Autophagy is considered physiologically important for the maintenance of normal cardiovascular morphology and function, whilst excessive autophagy by various factors contributes to the induction and exacerbation of several types of cardiomyopathy. We found that doxorubicin-treated rats receiving adeno-ILK displayed a decreased number of autophagic vacuoles compared to those receiving adeno-null. In line with this finding, we also observed a reduction in beclin 1 expression in the adeno-ILK group. In detail, the hydroxyl oxygen of Ser154 is firstly polarized by Povidone iodine adjacent His309 before Ser154 attacks the hydrogen atom of a free water molecule, and then, the activated water molecule attacks the carbonyl carbon Methicillin sodium salt within the C-O ester bond. However, it cannot be ignored that the binding of substrate to Rv0045c may cause conformational change of the enzyme. In that case, Ser154 might be close enough to directly attack the carbonyl carbon within the C-O ester bond and the enzyme employed a direct mechanism. Rv0045c can catalyze a mount of substrates with hydrocarbon chains of different length. We infer that Rv0045c may adopt different enzymatic mechanisms when binding different substrates. Although VDAC has been extensively studied in various tissues and cells, there is little knowledge about the distribution and function of VDAC in male mammalian reproductive system. According to current animal studies, VDAC1 is exclusively localized in the Sertoli cells, and VDAC2 and VDAC3 are present in the germ cells. The binding specificity of antiVDAC2 antibody used in our study was firstly confirmed. Native VDAC2 protein was identified in the hydrophobic membrane protein extracts from human spermatozoa. Our results suggested that VDAC2 was located in membrane components. The antiVDAC2 antibody will contribute to our further study about the new characteristics and functions of VDAC2 in human spermatozoa. It has been demonstrated that VDAC2 can form the channel structure in the lipid bilayer and play important roles in cellular functions through mediating the transmembrane ion transport.