• Applied Biological Chemistry
• /
• v.49 no.1
• /
• pp.65-69
• /
• 2006

With extracted Aloe vera and Aloe arborescens, anti-inflammatory effect was examined in phosphatidic acid-stimulated Raw 264.7 cells. Phosphatidic acid $(50\;{\mu}g/ml)$ treatment increased inflammation related 264.7 cells. The extracts of $80\;{\mu}g/ml$ concentration from Aloe arborescens reduced the expression of iNOS. Aloe vera and Aloe arborescens also reduced the expression of COX-2, it seems that anti-inflammatory effects of Aloe extracts is partly due to the inhibition of COX-2 expression by inhibiting in Raw 264.7 cells.

• Biomolecules & Therapeutics
• /
• v.2 no.1
• /
• pp.39-46
• /
• 1994

The present study was undertaken to demonstrate whether or not bradykinin activates a phospholipase D in rabbit kidney proximal tubule cells. By measuring the formation of [$^3$H]phosphatidic acid and [$^3$H]phosphatidylethanol we could elucidate the direct stimulation of phospholipase D by bradykinin. Bradykinin leads to a rapid increase in [$^3$H]phosphatidic acid and [$^3$H]diacylglycerol, and [$^3$H]phosphatidic acid formation preceded the formation of [$^3$H]diacylglycerol. This result suggests that some phosphatidic acid seems to be formed directly from phosphatidylcholine by the action of phospholipase D, not from diacylglycerol by the action of diacylglycerol kinase. In addition, the other mechanisms by which phospholipase D is activated was examined. We have found that phospholipase D was activated and regulated by extracellular calcium ion and pertussis toxin-insensitive G protein, respectively. It has also been shown that bradykinin may activate phospholipase D through protein kinase C-dependent pathway. In conclusion, we are now, for the first time, strongly suggesting that bradykinin-induced activation of phospholipase D in the rabbit kidney proximal tubule cells is mediated by a pertussis toxin-insensitive G protein and is dependent of protein kinase C.

• Proceedings of the Botanical Society of Korea Conference
• /
• 2001.04a
• /
• pp.24-24
• /
• 2001

• BMB Reports
• /
• v.29 no.1
• /
• pp.11-16
• /
• 1996

The present study showed that receptor-mediated activation of rabbit kidney proximal tubule cells by angiotensin II, the $Ca^{2+}$ ionophore A23187, or the protein kinase C activator phorbol myristate acetate (PMA) all stimulated phospholipase D (PLD). This was demonstrated by the increased formation of phosphatidic acid, and in the presence of 0.5% ethanol, phosphatidylethanol (PEt) accumulation. Angiotensin II leads to a rapid increase in phosphatidic acid and diacylglycerol, and phosphatidic acid formation preceeded the formation of diacylglycerol. This result suggests that some phosphatidic acid seems to be formed directly from phosphatidylcholine hydrolyzed by Pill. On the other hand, EGTA substantially attenuated angiotensin II and A23187-induced PEt formation, and when the cells were pretreated with verapamil angiotensin II-induced Pill activation was completely abolished. These results provide the evidence that calcium ion influx is essential for the agonist-induced Pill activation. In addition, staurosporine, an inhibitor of protein kinase C, strongly inhibited PMA-induced PEt formation, but was ineffective on angiotensin II-induced PEt accumulation. $GTP{\gamma}S$ also stimulates PEt formation in digitonin-permeabilized cells, but pretreatment of the cells with pertussis toxin failed to suppress angiotensin II-induced PEt formation. From these results, we conclude that in the rabbit kidney proximal tubule cells the mechanisms of angiotensin II- and PMA-induced Pill activation are different from each other and mediated via a pertussis toxin-insensitive trimeric G protein.

• Bulletin of the Korean Chemical Society
• /
• v.18 no.11
• /
• pp.1204-1207
• /
• 1997

Effects of exogenous glycerophospholipids on oleate-dependent phospholipase D (PLD) activity were studied in lymphocytic mouse leukemia L1210 cells and in solubilized microsomal phospholipase D of rat brain. Among the phospholipids tested phosphatidic acid had the most stimulatory effects on both PLD activities up to about 3 folds. Lysophosphatidic acid also showed promoting effect on microsomal PLD activity but much less on L1210 cells compared to that of phosphatidic acid. While phosphatidylethanolamine increased PLD activity slightly, phosphatidylinositides were nearly ineffective in the tested sources. The stimulatory effect of phosphatidic acid observed can be utilized to improve the in vitro assay system for oleate-dependent PLD in mammalian sources.

• Korean Journal of Food Science and Technology
• /
• v.21 no.1
• /
• pp.25-30
• /
• 1989

Effects of cooking and drying methods on the composition of glycolipids and phospholipids of shrimp, Metapenaeus joyneri, were investigated. Major components of the glycolipids were esterified steryl glycosides, monogalactosyl diglycerides and steryl glycosides. Hot air drying enhanced the esterified steryl glycosides content substantially with the reduction of the monogalactosyl diglycerides content. However, reversed pattern was shown for freeze drying. Main components of the phospholipids were phosphatidyl ethanolamines, phosphatidyl cholines, phosphatidic acids, phosphatidyl inositols and phosphatidyl serines. Phosphatidic acids content for hot air and freeze dried shrimp without tooting was 8.3% and 5.9%, respectively. On the other hand, freeze dried shrimp with microwave heating was higher in phosphatidyl ethanolamines contents but lower in phosphatidyl cholines contents than hot air dried shrimp. Major fatty acids of the glycolipids and phospholipids fractions were pentadecanoic acid, palmitic acid, oleic acid, nervonic acid and eicosapentaenoic acid in fresh shrimp.

• Archives of Pharmacal Research
• /
• v.17 no.6
• /
• pp.405-410
• /
• 1994

The present study was undetertaken to demonstrate whether or not angiotensin II activates a phopholipase D in rabbit kidney proximal tubule cells. By measuring the formation of [$^3H$] phosphatidic acid and [$^3H$]diacylglycerol. This result suggests that some phosphatidic acid seems to be formed directly from phosphatidylcholin by the action of phopholipase D, not from the action of diacylglycerol kinase on the diacylglycerol. In addition the other mechanisms by which phospholipase D is activated was examined. We have found that phospholipase D was activited by extracellular calium ion. It has also been shown that angiotensin II may activate phosphoilpase D through protein kinase C-independent pathway.

• Journal of Microbiology and Biotechnology
• /
• v.6 no.6
• /
• pp.407-413
• /
• 1996

A novel type of extracellular phospholipase $A_1$ was isolated from Serratia sp. MK1 and purified to homogeneity by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified enzyme was a monomer with a molecular mass of about 43, 000 Da. This enzyme showed the highest lipolytic activity toward phosphatidylserine among the phosphoglycerides tested, and preferentially catalyzed the hydrolysis of the ester bond in phosphatidic acid to lyso-phosphatidic acid. Enzyme activity was completely inhibited by the addition of a chelating agent such as EDTA, and inhibited enzyme activity was fully recovered by the presence of $Ca^{2+}$. This implies that the enzyme requires $Ca^{2+}$ for activity. The enzyme was stable up to $70^{\circ}C$ when incubated for 1 h at pH 8.5, and the optimal pH and temperature were 8.5 and $50^{\circ}C$, respectively.

• Bulletin of the Korean Chemical Society
• /
• v.10 no.6
• /
• pp.595-599
• /
• 1989

The effects of phosphatidic acid(PA) on the activity of phospholipase D were examined in detail. The enzyme activity was examined in the liposome system containing phosphatidylcholine and PA, which was suspended in a desired buffer solution by ultrasonication. The substrate of large unilamella vesicle (LUV) state by ultrasonication was more effective on the enzyme activity than that of multilamella vesicle(MLV) by water-bath type sonication. The most effective molar ratio of PC-PA liposome for enzyme activity was found to be 1:0.7. The other optimum conditions were found 5 mM $Ca^{2+}$ ion, pH 6.6, and incubation temperature of $27^{\circ}C. K_m \;and \;V_{max}$ values were estimated to be 1.43 mM and 0.8 $nmole/min/{\mu}g$ protein respectively. These properties in a PC-PA liposome system were compared with those in a PC-SDS mixed micelle system. The effects of other phospholipids and organic phosphates on the enzyme activity were also examined.

• Proceedings of the Korea Environmental Mutagen Society Conference
• /
• 2004.11a
• /
• pp.101-101
• /
• 2004