scalaradial (de Carvalho & Jacobs, 1991) inhibit this activity in vitro in a concentration-dependent manner. This enzyme presents the general characteristics of a secretory type II PLA2 with an optimum pH in the neutralbasic range, an absolute requirement for calcium ions for expression of full activity in the mM range and a lack of selectivity for arachidonic acid release, for it caused the release of [3H]-oleic acid from the 2-position of E. coli membrane phospholipids (Reynolds et al, 1993;Kudo et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

Involvement of secretory phospholipase A₂ activity in the zymosan rat air pouch model of inflammation

Payá

Terencio

Ferrándiz

et al. 1996

British J Pharmacology

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1 In the zymosan rat air pouch model of inflammation we have assessed the time dependence of phospholipase A2 (PLA2) accumulation in the inflammatory exudates as well as cell migration, myeloperoxidase activity, prostaglandin E2 (PGE2) and leukotriene B4 (LTB4) levels. 2 A significant increase in PLA2 activity was detected in 1,200 g supernatants of exudates 8 h after injection of zymosan into rat air pouch. This event coincided with peaks in cell accumulation (mainly neutrophils) and myeloperoxidase activity in exudates and was preceded by a rise in eicosanoid levels. 3 This enzyme (without further purification) behaved as a secretory type II PLA2 with an optimum pH at 7-8 units, lack of selectivity for arachidonate release and dependence on mM calcium concentrations for maximal activity. 4 The PLA2 inhibitors manoalide and scalaradial inhibited this enzyme activity in vitro in a concentration-dependent manner. Scalaradial also inhibited zymosan stimulated myeloperoxidase release in vitro.5 Injection of the marine PLA2 inhibitor scalaradial together with zymosan into the pouch at doses of 0.5, 1 and 5 umol per pouch resulted in a dose-dependent inhibition of PLA2 activity in exudates collected 8 h later. Myeloperoxidase levels and cell migration were also decreased, while eicosanoid levels were not modified. 6 Colchicine administration to rats prevented infiltration and decreased PLA2 levels in the 8 h zymosan-injected air pouch. 7 These results indicate that during inflammatory response to zymosan in the rat air pouch a secretory PLA2 activity is released into the exudates. The source of this activity is mainly the neutrophil which migrates into the pouch. 8 Scalaradial exerts anti-inflammatory effects in the zymosan air pouch.

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Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2

Cited by 158 publications

References 46 publications

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A₂

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A₂

Characterization and Function in Vivo of Two Novel Phospholipases B/Lysophospholipases fromSaccharomyces cerevisiae

Involvement of secretory phospholipase A₂ activity in the zymosan rat air pouch model of inflammation

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Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2

Cited by 158 publications

References 46 publications

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A2

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A2

Characterization and Function in Vivo of Two Novel Phospholipases B/Lysophospholipases fromSaccharomyces cerevisiae

Involvement of secretory phospholipase A2 activity in the zymosan rat air pouch model of inflammation

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Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A₂

Characteristics of lysophospholipase activity expressed by cytosolic phospholipase A₂

Involvement of secretory phospholipase A₂ activity in the zymosan rat air pouch model of inflammation