NGAL attenuates renal ischemia/reperfusion injury through autophagy activation and apoptosis inhibition in rats.

Ischemia/reperfusion (I/R) injury is a main cause of acute kidney injury (AKI), and currently lacks effective therapies. This study is to investigate the level of Neutrophil gelatinase-associated lipocalin (NGAL) and autophagy status during renal I/R injury, so as to determine whether the exogenous NGAL protein could exert a protective effect for I/R injury and explore the potential mechanisms. Forty male Wistar rats were randomly divided into the following four groups: Sham, I/R, pre-treated with NGAL before I/R (I/R + pre-N), treated with NGAL after I/R (I/R + post-N).

[Effects of doxazosin and its enantiomers on serum lipid levels in rabbits fed by an atherogenic diet].

Objective: To observe the effects of (-)doxazosin(DOX), (+)DOX and (+/-)DOX on serum lipid levels and the mortality rates of the rabbits fed by an atherogenic diet.

Methods: Male white New Zealand rabbits were fed by an atherogenic diet for 4 weeks. 8 rabbits whose serum TC <10 mmol/L were confirmed as normal diet group and were fed normally.

[Characteristic and prospects of heterotrophic nitrification].

Nitrification is a key step in the global nitrogen cycle. Classically, nitrifying bacteria are chemoautotroph. Recently, bacteria that have the ability of heterotrophic nitrification have been intensively studied as potential microorganisms that may be used to overcomeproblems inherent in the conventional method.

Capillary electrophoresis and circular dichroism study of trichosanthin and its mutants.

The type-I ribosome-inactivating protein trichosanthin (TCS) has a broad spectrum of biological and pharmacological activities, including abortifacient, anti-tumor and anti-human-immunodeficiency-virus (anti-HIV). In this study, circular dichroism (CD) and capillary electrophoresis were used for the first time to study TCS and its two TCS mutants of Y55G TCS (tyrosine 55 converted to glycine) and FYY140-142GSA TCS (tripeptide phenylalanine-tyrosine-tyrosine 140-142 converted to glycine-serine-alanine). The results indicated that the substitution of amino acids changed the secondary structures and the hydrophobility of TCS.