Anti-inflammatory and antioxidant activities of Jungia paniculata.
ABSTRACT The present study was conducted to evaluate the antioxidant and anti-inflammatory activities of Jungia paniculata (DC.) A. Gray (Asteraceae), used traditionally in Peru. The dry leaves were extracted with methanol, 50% methanol, and water. The anti-inflammatory activity of this plant was studied using in vitro (nitric oxide production in RAW 264.7 macrophages and sPLA(2) inhibition assay) and in vivo (carrageenan-induced paw edema in rats and TPA-induced ear edema in mice) model systems. The antioxidant activity of extracts was studied using three in vitro model systems (DPPH(*) radical-scavenging assay, ABTS(*+) assay, and superoxide radical-scavenging activity). The results have been correlated with total phenolics and total flavonoids contents. In the NO test of the extracts of Jungia paniculata, no significant cytotoxicities were observed at the concentrations determined by MTT assay. Only the MeOH50 extract of Jungia paniculata significantly inhibited PLA(2) enzyme activity (82.3 +/- 2.6%). At 3 h, the 50% methanol extract of Jungia paniculata at an oral dose of 500 mg/kg showed significant suppression of carrageenan-induced rat paw edema (36.36%). The same extract induced a 93.99% reduction in TPA-induced edema in topical administration. The extracts exhibited a high antioxidant activity and contained high total levels of polyphenols and flavonoids. There was a significant linear correlation between total phenolics and flavonoids contents and antioxidant activity in the three models used. In conclusion, Jungia paniculata possesses anti-inflammatory and antioxidant properties, which confirm the use of this plant in folk medicine as a topical anti-inflammatory herbal.
Article: The croton oil ear test revisited.[Show abstract] [Hide abstract]
ABSTRACT: measurement the ear plugs were homogenized in physiological saline containing 0.1% of hexadecyltrimethylammonium bromide. The post 15,000 g supernatants of the homogenates (which contained more than 95% of the PA) were used for the assay . PA units are expressed as nmoles of tetraguaiacol/min at 25~ Results and discussionAgents and Actions 02/1986; 17(3-4):347-9.
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ABSTRACT: Polymorphonuclear leukocytes obtained from sterile peritoneal exudates in rabbits contain two phospholipid-splitting activities (phosphatidylacylhydrolases EC 184.108.40.206), one most active at pH 5.5 and the other between pH 7.2 and 9.0. Hydrolysis of phospholipid was demonstrated using Escherichia coli labeled during growth with [1-(14)C]oleate and then autoclaved to inactivate E. coli phospholipases and to increase the accessibility of the microbial phospholipid substrates. The acid and alkaline phospholipase activities are both membrane bound, calcium dependent, and heat stable, and they appear to be specific for the 2-acyl position of phospholipids. Evidence was also obtained suggesting that the E. coli envelope phospholipids with oleate in position 2 are more readily degraded than those with palmitate. The two activities are associated with azurophilic as well as specific granules (obtained by zonal centrifugation) and with phagosomes (isolated after ingestion of paraffin particles by the granulocytes). Phospholipase A activities at pH 5.5 and pH 7.5 degrade the two major phospholipids of E. coli, phosphatidylethanolamine and phosphatidylglycerol, to the same extent, but the phospholipase activity at acid pH does not hydrolyze micellar dispersions of phosphatidylethanolamine. By contrast, phospholipase A(2) activity at pH 7.5 degrades both types of phosphatidylethanolamine substrates. Heparin and chondroitin sulfate inhibit phospholipase activity at pH 5.5 but have little effect on activity at pH 7.5. All detergents tested inhibited phospholipase activity, and both activities are inhibited by reaction products, free fatty acid and lysophosphatidylethanolamine. This product inhibition is only partially prevented by addition of albumin. Supernatant fractions of granulocyte homogenates contain a heat-labile inhibitor of granule phospholipase activity at pH 7.5. Boiling the fraction not only removes the inhibition but actually results in stimulation of hydrolysis at pH 7.5 as well as pH 5.5. These granule-associated phospholipase A activities of polymorphonuclear leukocytes differ in several of their properties from granule or lysosomal phospholipases of other phagocytic cells.The Journal of Lipid Research 08/1974; 15(4):380-8. · 4.39 Impact Factor
- Endocrinology 11/1965; 77(4):625-34. · 4.72 Impact Factor