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Prostate Cancer, High Cortisol Levels and Complex Hormonal Interaction
Fabre, Bibiana,Grosman, Halina,Gonzalez, Diego,Machulsky, Nahuel Fernandez,Repetto, Esteban M,Mesch, Viviana,Lopez, Miguel Angel,Mazza, Osvaldo,Berg, Gabriela Asian Pacific Journal of Cancer Prevention 2016 Asian Pacific journal of cancer prevention Vol.17 No.7
Prostate cancer (PCa) is one of the most common diseases in men. It is important to assess prognostic factors and whether high cortisol levels and complex hormonal interactions could be responsible for PCa development. We evaluated the relationship between cortisol, leptin and estrogens in 141 men, 71 with PCa and the remaining 70 constituting a low risk group (LRG). They were recruited for this study from a total of 2906 middle-aged men (ages 45-70 years) who completed an evaluation for prostatic diseases at the Urology Division, Hospital de Clínicas "$Jos{\acute{e}}$ de San $Mart{\acute{i}}n$", University of Buenos Aires, in May 2009. In this cross sectional study, cortisol, PSA, total-testosterone, free-testosterone, bioavailable testosterone, LH and estradiol were measured in serum. We observed increased cortisol levels in PCa patients as compared to LRG cases (p=0.004,). Leptin and estradiol levels were also higher in PCa patients (p=0.048; p<0.0001, respectively). Logistic regression analysis indicated that serum cortisol (OR: 1.110 (95% CI 1.016-1.213), p=0.022), estradiol (OR: 1.044 (95% CI 1.008-1.081), p=0.016) and leptin (OR: 1.248 (95% CI 1.048-1.487), p=0.013) explained 27% of the variance of dependent variables, even after adjusting for age, smoking, BMI and waist circumference. We found increased cortisol levels in PCa patients as compared to LRG, as well as an altered circulating hormonal profile.
p62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome
Cohen-Kaplan, Victoria,Livneh, Ido,Avni, Noa,Fabre, Bertrand,Ziv, Tamar,Kwon, Yong Tae,Ciechanover, Aaron National Academy of Sciences 2016 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.113 No.47
<P>The ubiquitin-proteasome system and autophagy are the two main proteolytic systems involved in, among other functions, the maintenance of cell integrity by eliminating misfolded and damaged proteins and organelles. Both systems remove their targets after their conjugation with ubiquitin. An interesting, yet incompletely understood problem relates to the fate of the components of the two systems. Here we provide evidence that amino acid starvation enhances polyubiquitination on specific sites of the proteasome, a modification essential for its targeting to the autophagic machinery. The uptake of the ubiquitinated proteasome is mediated by its interaction with the ubiquitin-associated domain of p62/SQSTM1, a process that also requires interaction with LC3. Importantly, deletion of the PB1 domain of p62, which is important for the targeting of ubiquitinated substrates to the proteasome, has no effect on stress-induced autophagy of this proteolytic machinery, suggesting that the domain of p62 that binds to the proteasome determines the function of p62 in either targeting substrates to the proteasome or targeting the proteasome to autophagy.</P>