Cardiac overexpression of catalase rescues cardiac contractile dysfunction induced by insulin resistance: Role of oxidative stress, protein carbonyl formation and insulin sensitivity.

AIMS/HYPOTHESIS: Insulin resistance leads to oxidative stress and cardiac dysfunction. This study examined the impact of catalase on insulin-resistance-induced cardiac dysfunction, oxidative damage and insulin sensitivity. METHODS: Insulin resistance was initiated in FVB and catalase-transgenic mice by 12 weeks of sucrose feeding. Contractile and intracellular Ca2+ properties were evaluated in cardiomyocytes including peak shortening (PS), time-to-PS (TPS), time-to-90% relengthening (TR90), half-width duration (HWD), maximal velocity of shortening/relengthening (+/-dL/dt), fura-fluorescence intensity change (DeltaFFI) and intracellular Ca2+ clearance rate (tau). Reactive oxygen species (ROS) and protein damage were evaluated with dichlorodihydrofluorescein and protein carbonyl formation. RESULTS: Sucrose-fed mice displayed hyperinsulinaemia, impaired glucose tolerance and normal body weight. Myocytes from FVB sucrose-fed mice exhibited depressed PS and +/-dL/dt, prolonged TR90 and tau, and reduced DeltaFFI associated with normal TPS and HWD compared with those from starch-fed control mice. ROS and protein carbonyl formation were elevated in FVB sucrose-fed mice. Insulin sensitivity was reduced, evidenced by impaired insulin-stimulated 2-deoxy-D: -[3H]glucose uptake. Western blot analysis indicated that sucrose feeding: (1) inhibited insulin-stimulated phosphorylation of insulin receptor and Akt; (2) enhanced protein-tyrosine phosphatase 1B (PTP1B) expression; and (3) suppressed endothelial nitric oxide synthase (eNOS) and Na+-Ca2+ exchanger expression without affecting peroxisome proliferator-activated receptor gamma (PPARgamma), sarco(endo)plasmic reticulum Ca2+-ATPase isozyme 2a and phospholamban. Catalase ablated insulin-resistance-induced mechanical dysfunction, ROS production and protein damage, and reduced eNOS, but not insulin insensitivity. Catalase itself decreased resting FFI and enhanced expression of PTP1B and PPARgamma. CONCLUSIONS/INTERPRETATION: These data indicate that catalase rescues insulin-resistance-induced cardiac dysfunction related to ROS production and protein oxidation but probably does not improve insulin sensitivity.

Beauveria bassiana as a pathogen of the Mexican fruit fly (Diptera: Tephritidae) under laboratory conditions.

Bioassays were carried out under controlled conditions (27 +/- 2 degrees C, 80 +/- 5% RH, and a photoperiod of 12:12 [L:D] h) to evaluate the effect of eight strains of the entomopathogenic fungus Beauveria bassiana upon larvae, pupae, and adult females of the Mexican fruit fly, Anastrepha ludens (Loew). Mortality of the immature stages was low, 2-8% in larvae and 0% in pupae. However, very high levels of mortality were obtained for adult flies, with values of 100, 98, and 98% for the strains Bb16, Bb24, and Bb26, respectively. LC50 values for these three strains ranged from 3.12 x 10(6) to 9.07 x 10(6) conidia/ml. Lethal time 50 (LT50) was 2.8, 3.7, and 4.2 d for Bb16, Bb26, and Bb24 strains, respectively, with an average LT50 of 4.4 d across all strains. The fungal mycelium emerged through the soft parts of the exoskeleton, such as the wing bases, mouth, intersegmental regions of the legs, and membranous regions of the abdomen, coxae, and neck. Maximum percentage sporulation ranged from 66.4 to 74.7% for the three most virulent strains.