• The Journal of the Korean Society for Microbiology
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• v.22 no.4
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• pp.403-411
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• 1987

This study investigated whether a correlation exists between proteinase activity, phospholipase activity and adherence of Candida albicans to buccal epithelial cells by using of various strains isolated from oral cavity. The proteinase activity of 30 strains was tested by culture on agar media that contained bovine serum albumin as a nitrogen source. Using the serum-protein-agar method to test proterolysis of serum albumin in 20 strains of Candida albicans. Twenty-six strains of Candida albicans were phospholipase producers and the degree of phopholipase activity of experimental strains were $0.51{\sim}0.89$ measured by Pz-value. Twenty-eight strains of Candida albicans were adhersive to buccal epithelial cells and 15 strains were foung significantly active adherence. Fifteen strains of Candida albicans were correlated with proteinase activity and adherence to epithelial cells and concomitantly 20 strains of Candida albicans were also correlated with phospholipase activity and adherence. In conclusion our investigation provides evidence of a correlation between quantitative proteinase, phospholipase and adherence. An association of these parameters may be an important contributory factor for pathogenicity.

• YAKHAK HOEJI
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• v.45 no.3
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• pp.287-292
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• 2001

To investigate whether phospholipase $A_2$pathway is involved in histamine release of rat peritoneal mast cells, we measured histamine release in the presence of various enzyme inhibitors involved in eicosanoid pathway, such as phospholipase $A_2$, cyclooxygenase and lipoxygenase. Phospholipase $A_2$inhibitors, manoalide and OPC, significantly inhibited histamine release induced by 100 $\mu$M ATP and 1$\mu$g/ml compound 48/80. Cyclooxygenase inhibitors, ibuprofen and indomethacin, significantly inhibited ATP-induced histamine release and lipoxygenase inhibitors, baicalein and caffeic acid, also significantly inhibited. To investigate the involvement of protein kinase in ATP- and compound 48/80-induced histamine release, we observed effects of protein kinase inhibitors on histamine release. Bisindolmaleimide (protein kinase C antagonist) dose-dependently inhibited both ATP and compound 48/80-induced histamine release. Tyrosine kinase inhibitors (methyl 2,5-dihydroxy cinnamate and genistein) dose-dependently inhibited ATP and compound 48/80-induced histamine release. Protein kinase C and tyrosine kinase seem to be involved in histamine release induced by ATP and compound 48/80. These results suggest that phospholipase $A_2$pathway as well as protein kinase C and tyrosine kinase are involved in histamine release of rat peritoneal mast cells by ATP and compound 48/80.

• Natural Product Sciences
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• v.26 no.4
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• pp.259-267
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• 2020

Snakebite is a severe medical, economic, and social problem across the world, mostly in the tropical and subtropical area. These regions of the globe have typical of the world's venomous snakes present where access to prompt treatment is limited or not available. Snake venom is a complex mixture of toxin proteins like neurotoxin and cardiotoxin, and other enzymes like phospholipase A2 (PLA2), haemorrhaging, transaminase, hyaluronidase, phosphodiesterase, acetylcholinesterase, cytolytic and necrotic toxins. Snake venom shows a wide range of biological effects like anticoagulation or platelet aggregation, hemolysis, hypotension and edema. Phospholipase A2 is the principal constituent of snake venom; it catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid, which is the precursor of eicosanoids including prostaglandins and leukotrienes. The information regarding the structure and function of the phospholipase A2 enzyme may help in treating the snakebite victims. This review article constitutes a brief description of the structure, types, mechanism occurrence, and tests of phospholipase A2 and role of components of medicinal plants used to inhibit phospholipase A2.

• Journal of the Korean Chemical Society
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• v.52 no.5
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• pp.488-494
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• 2008

• Natural Product Sciences
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• v.7 no.1
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• pp.17-20
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• 2001

The activity of the lipase and phospholipase extracted from the seed meal of Nicotiana tabacum L. was studied with the help of Spectrophotometer at different pH, Temperatures and Solvents. Both lipase and phospholipase shown optimum activity at pH 6 and $45^{\circ}C$. Their activities also maximize when n-heptane was used as solvent media.

• YAKHAK HOEJI
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• v.39 no.5
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• pp.554-559
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• 1995

MT 2511-5 was purified as a inhibitor of phospholipase C(PLC) from culture broth of a Streptmyces sp. NO. 2511-5. It was identified as scopafungin, 36-membered marcrolide by physico-chemical and spectroscopic data. Its $IC_{50}$ was 30.mu.M against phospholipase C and it also showed inhibitory activity against some fungi.

• The Korean Journal of Pharmacology
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• v.27 no.2
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• pp.191-196
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• 1991

The present study was performed to determine whether estradiol, via cAMP mediation, induces prostaglandin synthesis by modulating phospholipase $A_2$ activity which hydrolyzes phospholipids into arachidonic acids, a precursor for prostaglandin synthesis, during the implantation process in rats. Uterine phospholipase $A_2$ activity was elevated on day 5 of pregnancy when implantation normally occurs in rats. Moreover, phospholipase $A_2$ activity was higher in the implant sites than in the non-implant sites of uterus on day 6. In delayed implantation model, phospholipase $A_2$ activity was increased at 12 hrs after estradiol administration and at 8 hrs after dbcAMP administration. In addition, higher activity of phospholipase $A_2$ was induced by the treatment of estradiol plus theophylline, compared with estradiol-only treated group. The simultaneous treatment of indomethacin with estradiol or dbcAMP did not alter phospholipase $A_2$ activity compared with estradiol or dbcAMP-only treated group although significant suppression was observed in uterine PGE and $PGF_{2{\alpha}}$ concentrations. These results suggest that estradiol or cAMP stimulates uterine phospholipase $A_2$ activity, thereby increasing prostaglandin synthesis during the implantation process in rats.

• BMB Reports
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• v.30 no.2
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• pp.101-105
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• 1997

Extracellular phospholipase $A_2$ activity has been detected in urine of patients with acute pyelonephritis (APN). This enzyme required micromolar $Ca^{2+}$ ion for its maximum activity and showed a broad range of pH (4.5~10) optimum. Urine enzyme hydrolyzed phosphatidylethanolamine (PE) and phosphatidylserine (PS) more effectively than phosphatidylcholine (PC). $PLA_2$ activity in the urine of patients with APN was about 5-fold higher than that of healthy individuals. When urine was subjected to heparinSepharose column chromatography, phospholipase $A_2$ activity was detected in both heparin-non-binding and binding fractions. Both phospholipase $A_2$ activities were sensitive less than a micromolar calcium concentration and did not react with anti-human 14-kDa group II phospholipase $A_2$ monoclonal antibody, HP-l. These findings suggest that two kinds of novel extracellular phospholipase $A_2$. which may not belong to the 14-kDa group II phospholipase $A_2$ family, exist in the urine of patients with APN.

• YAKHAK HOEJI
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• v.49 no.5
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• pp.405-409
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• 2005

To investigate anti-inflammatory activity of Noni extracts, we measured the phospholipase $A_2$ activity using both in vitro and in vivo system. Water soluble fraction of Noni extracts did not affect melittin-induced arachidonic acid release, whereas lipid soluble fraction inhibited it in a dose dependent manner in Raw 264.7 cells. The purified phos­pholipase $A_2$ activity was dose-dependently inhibited by lipid soluble fraction of Noni extracts but not by its water soluble fraction. Lipid peroxidation, myeloperoxidase and phospholipase $A_2$ activity in incised skin of mice were significantly increased as compared with those in non-incised skin, and these increase was attenuated by the treatment with Noni pow­der. Our data suggest that Noni extracts has anti-inflammatory activity, and this is, in part, caused by inhibitory activity of phospholipase $A_2$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.5
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• pp.908-913
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• 1997

The purpose of this study was to investigate phospholipase $A_{2}$ activity and lipid peroxidation I streptozotocin induced diabetic rats. Sprague-Dawley male rats weighting-Dawley male rats weighting 300$\pm$10gm were randomly assigned to normal and STZ-induced diabetic group. Diabetes was induced by intravenous injection of 55mg/kg of STZ in sodium citrate buffer(pH 4.3). Animals were sacrificed at the 6th day of diabetic states. Body weight gains were lower in DM group. Phosphatidylcholine hydrolysis in liver was not significantly different between two groups, whereas phosphatidylethanolamine hydrolysis in liver was increased by 69% in DM group comparing with that of normal group. Liver microsomal phospholipase $A_{2}$ activity and level of TBARS was increased by 91%, 109% in DM group compared with that of normal group, respectively. The present results indicate that phospholipase $A_{2}$ activity is specific to PE hydrolysis, leading to lipid peroxidation process in STZ induced diabetic rats.