ABSTRACT. Cytochrome P450 17a-hydroxylase (CYP17) plays a critical role in androgen biosynthesis. Polymorphisms of the CYP17 promoter have been proposed as risk factors for prostate cancer; however, some studies have produced inconclusive or controversial results. We investigated the relationship between polymorphisms of the CYP17 gene and the risk of prostate cancer. A total of 176 patients with prostate cancer were enrolled in the study, and 168 healthy individuals acted as the control group. The participants were divided into those <71 years old and those ≥71 years old. Restriction fragment length polymorphism-polymerase chain reaction was used to confirm the genotype of CYP17 in the samples. The prostate-specific antigen (PSA) concentrations were also measured in all subjects. When T/C and C/C were compared with T/T, the ORs were 0.478 (P = 0.489) and 0.814 (P = 0.367), respectively. There was no significant difference in PSA concentration among the three genotypes in the <71 group, whereas there were statistically significant differences in the ≥71 group (P = 0.003 and 0.012, respectively). There was no significant difference in free PSA and total PSA levels between the three groups and the control group. The T/C and C/C genotypes were not associated with the risk of prostate cancer, and there were no significant differences between them. In the ≥71 group, the T/C and C/C genotypes were closely associated with prostate cancer, which suggests that the CYP17 gene might be a risk factor for prostate cancer in males of advanced age.
ABSTRACT. We constructed hepatocellular carcinoma (HCC) cells that stably express stathmin with a Ser25 phosphorylation site mutation (stathmin S25A). We used the polymerase chain reaction for site-directed mutagenesis, constructed a stathmin S25A plasmid, and verified the results by restriction enzyme cleavage and sequencing technology. Using the liposome transfection method, stathmin wild-type and S25A HCCLM6 cells were established, which were identified by western blotting. The sequencing report of the stathmin S25A plasmid showed that stathmin serine at position 25 had mutated into alanine. Stable cells transfected with stathmin wild-type and S25A plasmids were constructed. Using western blotting, we confirmed that the expression level of stathmin pS25 in the stathmin S25A cells was reduced than that in the stathmin wild-type and HCCLM6 control cells (P < 0.05). We constructed stathmin S25A HCCLM6 cells, which offer an experimental model for further investigation of the molecular mechanism of stathmin phosphorylation in hepatocarcinogenesis.
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