59 research outputs found

    Transcriptional Profile Associated with Clinical Outcomes in Metastatic Hormone-Sensitive Prostate Cancer Treated with Androgen Deprivation and Docetaxel

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    (1) Background: Androgen deprivation therapy (ADT) and docetaxel (DX) combination is a standard therapy for metastatic hormone-sensitive prostate cancer (mHSPC) patients. (2) Methods: We investigate if tumor transcriptomic analysis predicts mHSPC evolution in a multicenter retrospective biomarker study. A customized panel of 184 genes was tested in mRNA from tumor samples by the nCounter platform in 125 mHSPC patients treated with ADT+DX. Gene expression was correlated with castration-resistant prostate cancer-free survival (CRPC-FS) and overall survival (OS). (3) Results: High expression of androgen receptor (AR) signature was independently associated with longer CRPC-FS (hazard ratio (HR) 0.6, 95% confidence interval (CI) 0.3-0.9; p = 0.015), high expression of estrogen receptor (ESR) signature with longer CRPC-FS (HR 0.6, 95% CI 0.4-0.9; p = 0.019) and OS (HR 0.5, 95% CI 0.2-0.9, p = 0.024), and lower expression of tumor suppressor genes (TSG) (RB1, PTEN and TP53) with shorter OS (HR 2, 95% CI 1-3.8; p = 0.044). ARV7 expression was independently associated with shorter CRPC-FS (HR 1.5, 95% CI 1.1-2.1, p = 0.008) and OS (HR 1.8, 95% CI 1.2-2.6, p = 0.004), high ESR2 was associated with longer OS (HR 0.5, 95% CI 0.2-1, p = 0.048) and low expression of RB1 was independently associated with shorter OS (HR 1.9, 95% CI 1.1-3.2, p = 0.014). (4) Conclusions: AR, ESR, and TSG expression signatures, as well as ARV7, RB1, and ESR2 expression, have a prognostic value in mHSPC patients treated with ADT+DX

    Predictors of pain intensity and persistence in a prospective Italian cohort of patients with herpes zoster: relevance of smoking, trauma and antiviral therapy

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    Herpes zoster (HZ) is a common disease, characterized by rash-associated localized pain. Its main complication, post-herpetic neuralgia (PHN), is difficult to treat and may last for months to years in the wake of rash resolution. Uncertainties remain as to the knowledge of predictors of HZ-related pain, including the role of antiviral therapy in preventing PHN in ordinary clinical practice. This prospective cohort study was aimed at investigating pain intensity at HZ presentation and its correlates, as well as the incidence of PHN and its predictors

    High Performance Liquid Chromatography Assay for Alanine Amino Transferase

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    An improved method of alanine-amino transferase determination is proposed. The reaction is carried out with alanine and 2-oxoglutarate as substrates and analysis is by HPLC on a reversed-phase chromatographic system using a Ca8 column and tetrabutylammonium phosphate in Phosphate buffer (pH 7.0)-acetonitrile as mobile phase. The enzyme activity was determined by directly following the formation of pyruvic acid without employing any sec- Ondary reaction, which is necessary in the spectrophotometric method. The detection limit of pyruvic acid is 10 Pmole/al-I and the standard deviation for the enzymatic activity of standard solutions is 5.4%. Furthermore under the chromatographic conditions selected it is possible to detect the presence of some intermediate species

    Determination of aspartate aminotransferase activity by high performance liquid chromatography

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    A sensitive and reproducible assay of aspartate aminotransferase activity based on UV detection of the reaction products after their separation by HPLC is described. The main advantage is the direct measurement of the enzyme activity as micromoles of product (glutamate) formed within a known period of time without any coupled reaction. Further, with the chromatographic method, all components of the reaction mixture are identified, allowing the reaction course to be controlled and the possible presence of side-reactions to be monitored

    New method for guanase activity measurement by high performance liquid chromatography

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    A rapid isocratic high-performance liquid chromatographic method for the determination of guanase (EC 3.5.4.3) activity is proposed. The method is highly reproducible, with a coefficient of variation of less than 1%, and requires only ca. 10 min for a complete chromatographic separation of the enzyme reaction mixture. The method allows the detection of nanomolar changes in the concentrations of both the substrate and the product, and does not require additional reactions or sample pretreatment. Kinetic studies with the proposed method showed the guanase activity to have an apparent Michaelis constant of 13.3 and 8.5 microM, and a maximum rate of 1.95 and 3.84 pmol/min per mg protein at 37 degrees C, in Tris-HCl and phosphate buffer, respectivel
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