RESUMO
Background: To evaluate the human papillomavirus HC2 different range detection values and their clinical significance in prediction of CIN lesions grades as well as their role in the follow-up outcome after treatment.Methods: Using the hybrid capture 2 to detect and measure the HPV and the viral load quantity, we enrolled a total of 527 HPV positive women. All patients underwent thin prep liquid-based cytology test (TCT) and only 325 underwent colposcopy guided biopsy due to abnormal cytology results. All cytology and biopsy results were collected and analyzed according to the HPV viral load. Among these patients 108 patients were followed during 2years post-operatives and their prognosis results were collected and analyzed.Results: The proportion and severity of cytological abnormalities was positively correlated with the HPV-HC2 viral load (P<0.05). There was a positive correlation between cervical biopsy results and the HPV viral load P <0.05). The more the HPV-HC2 viral load was, the higher CIN2-3 grade percentage was getting. However no statically significant correlation was found between the HPV-HC2 viral load and the follow up outcomes after treatment (P>0.05).Conclusions: High HPV-HC2 viral load is significantly associated with the severity of cervical lesions (CIN), however it does not predict any further prognosis on follow-up after treatment.
RESUMO
BACKGROUND: Deubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38's functions on the LSD1 protein and on cell physiology were investigated. MATERIALS AND METHODS: Western blotting, real-time quantitative PCR, immunoprecipitation, denaturing immunoprecipitation and luciferase reporter assays were used to analyze the protein stability, protein interactions and changes in the ubiquitin chain. Cell proliferation assays, colony formation assays, drug treatments and western blotting were used to explore the functions of USP38 in cells. RESULTS: The deubiquitinase USP38 stabilizes protein LSD1 in cells by binding LSD1 and cleaving its ubiquitin chain to prevent the degradation of LSD1 by the intracellular proteasome. USP38 enhances the ability of LSD1 to activate signaling pathways and hence promotes cellular abilities of proliferation and colony formation through interacting with LSD1. Furthermore, USP38 enhances the drug tolerance of human colon cancer cells. CONCLUSIONS: USP38 is an LSD1-specific deubiquitinase that affects cellular physiology through interacting with LSD1.