No abstract

These findings indicate that 1,8-cineole can attenuate cerulein-induced AP via an anti-inflammatory mechanism and by combating oxidative stress. Further studies are needed to clearly elucidate its benefits in patients on acute pancreatitis.

No abstract

alpha,beta-amyrin has the potential to combat acute pancreatitis by acting as an anti-inflammatory and antioxidant agent.

The anti-inflammatory effect of physalin E, a seco-steroid isolated from Physalis angulata L. was evaluated on acute and chronic models of dermatitis induced by 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and oxazolone, respectively, in mouse ear. The changes in ear edema/thickness, production of pro-inflammatory cytokines (TNF-alpha and IFN-gamma), myeloperoxidase (MPO) activity, and histological and immunohistochemical findings were analysed, as indicators of dermal inflammation. Similar to dexamethasone, topically applied Physalin E (0.125; 0.25 and 0.5 mg/ear) potently inhibited the TPA and oxazolone-induced dermatitis, leading to substantial reductions in ear edema/thickness, pro-inflammatory cytokines, and MPO activity. These effects were reversed by mifepristone, a steroid antagonist and confirmed by immunohistochemical and histopathological analysis. The data suggest that physalin E may be a potent and topically effective anti-inflammatory agent useful to treat the acute and chronic skin inflammatory conditions.

No abstract

Endooligopeptidase A was purified approximately 3 000-fold and endooligopeptidase B approximately 1200-fold from the 25 000g supernatant fraction of rabbit brain homogenate. The purified enzymes were homogeneous on the basis of acrylamide gel electrophoresis under denaturing and nondenaturing conditions, isoelectric focusing, immunochemical criteria, and specific activities of the elution profile of gel filtration on Sephadex G-100. The only peptide bond cleaved by endooligopeptidase A in bradykinin, Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9, is Phe5-Ser6, whereas endooligopeptidase B hydrolyzes the Pro7-Phe8 peptide bond of bradykinin and the Pro3-Gly4 bond of des-Phe8-Arg9-bradykinin. The specific activity of the homogeneous enzymes using bradykinin as substrate was 1087 nmol min-1 mg-1 for endooligopeptidase A and 292 nmol min-1 mg-1 for endooligopeptidase B. Gel filtration suggested molecular weights of 75 000 and 68 000 for endooligopeptidases A and B, respectively. Sodium dodecyl sulfate gel electrophoresis suggested that each endooligopeptidase consisted of a single polypeptide chain with molecular weights of 74 000 and 69 000 for the A and B enzymes, respectively. Purified endooligopeptidase A or B injected into goats produces monospecific antisera directed against each enzyme. The antibody prepared against each endooligopeptidase did not react with or inhibit the activity of the other enzyme.

No abstract