Log in

Relevant bibliographies by topics / Phospholipase A1 / Journal articles

To see the other types of publications on this topic, follow the link: Phospholipase A1.

Journal articles on the topic 'Phospholipase A1'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Phospholipase A1.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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, alpha 1- and alpha 2-adrenergic agonists respectively, had a stimulatory effect on the hydrolysis of the PE substrate. Guanosine 5′(-)[gamma-thio]triphosphate (GTP[S]) and guanosine 5′(-)[beta, gamma-imido]triphosphate, but not guanosine 5′(-)[beta-thio]diphosphate (GDP[S]) or adenosine 5′(-)[gamma-thio]triphosphate, stimulated the hydrolysis of 1-palmitoyl-2-linoleoyl-GPE by phospholipase A1. GDP[S] inhibited the isoprenaline-mediated stimulation of phospholipase A1 activity. Phospholipase A1 hydrolysis of 1-palmitoyl-2-linoleoyl-GPE was not dependent on cations; however, the stimulatory effects of isoprenaline and GTP[S] on the hydrolytic activity were abolished by cation chelators. The above data suggest that phospholipase A1 activity in guinea-pig heart microsomes is activated by the binding of isoprenaline to beta 2-adrenergic receptors. Furthermore the stimulation of phospholipase A1 activity by the agonist may be mediated via activation of G-proteins.

APA, Harvard, Vancouver, ISO, and other styles

2

Badiani, K., X. Lu та G. Arthur. "Evidence for the regulation of guinea-pig heart microsomal phosphatidylcholine-hydrolysing phospholipase A1 by guanosine 5′-[γ-thio]triphosphate". Biochemical Journal 288, № 3 (1992): 965–68. http://dx.doi.org/10.1042/bj2880965.

Full text

Abstract:

We have recently characterized lysophospholipase A2 activities in guinea-pig heart microsomes and postulated that these enzymes act sequentially with phospholipases A1 to release fatty acids selectively from phosphatidylcholine (PC) and phosphatidylethanolamine, thus providing an alternative route to the phospholipase A2 mode of release. In a further investigation of the postulated pathway, we have characterized the PC-hydrolysing phospholipase A1 in guinea-pig heart microsomes. Our results show that the enzyme may have a preference for substrates with C16:0 over C18:0 at the sn-1 position. In addition, although the enzyme cleaves the sn-1 fatty acid, the rate of hydrolysis of PC substrates with C16:0 at the sn-1 position was influenced by the nature of the fatty acid at the sn-2 position. The order of decreasing preference was C18:2 > C20:4 = C18:1 > C16:0. The hydrolyses of the molecular species were differentially affected by heating at 60 degrees C. An investigation into the effect of nucleotides on the activity of the enzyme showed that guanosine 5′-[gamma-thio]triphosphate (GTP[S]) inhibited the hydrolysis of PC by phospholipase A1 activity, whereas GTP, guanosine 5′-[beta-thio]diphosphate (GDP[S]), GDP, ATP and adenosine 5′-[gamma-thio]triphosphate (ATP[S]) did not affect the activity. The inhibitory effect of GTP[S] on phospholipase A1 activity was blocked by preincubation with GDP[S]. A differential effect of GTP[S] on the hydrolysis of different molecular species was also observed. Taken together, the results of this study suggest the presence of more than one phospholipase A1 in the microsomes with different substrate specificities, which act sequentially with lysophospholipase A2 to release linoleic or arachidonic acid selectively from PC under resting conditions. Upon stimulation and activation of the G-protein, the release of fatty acids would be inhibited.

APA, Harvard, Vancouver, ISO, and other styles

3

Reisfeld, Nurit, Dov Lichtenberg, Arie Dagan, and Saul Yedgar. "Apolipoprotein B exhibits phospholipase A1 and phospholipase A2 activities." FEBS Letters 315, no. 3 (1993): 267–70. http://dx.doi.org/10.1016/0014-5793(93)81176-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Tani, Katsuko, Takeshi Kogure, and Hiroki Inoue. "The intracellular phospholipase A1 protein family." BioMolecular Concepts 3, no. 5 (2012): 471–78. http://dx.doi.org/10.1515/bmc-2012-0014.

Full text

Abstract:

AbstractPhospholipase A1 is an enzyme that hydrolyzes phospholipids, producing 2-acyl-lysophospholipids and fatty acids. The intracellular phospholipase A1 (iPLA1) protein family is a relatively recently discovered lipid-metabolizing enzyme family. Lower eukaryotes, such as yeasts and nematodes, and plants have only one iPLA1 protein, whereas mammals have three iPLA1 family proteins (PA-PLA1/DDHD1/iPLA1α, p125/Sec23IP/iPLA1β and KIAA0725p/DDHD2/iPLA1γ). Mammalian iPLA1 proteins are localized in different cellular compartments, and two of them, p125 and KIAA0725p, have been implicated in membrane trafficking events. Recent gene targeting studies on several organisms showed that iPLA1 family proteins are involved in various physiological functions, including plant shoot gravitropism, epithelial stem cell differentiation and spermiogenesis. In this review, we describe the features of iPLA1 family proteins and recent progress regarding our understanding of their physiological functions.

APA, Harvard, Vancouver, ISO, and other styles

5

Inoue, Asuka, and Junken Aoki. "Phospholipase A1: structure, distribution and function." Future Lipidology 1, no. 6 (2006): 687–700. http://dx.doi.org/10.2217/17460875.1.6.687.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Merino, Susana, Alicia Aguilar, Maria Mercedes Nogueras, Miguel Regue, Simon Swift, and Juan M. Tomás. "Cloning, Sequencing, and Role in Virulence of Two Phospholipases (A1 and C) from Mesophilic Aeromonas sp. Serogroup O:34." Infection and Immunity 67, no. 8 (1999): 4008–13. http://dx.doi.org/10.1128/iai.67.8.4008-4013.1999.

Full text

Abstract:

ABSTRACT Two different representative recombinant clones encodingAeromonas hydrophila lipases were found upon screening on tributyrin (phospholipase A1) and egg yolk agar (lecithinase-phospholipase C) plates of a cosmid-based genomic library of Aeromonas hydrophila AH-3 (serogroup O34) introduced into Escherichia coli DH5α. Subcloning, nucleotide sequencing, and in vitro-coupled transcription-translation experiments showed that the phospholipase A1 (pla) and C (plc) genes code for an 83-kDa putative lipoprotein and a 65-kDa protein, respectively. Defined insertion mutants ofA. hydrophila AH-3 defective in either pla orplc genes were defective in phospholipase A1 and C activities, respectively. Lecithinase (phospholipase C) was shown to be cytotoxic but nonhemolytic or poorly hemolytic. A. hydrophila AH-3 plc mutants showed a more than 10-fold increase in their 50% lethal dose on fish and mice, and complementation of the plc single gene on these mutants abolished this effect, suggesting that Plc protein is a virulence factor in the mesophilic Aeromonas sp. serogroup O:34 infection process.

APA, Harvard, Vancouver, ISO, and other styles

7

KUNZE, Hans, Ernst BOHN, and Bernd-Michael LOFFLER. "Inhibitors of liver lysosomal acid phospholipase A1." European Journal of Biochemistry 177, no. 3 (1988): 591–95. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14411.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Manjula, Sarode, Anju Jose, Soundar Divakar, and Rangaswamy Subramanian. "Degumming rice bran oil using phospholipase-A1." European Journal of Lipid Science and Technology 113, no. 5 (2011): 658–64. http://dx.doi.org/10.1002/ejlt.201000376.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Kim, M. K., J. K. Kim, and J. S. Rhee. "Isolation of a phospholipase A1-producing microorganism." Journal of Industrial Microbiology 16, no. 3 (1996): 171–74. http://dx.doi.org/10.1007/bf01570000.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

YOSHIDA, TADASHI, SHOZO NAKAMOTO, RYUZI SAKAZAKI, et al. "Thielocins A1.ALPHA. and A1.BETA., novel phospholipase A2 inhibitors from ascomycetes." Journal of Antibiotics 44, no. 12 (1991): 1467–70. http://dx.doi.org/10.7164/antibiotics.44.1467.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Teajaroen, Withan, Suphaporn Phimwapi, Jureerut Daduang, Sompong Klaynongsruang, Varomyalin Tipmanee, and Sakda Daduang. "A Role of Newly Found Auxiliary Site in Phospholipase A1 from Thai Banded Tiger Wasp (Vespa affinis) in Its Enzymatic Enhancement: In Silico Homology Modeling and Molecular Dynamics Insights." Toxins 12, no. 8 (2020): 510. http://dx.doi.org/10.3390/toxins12080510.

Full text

Abstract:

Phospholipase A1 from Thai banded tiger wasp (Vespa affinis) venom also known as Ves a 1 plays an essential role in fatal vespid allergy. Ves a 1 becomes an important therapeutic target for toxin remedy. However, established Ves a 1 structure or a mechanism of Ves a 1 function were not well documented. This circumstance has prevented efficient design of a potential phospholipase A1 inhibitor. In our study, we successfully recruited homology modeling and molecular dynamic (MD) simulation to model Ves a 1 three-dimensional structure. The Ves a 1 structure along with dynamic behaviors were visualized and explained. In addition, we performed molecular docking of Ves a 1 with 1,2-Dimyristoyl-sn-glycero-3-phosphorylcholine (DMPC) lipid to assess a possible lipid binding site. Interestingly, molecular docking predicted another lipid binding region apart from its corresponding catalytic site, suggesting an auxiliary role of the alternative site at the Ves a 1 surface. The new molecular mechanism related to the surface lipid binding site (auxiliary site) provided better understanding of how phospholipase A1 structure facilitates its enzymatic function. This auxiliary site, conserved among Hymenoptera species as well as some mammalian lipases, could be a guide for interaction-based design of a novel phospholipase A1 inhibitor.

APA, Harvard, Vancouver, ISO, and other styles

12

Xiaoyang, Sun, Tian Shaojun, Zhang Lifen, and Xie Jianchun. "Effect of Phospholipase A1-Catalyzed Degumming on Oryzanol, Tocopherols, and Tocotrienols of Dewaxed Rice Bran Oil." Journal of Chemistry 2019 (March 27, 2019): 1–8. http://dx.doi.org/10.1155/2019/1608750.

Full text

Abstract:

The effect of phospholipase A1-catalyzed degumming on the phosphorus content, the retention rate of oryzanol, and total tocopherols and tocotrienols of dewaxed rice bran oil was investigated with comparison to water degumming and citric acid degumming. The fatty acid composition of dewaxed rice bran oil was also studied by gas chromatography. The phosphorus content of dewaxed rice bran oil after phospholipase A1-catalyzed degumming could be decreased from 332.5 mg·kg−1 to 9.3 mg·kg−1 with the citric acid dosage of 0.10%, high shearing rate of 23000 rpm, chelation time of 60 min, NaOH dosage of 1.5 mole equivalent to the amount of citric acid, reaction temperature of 50°C, and total water dosage of 2.5%, while the phosphorus content of dewaxed rice bran oil after water and acid degumming was 120.5 mg·kg−1 and 66.4 mg·kg−1, respectively. The retention rate of oryzanol and total tocopherols and tocotrienols was 97.58% and 96.81% for phospholipase A1-catalyzed degumming, 91.44% and 85.98% for water degumming, and 92.85% and 87.75% for acid degumming. There was no obvious change in fatty acid composition. The results indicated that phospholipase A1-catalyzed degumming was an effective method since it could decrease the phosphorus content to the required level and provide high retention rate of oryzanol and total content of tocopherols and tocotrienols without obvious change of fatty acid composition.

APA, Harvard, Vancouver, ISO, and other styles

13

Schmidt, D., and G. E. Hoffmann. "Activity of phospholipase A compared in serum of patients with pancreatic and nonpancreatic diseases." Clinical Chemistry 33, no. 4 (1987): 594–96. http://dx.doi.org/10.1093/clinchem/33.4.594.

Full text

Abstract:

Abstract Phospholipase A (PLA) activity was measured with a semi-automated photometric test system that is based on liberation of fatty acids from phosphatidylcholine by phospholipases A1 (EC 3.1.1.32) and A2 (EC 3.1.1.4). We studied 528 serum samples from 86 patients whose lipase activities were increased owing to pancreatitis, pancreatic carcinoma, and extrapancreatic diseases. PLA activity showed no correlation with lipase or amylase activities or with the primary cause of the disease, but was clearly related to prognosis. Noncomplicated acute pancreatitis was characterized by "normal" PLA activities (0-10 U/L), whereas the values (50-137 U/L) were highest in necrotizing pancreatitis and septicemia with a lethal outcome. Changes in lipase and phospholipase A activities exhibited completely different time courses in the various diagnostic groups.

APA, Harvard, Vancouver, ISO, and other styles

14

WAINSZELBAUM, Marisa, Estela ISOLA, Silvina WILKOWSKY, Joaquin J. B. CANNATA, Jorge FLORIN-CHRISTENSEN, and Monica FLORIN-CHRISTENSEN. "Lysosomal phospholipase A1 in Trypanosoma cruzi: an enzyme with a possible role in the pathogenesis of Chagas’ disease." Biochemical Journal 355, no. 3 (2001): 765–70. http://dx.doi.org/10.1042/bj3550765.

Full text

Abstract:

We found that, as in African trypanosomes, endogenous phospholipase A1 (Plase A1) activity can catalyse extensive deacylation of phospholipids upon cell death in all life stages of Trypanosoma cruzi. A major lysosomal Plase A1 was purified and characterized. The enzyme products can explain the lesions surrounding degenerating T. cruzi cells in host tissues. Thus Plase A1 emerges as a target to block pathogenesis in trypanosomal infections.

APA, Harvard, Vancouver, ISO, and other styles

15

Aoki, J. "Structure and function of phosphatidylserine-specific phospholipase A1." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1582, no. 1-3 (2002): 26–32. http://dx.doi.org/10.1016/s1388-1981(02)00134-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Nakawatari, Kazuki, Makoto Kurano, Osamu Araki, et al. "Elevated phosphatidylserine-specific phospholipase A1 level in hyperthyroidism." Clinica Chimica Acta 503 (April 2020): 99–106. http://dx.doi.org/10.1016/j.cca.2020.01.011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Kunze, H., and B. M. Löffler. "Acid phospholipase A1 in liver — A brief survey." Klinische Wochenschrift 67, no. 3 (1989): 126–30. http://dx.doi.org/10.1007/bf01711337.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Kubo, M., and K. Y. Hostetler. "Metabolic basis of diethylaminoethoxyhexestrol-induced phospholipid fatty liver." American Journal of Physiology-Endocrinology and Metabolism 252, no. 3 (1987): E375—E379. http://dx.doi.org/10.1152/ajpendo.1987.252.3.e375.

Full text

Abstract:

Diethylaminoethoxyhexestrol caused a foam cell lipidosis in humans characterized by phospholipid storage in the liver, spleen, and other tissues, and this represents the first description of acquired lipidosis caused by a drug. It has been proposed that diethylaminoethoxyhexestrol causes phospholipid fatty liver by concentrating in lysosomes and inhibiting phospholipases but it has not previously been possible to measure the intralysosomal concentration of diethylaminoethoxyhexestrol. In this paper we report for the first time the intralysosomal concentration of this drug in rats. After a single oral dose of diethylaminoethoxyhexestrol (100 mg/kg) the intralysosomal concentration was 7.9 mM at 2.5 h, 15.6 mM at 12 h, and 20.9 mM at 24 h, respectively. The total phospholipid content of lysosomes in drug-treated rats increased 1.9-, 6.0-, and 7.6-fold over control at 2.5, 12, and 24 h, respectively. Purified lysosomal phospholipase A1 was strongly inhibited by diethylaminoethoxyhexestrol in vitro. In phospholipid fatty liver, phospholipid accumulation in lysosomes appears to be caused by the presence of diethylaminoethoxyhexestrol in lysosomes at concentrations estimated to be 7.9–20 mM, because drug levels above 1 mM completely block the activity of purified lysosomal phospholipase A1 in vitro.

APA, Harvard, Vancouver, ISO, and other styles

19

Jiang, Xiaofei, Ming Chang, Xiaosan Wang, Qingzhe Jin, and Xingguo Wang. "A Comparative Study of Phospholipase A1 and Phospholipase C on Soybean Oil Degumming." Journal of the American Oil Chemists' Society 91, no. 12 (2014): 2125–34. http://dx.doi.org/10.1007/s11746-014-2555-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

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.

Full text

Abstract:

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 material. These include: phospholipase A1 and phospholipase A2, enzymes that release free fatty acid from the PI and GIPLs; an acyltransferase responsible for the acylation of the generated monoacyl or monoalkylglycerolipids with endogenous unlabelled fatty acid; two activities of phospholipase C, one releasing ceramide from IPC and the other alkylacylglycerol, alkylglycerol or diacylglycerol from PI. The neutral lipids were also generated on incubation of the GIPLs. The phospholipase C activities were inhibited by p-chloromercuriphenylsulphonic acid, as reported for other PI phospholipases C. An IPC-fatty-acid hydrolase, releasing fatty acid from the labelled IPC, was also observed. The enzyme activities reported in the present study may be acting in remodelling reactions leading to the anchor of the mature glycoproteins of T. cruzi.

APA, Harvard, Vancouver, ISO, and other styles

21

Flesch, Inge, Brigitte Schmidt, and Ernst Ferber. "Acylchain Specificity and Kinetic Properties of Phospholipase A1 and A2 of Bone Marrow-Derived Macrophages." Zeitschrift für Naturforschung C 40, no. 5-6 (1985): 356–63. http://dx.doi.org/10.1515/znc-1985-5-613.

Full text

Abstract:

Abstract The fatty acyl specificity of phospholipase A1 and A2 in homogenates of mouse bone marrow-derived macrophages was determined using phosphatidylcholine and phosphatidylethanolamine of different acylchain composition. Phosphatidylcholine with arachidonoyl at position 2 was cleaved preferentially by an alkaline phospholipase A2 (pH-optimum 9.0) leading to selective liberation of arachidonic acid. In contrast, phosphatidylcholines with oleoyl or linoleoyl at position 2 were degraded mainly by an acid phospholipase A1 (pH-optimum 4 -5) resulting in a conservation of these fatty acids esterified in lysophosphatides. Substrate kinetics of the alkaline phospholipase A2 revealed a 30 fold higher affinity (Km = 3.8 x 10-7 ᴍ) for 1-acyl-2-arachidonoyl-glycerophosphocholine compared to 1-acyl-2-oleoyl-glycerophosphocholine. The kinetic data were not influenced by endogenous lipids indicating that exogenous substrates do not equilibrate with cellular lipids. These results are suitable to explain a selective liberation of arachidonic acid from a mixture of phospholipids.

APA, Harvard, Vancouver, ISO, and other styles

22

Fujikawa, Yukichi, Ritsuko Fujikawa, Noriaki Iijima, and Muneharu Esaka. "Characterization of Secretory Phospholipase A2 with Phospholipase A1 Activity in Tobacco, Nicotiana tabacum (L.)." Lipids 47, no. 3 (2011): 303–12. http://dx.doi.org/10.1007/s11745-011-3632-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Murayama, Kazutaka, Kota Kano, Yusaku Matsumoto, and Daisuke Sugimori. "Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297." Journal of Structural Biology 182, no. 2 (2013): 192–96. http://dx.doi.org/10.1016/j.jsb.2013.02.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Kucera, G. L., C. Miller, P. J. Sisson, R. W. Wilcox, Z. Wiemer, and M. Waite. "Hydrolysis of thioester analogs by rat liver phospholipase A1." Journal of Biological Chemistry 263, no. 26 (1988): 12964–69. http://dx.doi.org/10.1016/s0021-9258(18)37657-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Belaunzarán, María Laura, Silvina Elizabeth Wilkowsky, Estela María Lammel, et al. "Phospholipase A1: A novel virulence factor in Trypanosoma cruzi." Molecular and Biochemical Parasitology 187, no. 2 (2013): 77–86. http://dx.doi.org/10.1016/j.molbiopara.2012.12.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Kucera, G. L., P. J. Sisson, M. J. Thomas, and M. Waite. "On the substrate specificity of rat liver phospholipase A1." Journal of Biological Chemistry 263, no. 4 (1988): 1920–28. http://dx.doi.org/10.1016/s0021-9258(19)77966-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Nishihara, Masaaki, Masazumi Kamata, Tomoyuki Koyama, and Kazunaga Yazawa. "New Phospholipase A1-producing Bacteria from a Marine Fish." Marine Biotechnology 10, no. 4 (2008): 382–87. http://dx.doi.org/10.1007/s10126-007-9074-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Schmidt, Brigitte, Käthe Hansen, and Ernst Ferber. "Secretion of phospholipase A1 by bone marrow-derived macrophages." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 836, no. 3 (1985): 312–20. http://dx.doi.org/10.1016/0005-2760(85)90135-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Waite, Moseley, Gernot Osthoff, Pat Sisson, and Tom Thuren. "Action of lysosomal phospholipase A1 on bis(monoacylglycerol)phosphate." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1128, no. 2-3 (1992): 281–84. http://dx.doi.org/10.1016/0005-2760(92)90319-q.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Pete, M. J., A. H. Ross, and J. H. Exton. "Purification and properties of phospholipase A1 from bovine brain." Journal of Biological Chemistry 269, no. 30 (1994): 19494–500. http://dx.doi.org/10.1016/s0021-9258(17)32196-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Nalbone, G., and K. Y. Hostetler. "Subcellular localization of the phospholipases A of rat heart: evidence for a cytosolic phospholipase A1." Journal of Lipid Research 26, no. 1 (1985): 104–14. http://dx.doi.org/10.1016/s0022-2275(20)34409-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Vecchi, Lara, Thaise Gonçalves Araújo, Fernanda Van Petten de Vasconcelos Azevedo, et al. "Phospholipase A2 Drives Tumorigenesis and Cancer Aggressiveness through Its Interaction with Annexin A1." Cells 10, no. 6 (2021): 1472. http://dx.doi.org/10.3390/cells10061472.

Full text

Abstract:

Phospholipids are suggested to drive tumorigenesis through their essential role in inflammation. Phospholipase A2 (PLA2) is a phospholipid metabolizing enzyme that releases free fatty acids, mostly arachidonic acid, and lysophospholipids, which contribute to the development of the tumor microenvironment (TME), promoting immune evasion, angiogenesis, tumor growth, and invasiveness. The mechanisms mediated by PLA2 are not fully understood, especially because an important inhibitory molecule, Annexin A1, is present in the TME but does not exert its action. Here, we will discuss how Annexin A1 in cancer does not inhibit PLA2 leading to both pro-inflammatory and pro-tumoral signaling pathways. Moreover, Annexin A1 promotes the release of cancer-derived exosomes, which also lead to the enrichment of PLA2 and COX-1 and COX-2 enzymes, contributing to TME formation. In this review, we aim to describe the role of PLA2 in the establishment of TME, focusing on cancer-derived exosomes, and modulatory activities of Annexin A1. Unraveling how these proteins interact in the cancer context can reveal new strategies for the treatment of different tumors. We will also describe the possible strategies to inhibit PLA2 and the approaches that could be used in order to resume the anti-PLA2 function of Annexin A1.

APA, Harvard, Vancouver, ISO, and other styles

33

Yoshida, Hiroshi, Yosuke Tsujishita, Françoise Hullin, et al. "Isolation and Properties of a Novel Phospholipase a from Rat Brain That Hydrolyses Fatty Acids at sn-1 and sn-2 Positions." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 35, no. 2 (1998): 295–301. http://dx.doi.org/10.1177/000456329803500216.

Full text

Abstract:

A Ca2+-independent phospholipase A that releases various fatty acids from sn-1 and sn-2 positions was partially purified from rat brain soluble fraction. The enzyme showed an approximate molecular mass of 300 kDa on gel filtration column chromatography. Its enzymatic properties are distinct from those of well characterized phospholipase A2 enzymes; by using a series of synthetic phosphatidylcholines, the enzyme cleaved oleic, linoleic, and arachidonic acids like phospholipase A2, and released palmitic and stearic acids like phospholipase A1. Phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, and phosphatidic acid were hydrolysed with almost equal efficiencies by this enzyme. These results indicate that the enzyme isolated is a novel Ca2+ -independent intracellular phospholipase A that might be responsible for production of various fatty acids from membrane phospholipids.

APA, Harvard, Vancouver, ISO, and other styles

34

Bott, Emanuel, María Gabriela López, Estela María Lammel, et al. "Cellular localization, cloning and expression of Leishmania braziliensis Phospholipase A1." Microbial Pathogenesis 141 (April 2020): 104010. http://dx.doi.org/10.1016/j.micpath.2020.104010.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Saxena, M., J. K. Gupta, and D. V. Vadehra. "Factors affecting intra- and extracellular phospholipase A1 production bySalmonella newport." Folia Microbiologica 34, no. 3 (1989): 195–201. http://dx.doi.org/10.1007/bf02821292.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Hölbling, N., H. El-Kalak, A. Georgopoulos, L. Stilianu, and G. Hacker. "Phospholipase-A1 and -A2 in experimental acute pancreatitis in rats." Research In Experimental Medicine 185, no. 2 (1985): 131–37. http://dx.doi.org/10.1007/bf01854898.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Wang, Yong, Mouming Zhao, Keke Song, Lili Wang, Shuze Tang, and William W. Riley. "Partial hydrolysis of soybean oil by phospholipase A1 (Lecitase Ultra)." Food Chemistry 121, no. 4 (2010): 1066–72. http://dx.doi.org/10.1016/j.foodchem.2010.01.051.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Pete, Matthew J., and John H. Exton. "Phospholipid interactions affect substrate hydrolysis by bovine brain phospholipase A1." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1256, no. 3 (1995): 367–73. http://dx.doi.org/10.1016/0005-2760(95)00047-g.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Wang, J., X. Y. Wen, A. K. Stewart, and R. A. Hegele. "Polymorphisms in the gene encoding phosphatidylserine-specific phospholipase A1 (PSPLA1)." Journal of Human Genetics 47, no. 11 (2002): 0611–13. http://dx.doi.org/10.1007/s100380200093.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Pappu, Anuradha S., Paul J. Yazaki, and Karl Y. Hostetler. "Inhibition of purified lysosomal phospholipase A1 by beta-adrenoceptor blockers." Biochemical Pharmacology 34, no. 4 (1985): 521–24. http://dx.doi.org/10.1016/0006-2952(85)90183-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Cheng, Shi, Zitao Guo, Chaojuan Liang, et al. "Immobilization of Phospholipase A1 Using a Protein-Inorganic Hybrid System." Polymers 13, no. 17 (2021): 2865. http://dx.doi.org/10.3390/polym13172865.

Full text

Abstract:

In this study, four kinds of phospholipase A1-metal (Al/Co/Cu/Mn) hybrid nanostructures were prepared for enhancing the stability of the free PLA1. The formed hybrid complexes were characterized by scanning electron microscope (SEM), Fourier infrared spectroscopy (FTIR), and X-ray diffraction (XRD). The stability and substrate specificity of immobilized enzymes were subsequently determined. After immobilization, the temperature tolerance of PLA1–metal hybrid nanostructures was enhanced. The relative activity of PLA1–Al/Co/Cu hybrid nanostructures remained above 60% at 50 °C, while that of free enzyme was below 5%. The thermal transition temperature measured by differential scanning calorimetry (DSC) was found to increase from 65.59 °C (free enzyme) to 173.14 °C, 123.67 °C, 96.31 °C, and 114.79 °C, referring to PLA1–Cu/Co/Al/Mn hybrid nanostructures, respectively. Additionally, after a storage for fourteen days at 4 °C, the immobilized enzymes could exhibit approximately 60% of the initial activity, while the free PLA1 was inactivated after four days of storage. In brief, using Co2+, Cu2+, Al3+, and Mn2+ as the hybridization materials for immobilization could improve the catalytic properties and stability of the free PLA1, suggesting a promising method for a wider application of PLA1 in many fields such as food, cosmetics, and the pharmaceutical industry.

APA, Harvard, Vancouver, ISO, and other styles

42

Jackson, Edwin K., Dongmei Cheng, Stevan P. Tofovic, and Zaichuan Mi. "Endogenous adenosine contributes to renal sympathetic neurotransmission via postjunctional A1 receptor-mediated coincident signaling." American Journal of Physiology-Renal Physiology 302, no. 4 (2012): F466—F476. http://dx.doi.org/10.1152/ajprenal.00495.2011.

Full text

Abstract:

Adenosine A1 receptor antagonists have diuretic/natriuretic activity and may be useful for treating sodium-retaining diseases, many of which are associated with increased renal sympathetic tone. Therefore, it is important to determine whether A1 receptor antagonists alter renal sympathetic neurotransmission. In isolated, perfused rat kidneys, renal vasoconstriction induced by renal sympathetic nerve simulation was attenuated by 1) 1,3-dipropyl-8-p-sulfophenylxanthine (xanthine analog that is a nonselective adenosine receptor antagonist, but is cell membrane impermeable and thus does not block intracellular phosphodiesterases), 2) xanthine amine congener (xanthine analog that is a selective A1 receptor antagonist), 3) 1,3-dipropyl-8-cyclopentylxanthine (xanthine analog that is a highly selective A1 receptor antagonist), and 4) FK453 (nonxanthine analog that is a highly selective A1 receptor antagonist). In contrast, FR113452 (enantiomer of FK453 that does not block A1 receptors), MRS-1754 (selective A2B receptor antagonist), and VUF-5574 (selective A3 receptor antagonist) did not alter responses to renal sympathetic nerve stimulation, and ZM-241385 (selective A2A receptor antagonist) enhanced responses. Antagonism of A1 receptors did not alter renal spillover of norepinephrine. 2-Chloro- N6-cyclopentyladenosine (highly selective A1 receptor agonist) increased renal vasoconstriction induced by exogenous norepinephrine, an effect that was blocked by 1,3-dipropyl-8-cyclopentylxanthine, U73122 (phospholipase C inhibitor), GF109203X (protein kinase C inhibitor), PP1 (c-src inhibitor), wortmannin (phosphatidylinositol 3-kinase inhibitor), and OSU-03012 (3-phosphoinositide-dependent protein kinase-1 inhibitor). These results indicate that adenosine formed during renal sympathetic nerve stimulation enhances the postjunctional effects of released norepinephrine via coincident signaling and contributes to renal sympathetic neurotransmission. Likely, the coincident signaling pathway is: phospholipase C → protein kinase C → c-src → phosphatidylinositol 3-kinase → 3-phosphoinositide-dependent protein kinase-1.

APA, Harvard, Vancouver, ISO, and other styles

43

BELAUNZARÁN, M. L., M. J. WAINSZELBAUM, E. M. LAMMEL, et al. "Phospholipase A1 from Trypanosoma cruzi infective stages generates lipid messengers that activate host cell protein kinase c." Parasitology 134, no. 4 (2006): 491–502. http://dx.doi.org/10.1017/s0031182006001740.

Full text

Abstract:

Here we have studied phospholipase A1 (Plase A1) from Trypanosoma cruzi infective stages and it's possible role regarding the interaction with mammalian host cells. Plase A1 was mainly detected as a membrane-bound activity in the infective amastigote and trypomastigote stages, being remarkably higher with respect to the non-infective epimastigotes. It is noteworthy that only the infective stages secreted Plase A1. Moreover, along the differentiation process from epimastigotes into metacyclic trypomastigotes, the secreted enzyme activity increased simultaneously with the appearance of metacyclic forms, as expected. Since this enzyme is predominantly membrane-associated and secreted by the infective stages, Vero cell lipid profile modifications were analysed after interaction with either intact infective parasites or purified T. cruzi Plase A1. Significant changes in Vero cell lipid composition were observed, with the appearance of free fatty acids, diacylglycerol and lysophosphatidylcholine. Concomitantly with the generation of second lipid messengers, host cell protein kinase C activation was demonstrated. These results indicate that T. cruzi Plase A1 could play a critical role in the early events of parasite-host cell interaction that precede invasion.

APA, Harvard, Vancouver, ISO, and other styles

44

Guo, Min, Rongjuan Pei, Qi Yang, et al. "Phosphatidylserine-Specific Phospholipase A1 Involved in Hepatitis C Virus Assembly through NS2 Complex Formation." Journal of Virology 89, no. 4 (2014): 2367–77. http://dx.doi.org/10.1128/jvi.02982-14.

Full text

Abstract:

ABSTRACTSeveral members of the phospholipase family have been reported to be involved in hepatitis C virus (HCV) replication. Here, we identified another phospholipase, phosphatidylserine-specific phospholipase A1 (PLA1A), as a host factor involved in HCV assembly. PLA1A was upregulated by HCV infection, and PLA1A knockdown significantly reduced J399EM (genotype 2a) HCV propagation at the assembly step but not the entry, RNA replication, and protein translation steps of the life cycle. Protein localization and interaction analysis further revealed a role of PLA1A in the interaction of NS2-E2 and NS2-NS5A, as the formation of the NS2-E2 and NS2-NS5A complexes was weakened in the absence of PLA1A. In addition, PLA1A stabilized the NS2/NS5A dotted structure during infection. These data suggest that PLA1A plays an important role in bridging the membrane-associated NS2-E2 complex and the NS5A-associated replication complex via its interaction with E2, NS2, and NS5A, which leads to a coordinating interaction between the structural and nonstructural proteins and facilitates viral assembly.IMPORTANCEHepatitis C virus (HCV) genomic replication is driven by the replication complex and occurs at the membranous web, while the lipid droplet is the organelle in which virion assembly is initiated. In this study, we identified phosphatidylserine-specific phospholipase A1 (PLA1A), a member of phospholipase A 1 family, as a novel host factor involved in the assembly process of HCV. PLA1A, which is induced by HCV infection at a late infection stage, interacts with HCV E2, NS2, and NS5A proteins and enhances and stabilizes the NS2-E2 and NS2-NS5A complex formation, which is essential for viral assembly. Thus, PLA1A is an important host factor which is involved in the initiation of the viral assembly in close proximity to Core-decorated lipid droplets through bringing together the HCV replication complex and envelope complex.

APA, Harvard, Vancouver, ISO, and other styles

45

Tavernier, Eric, and Alain Pugin. "Phospholipase activities associated with the tonoplast from Acer pseudoplatanus cells: identification of a phospholipase A1 activity." Biochimica et Biophysica Acta (BBA) - Biomembranes 1233, no. 2 (1995): 118–22. http://dx.doi.org/10.1016/0005-2736(94)00273-r.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Wang, DingYan, Adili Reheman, Phil Connelly, et al. "Genetic Disruption of □pdl and □pdlr Phospholipases in Mice Leads to Impaired Platelet Adhesion and Aggregation." Blood 112, no. 11 (2008): 412. http://dx.doi.org/10.1182/blood.v112.11.412.412.

Full text

Abstract:

Abstract Platelet adhesion and aggregation are critical events in thrombosis. Bioactive phospholipid LPA (lysophosphatidic acid) has been identified as an important agonist for platelet aggregation. Plasma LPA can be generated from phospholipid substrates by phospholipase A1 (PLA1) and phospholipase D (PLD). We previously identified two novel PLA1 enzymes, designated lpdl (lpd lipase) and lpdlr (lpdl related lipase). Together with phosphatidylserine phospholipase A1 (PS-PLA1), these three phospholipases form a unique PLA1 lipase subfamily. Phospholipids are important structural components of cellular membranes. Recent studies demonstrate that lipid raft microdomains on the platelet membrane contribute to platelet activation. The gathering of membrane lipid rafts is necessary for ADP-mediated platelet activation. Disruption of lipid raft results in a reduction of ADP-induced platelet aggregation. In addition, it is reported that alteration of membrane lipid composition also affects the function of platelet β3 integrin (GPIIbIIIa). Thus, phospholipases may play an important role in platelet function. However, the roles of lpdl and lpdlr in platelet activation and thrombosis are unknown. To study the function of lpdl and lpdlr, we have recently knocked out both lpdl and lpdlr genes in mice by deleting their exons I and II, including their translation start codon ATG. RT-PCR confirmed that neither lpdl nor lpdlr gene is expressed in homozygous lpdl−/− or lpdlr−/− mice but expressed in wild-type (WT) tissues, indicating successful knockout of these phospholipases. Next, optical platelet aggregometry was used to assess platelet aggregation in platelet rich plasma (PRP). Platelet aggregation was induced with 5, 10 and 20 μM ADP in pooled PRP (3×108 platelets/mL) from age- and sex-matched WT, heterozygous and homozygous mice. Our results demonstrated that both the lpdl−/− and lpdlr−/− mice have decreased platelet aggregation after ADP stimulation. We further studied thrombus formation in lpdl−/− mice using an ex vivo perfusion chamber model on collagen type I-coated rectangular glass microcapillary tubes. Our preliminary data showed that both platelet adhesion and aggregation were impaired in the lpdl−/− mice. We are repeating these experiments and are examining lpdlr−/− mice using the same perfusion chamber model. In vivo thrombosis models with intravital microscopy and the mechanisms of how lpdl and lpdlr enzymes regulate platelet activation will also be investigated. These studies could potentially identify a novel pathway for regulation of platelet function, which may lead to development of new diagnostic and/or therapeutic methods for atherothrombosis. (Drs. D. Wang and A. Reheman contribute equally to this work)

APA, Harvard, Vancouver, ISO, and other styles

47

Shamburek, R. D., L. A. Zech, P. S. Cooper, J. M. Vandenbroek, and C. C. Schwartz. "Disappearance of two major phosphatidylcholines from plasma is predominantly via LCAT and hepatic lipase." American Journal of Physiology-Endocrinology and Metabolism 271, no. 6 (1996): E1073—E1082. http://dx.doi.org/10.1152/ajpendo.1996.271.6.e1073.

Full text

Abstract:

Metabolism of 1-stearoyl-2-arachidonyl-phosphatidyl-choline (SAPC), a major phosphatidylcholine (PC) species in rat plasma, was compared with 1-palmitoyl-2-linoleoyl-PC (PLPC) metabolism. High-density lipoproteins containing SAPC and PLPC tracers labeled in the sn-2 fatty acid with 3H and 14C isotopes, respectively, were administered. The rats were depleted of endogenous bile acids and infused via the ileum with individual bile acids that ranged widely in hydrophobicity. The half-lives for SAPC and PLPC in plasma were 48 and 57 min, respectively. Most of the 3H activity that disappeared from plasma at 1 h was found in the liver in 1-palmitoyl-2-arachidonyl-PC, SAPC, and 1-oleoyl-2-arachidonyl-PC, indicating phospholipase A1 hydrolysis of plasma SAPC forming 2-arachidonyl-lysophosphatidylcholine, which was reacylated in the liver. Plasma PLPC also underwent phospholipase A1 hydrolysis, as reported previously. The fraction of 3H dose that accumulated in plasma cholesteryl arachidonate was two- to threefold higher than the fraction of 14C dose in cholesteryl linoleate. Multicompartmental models for SAPC and PLPC were developed that included lysophosphatidylcholines and cholesteryl esters. Bile acids did not influence plasma PC metabolism. Lecithin-cholesterol acyltransferase and phospholipase A1 (hepatic lipase) hydrolysis accounted for > or = 90% of the SAPC and PLPC that disappeared from plasma; SAPC and PLPC are comparable as substrates for hepatic lipase, but SAPC is preferred by lecithin-cholesterol acyltransferase.

APA, Harvard, Vancouver, ISO, and other styles

48

Hsuan, S. L., M. S. Kannan, S. Jeyaseelan, Y. S. Prakash, G. C. Sieck, and S. K. Maheswaran. "Pasteurella haemolytica A1-Derived Leukotoxin and Endotoxin Induce Intracellular Calcium Elevation in Bovine Alveolar Macrophages by Different Signaling Pathways." Infection and Immunity 66, no. 6 (1998): 2836–44. http://dx.doi.org/10.1128/iai.66.6.2836-2844.1998.

Full text

Abstract:

ABSTRACT Leukotoxin and endotoxin derived from Pasteurella haemolytica serotype 1 are the primary virulence factors contributing to the pathogenesis of lung injury in bovine pneumonic pasteurellosis. Activation of bovine alveolar macrophages with endotoxin or leukotoxin results in the induction of cytokine gene expression, with different kinetics (H. S. Yoo, S. K. Maheswaran, G. Lin, E. L. Townsend, and T. R. Ames, Infect. Immun. 63:381–388, 1995; H. S. Yoo, B. S. Rajagopal, S. K. Maheswaran, and T. R. Ames, Microb. Pathog. 18:237–252, 1995). Furthermore, extracellular Ca2+ is required for leukotoxin-induced cytokine gene expression. However, the involvement of Ca2+ in endotoxin effects and the precise signaling mechanisms in the regulation of intracellular Ca2+ by leukotoxin and endotoxin are not known. In fura-2-acetoxymethyl ester-loaded alveolar macrophages, intracellular Ca2+regulation by leukotoxin and endotoxin was studied by video fluorescence microscopy. Leukotoxin induced a sustained elevation of intracellular Ca2+ in a concentration-dependent fashion by influx of extracellular Ca2+ through voltage-gated channels. In the presence of fetal bovine serum, endotoxin elevated intracellular Ca2+ even in the absence of extracellular Ca2+. Leukotoxin-induced intracellular Ca2+elevation was inhibited by pertussis toxin, inhibitors of phospholipases A2 and C, and the arachidonic acid analog 5,8,11,14-eicosatetraynoic acid. Intracellular Ca2+elevation by endotoxin was inhibited by inhibitors of phospholipase C and protein tyrosine kinase, but not by pertussis toxin, or the arachidonic acid analog. To the best of our knowledge, this is the first report of Ca2+ signaling by leukotoxin through a G-protein-coupled mechanism involving activation of phospholipases A2 and C and release of arachidonic acid in bovine alveolar macrophages. Ca2+ signaling by endotoxin, on the other hand, involves activation of phospholipase C and requires tyrosine phosphorylation. The differences in the Ca2+ signaling mechanisms may underlie the reported temporal differences in gene expression during leukotoxin and endotoxin activation.

APA, Harvard, Vancouver, ISO, and other styles

49

Spanoghe, Jeroen, Lars E. Larsen, Erine Craey, et al. "The Signaling Pathways Involved in the Anticonvulsive Effects of the Adenosine A1 Receptor." International Journal of Molecular Sciences 22, no. 1 (2020): 320. http://dx.doi.org/10.3390/ijms22010320.

Full text

Abstract:

Adenosine acts as an endogenous anticonvulsant and seizure terminator in the brain. Many of its anticonvulsive effects are mediated through the activation of the adenosine A1 receptor, a G protein-coupled receptor with a wide array of targets. Activating A1 receptors is an effective approach to suppress seizures. This review gives an overview of the neuronal targets of the adenosine A1 receptor focusing in particular on signaling pathways resulting in neuronal inhibition. These include direct interactions of G protein subunits, the adenyl cyclase pathway and the phospholipase C pathway, which all mediate neuronal hyperpolarization and suppression of synaptic transmission. Additionally, the contribution of the guanyl cyclase and mitogen-activated protein kinase cascades to the seizure-suppressing effects of A1 receptor activation are discussed. This review ends with the cautionary note that chronic activation of the A1 receptor might have detrimental effects, which will need to be avoided when pursuing A1 receptor-based epilepsy therapies.

APA, Harvard, Vancouver, ISO, and other styles

50

Jiang, Xiaofei, Ming Chang, Qingzhe Jin, and Xingguo Wang. "Application of phospholipase A1 and phospholipase C in the degumming process of different kinds of crude oils." Process Biochemistry 50, no. 3 (2015): 432–37. http://dx.doi.org/10.1016/j.procbio.2014.12.011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!