guanosine-diphosphate and Prostatic-Neoplasms

Widespread use of artificial light at night (ALAN) might contribute to the global burden of hormone-dependent cancers. Previous attempts to verify this association in population-level studies have been sparse. Using GLOBOCAN, US-DMSP, and World Bank 2010-2012 databases, we studied the association between ALAN and prostate cancer (PC) incidence in 180 countries worldwide, controlling for several country-level confounders. The PC-ALAN association emerged marginally significant when year-2012 PC age-standardized rate data were compared with ALAN levels (t = 1.886, p < .1); this association was more significant (t > 2.7; p < .01) when only 110 countries with well-maintained cancer registries were analyzed. Along with other variables, ALAN explains up to 79% of PC ASR variability. PC-ALAN association appears to vary regionally, with the greatest deviations in Central Africa, Small Island Developing States, Southeast Asia, and Gulf States.

Topics: Electricity; Global Health; Guanosine Diphosphate; Humans; Incidence; Lighting; Male; Prostatic Neoplasms; Registries; Residence Characteristics; Risk Factors

We previously reported that pheophorbide a (PhA), excited by 630 nm light, significantly inhibited the growth of prostate cancer cells. In this study, we employed whole-cell proteomics to investigate photodynamic treatment (PDT)-related proteins.. Two-dimensional gel electrophoresis (2-DE) coupled with tandem mass spectrometry was employed to reveal the proteins involved in PhA-mediated PDT in LNCaP and PC-3 prostate cancer cells.. After PhA-PDT treatment, decreased expression of translationally-controlled tumor protein (TCTP) was found in both PC-3 and LNCaP whole-cell proteomes. In contrast, human rab GDP dissociation inhibitor (GDI) in LNCaP cells and ras-related homologs GDI in PC-3 cells were up-regulated.. GDP-GTP exchange is an underlying target of photodynamic treatment in prostate cancer cells.

Topics: Cell Line, Tumor; Chlorophyll; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Male; PC-3 Cells; Photochemotherapy; Photosensitizing Agents; Prostatic Neoplasms; Proteomics; ras Proteins; Tandem Mass Spectrometry; Tumor Protein, Translationally-Controlled 1; Two-Dimensional Difference Gel Electrophoresis

Vessel dilator and kaliuretic peptide have anticancer effects in human prostate adenocarcinomas.. The effects of vessel dilator, kaliuretic peptide and cyclic GMP on Ras were examined in human prostate adenocarcinoma cells.. Vessel dilator and kaliuretic peptide decreased the activation of Ras -GTP over a concentration range of 0.01 microM to 1 microM. Vessel dilator and kaliuretic peptide (each 1 muM) inhibited the phosphorylation of Ras by 95% (p<0.0001) and 90% (p<0.0001), respectively. At 0.01 microM of kaliuretic peptide, the maximal inhibition was 95% . The inhibition of Ras lasted for 48 to 72 hours secondary to both peptides. Their ability to inhibit Ras was inhibited by cyclic GMP antibody and cyclic GMP itself inhibited Ras phosphorylation (89%; p=0.0015).. Vessel dilator and kaliuretic peptide both inhibit Ras partially mediated via cyclic GMP as part of their anticancer mechanism(s) of action.

Topics: Adenocarcinoma; Aged; Atrial Natriuretic Factor; Cyclic GMP; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Diphosphate; Humans; Immunoblotting; Male; Natriuresis; Peptide Fragments; Prostatic Neoplasms; Protein Precursors; ras Proteins; Sodium-Potassium-Exchanging ATPase; Tumor Cells, Cultured

The interaction of the antimitotic agent estramustine with bovine microtubule proteins and purified tubulin was investigated. Direct photoaffinity labeling of microtubule protein with [14C]estramustine resulted in the labeling of both alpha- and beta-tubulin, and this was inhibited with unlabeled estramustine in a dose-dependent manner. [14C]Estramustine was incorporated into both the soluble and polymerized forms of tubulin. The affinity constant for estramustine binding to tubulin was determined by equilibrium dialysis to be 23 +/- 5 mM. Estramustine did not affect [3H]vinblastine binding, and vinblastine had no effect on direct labeling with [14C]estramustine. Both rhizoxin and paclitaxel decreased the covalent labeling of tubulin with [14C]estramustine in a dose-dependent fashion and were noncompetitive inhibitors of the binding of estramustine to tubulin. The binding of colchicine to tubulin was not inhibited by estramustine as detected by fluorescence and DEAE filter assays. The estramustine binding site on tubulin is therefore distinct from that of colchicine and vinblastine and may at least partially overlap with the binding site for paclitaxel. In both bovine brain microtubules and cytoskeletal proteins from human prostatic carcinoma cells, the incorporation of [14C]estramustine into the beta III isotype of tubulin was found to occur with a reduced efficiency compared to that of the other beta-tubulin isotypes and alpha-tubulin. Since this isotype is overexpressed in estramustine resistant human prostate carcinoma cells, these results indicate that beta III-tubulin may play a role in the response to the effects of estramustine.

Topics: Animals; Antineoplastic Agents, Alkylating; Antineoplastic Agents, Hormonal; Binding Sites; Brain; Cattle; Colchicine; Estramustine; Guanosine Diphosphate; Guanosine Triphosphate; Humans; In Vitro Techniques; Male; Microtubule Proteins; Mitosis; Paclitaxel; Prostatic Neoplasms; Tubulin; Vinca Alkaloids