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Biomedical subjects

J Mishra

Publications and source records attributed to J Mishra.

26 records · Page 2Linked to original sources
PubMed1983

Malathion induced hematological and biochemical changes in the Indian catfish Heteropneustes fossilis.

The acute toxicity and effects of duration of sublethal exposure to malathion were determined in the Indian catfish (Heteropneustes fossils). Fish exposed to the pesticide for 2, 6, 12, 48, and 96 hr showed muscle glycogenolysis with concomitant hyperglycemia at all intervals; hepatic glycogen was unaffected. Malathion was also associated with hypochloremia at 2 and 6 hr and hyperchloremia at 48 and 96 hr; blood chloride concentration was unaffected at 12 hr. Fish developed erythropenia and leukopenia; lowered hematocrit and hemoglobin content and hypercoagulability of blood were also observed. The data show that homeostatic and hemostatic mechanisms are disturbed after malathion treatment and could be helpful for evaluating pesticide toxicosis in fish.

Animals↗
PubMed1983

Effects of fenthion on the blood and tissue chemistry of a teleost fish (Heteropneustes fossilis).

Exposure of a freshwater teleost, Heteropneustes fossilis, to a concentration of 14 . 625 mg per 1 (0.9 of 96 h LC50) fenthion induced muscle and hepatic glycogenolysis with concomitant hyperglycaemia at 2, 6, 12 and 48 h after treatment. The pesticide evoked an initial fall (at 2 and 6 h) and later a rise (at 48 and 96 h) in blood chloride concentration. The treatment also caused anaemia with simultaneous increase in ESR and hypo-coagulability of whole-blood. The results are compared with organophosphate poisoning in this and in other fish species.

Animals↗
PubMedDate not supplied

Recognition of cyclooxygenase-2 (COX-2) active site by NSAIDs: a computer modelling study.

The energetics and models of COX-2 complexed with nonsteroidal anti-inflammatory drugs (NSAIDs) having different degrees of selectivity for two isoforms of COX (COX-2 and COX-1) have been studied using computer modelling approach. The models are obtained for complexes of NS398 (NS), a selective COX-2 inhibitor; indoprofen (Ind), a non-selective inhibitor; di-tert-butylbenzofurans (DHDMBFs) with substituents at the 5th position: CONH(CH2)2OMe (BF1), CONH-c-Pr (BF2), 3-methylene-gamma-butyrolactonyl (BF3) and oxicams namely, meloxicam (Mel), piroxicam (Pir) and tenoxicam (Ten). These were optimized using molecular mechanics (MM) and molecular dynamics (MD) techniques. The binding energies and structures were compared with pharmacological parameters and available results with COX-1. In case of NS a larger difference in the binding energies between COX-2 and COX-1 was noticed as compared to that of Ind. It also had stronger interaction with His90 and Tyr355 which is considered important for COX-2 selectivity. There was a difference in the compactness at the channel entrance between COX-2 selective and non-selective ligands. Models with DHDMBFs and oxicams showed a similar correlation. The results were used to design a peptide inhibitor, Tyr-Arg-Cys-Ala-delta Phe-Cys (Pept) which could fit better in the COX-2 cavity. As per our MD simulation results this peptide inhibitor showed both higher activity and COX-2 selectivity.

Anti-Inflammatory Agents, Non-Steroidal↗