Aromatase and 5-alpha reductase gene expression: modulation by pain and morphine treatment in male rats

<p>Abstract</p> <p>Background</p> <p>The steroid hormone testosterone has been found to be greatly reduced by opioids in different experimental and clinical conditions. The purpose of this study on male rats was to determine the effects of a single injection of morphine (5 mg/Kg) on persistent pain (formalin test) and the single or combined effects on p450-aromatase and 5-alpha reductase type 1 mRNA expression in the brain, liver and testis. Testosterone was determined in the plasma and in the brain, morphine was assayed in the plasma.</p> <p>Results</p> <p>In the morphine-treated rats, there were increases of 5-alpha reductase mRNA expression in the liver and aromatase mRNA expression in the brain and gonads. Morphine was detected in the blood of all morphine-treated rats even though there were no clear analgesic affects in the formalin-treated animals three hours after treatment. Testosterone was greatly reduced in the plasma and brain in morphine-treated subjects.</p> <p>Conclusions</p> <p>It appears that morphine administration can induce long-lasting genomic effects in different body areas which contribute to the strong central and peripheral testosterone levels. These changes were not always accompanied by behavioral modifications.</p

Colorectal motor and sensitivity features in patients affected by ulcerative proctitis with constipation: A radiological and manometric controlled study

Background and Aims: Constipation may be present in ulcerative proctitis (UP), but its pathogenesis has not yet been evaluated. The aim of this article is to investigate functional and morphologic features of the anorectal region in patients with UP and constipation. Materials and Methods: Eleven patients with quiescent clinical, endoscopic, and histological UP and constipation and 10 patients with functional constipation (FC) underwent radiologic evaluation of intestinal transit time, anorectal manometry, and defecography. Transit time was measured with radiograms at 72 It after ingestion of radiopaque markers. Manometry was carried out using a continuous perfused catheter and a balloon inflated with increasing volumes of air. Defecography was performed after the injection of a barium-sulfate solution in the rectum, with the registration of videotapes during straining, squeezing, and evacuation. Results: Manometry showed in UP significantly lower values of rectal compliance than those in FC (3.10 and 5 mL/mmHg, respectively) (P = 0.03). Rectal sensitivity threshold was increased but without significant differences in UP and FC (30 and 50 mL air, respectively). At defecography, the median value of rectosacral space was increased in UP in comparison with FC (1.30 vs 0.8; P = 0.002). Lateral rectal diameter in UP was lower than in FC (6 and 8.8 cm, respectively; P = 0.016). Nonsymptomatic rectocele, mucosal prolapse, descending perineum, and abdominopelvic dyssynergy were equally present in UP and FC. The majority of UP patients showed a prolonged intestinal transit time similar to FC patients, and, more frequently, they showed low transit in the left colon in comparison with the right colon in comparison with FC patients. Conclusions: This study suggests that constipation in UP may be correlated with rectal fibrosis, which reduces the transit of stools from the left colon. The concomitance of asymptomatic anorectal organic or functional alteration may contribute to worsen constipation

Controlling self-assembly of a peptide-based material via metal-ion induced registry shift

Peptide TZ1C2 can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure

Atti del secondo convegno: Energy management nelle strutture del CNR. Il progetto Energy+ ed altre iniziative per l’efficienza energetica

A tre anni di distanza dal primo convegno “Energy management nelle strutture del CNR”, dedicato al tema della gestione dell’energia nelle strutture dell’Ente, il CNR ha organizzato questa seconda edizione dell’evento allo scopo di presentare alcune recenti iniziative per la promozione dell’efficienza energetica all’interno delle sue strutture. In particolare, due interventi hanno presentato le attività del progetto Energy+, riguardanti la realizzazione di una piattaforma dedicata agli Energy manager dell’Ente, un portale per la promozione delle buone pratiche di risparmio energetico fra i dipendenti CNR, una rete di stazioni meteo di supporto alle attività di miglioramento dell’efficienza energetica. Durante la giornata sono state inoltre illustrate alcune attività in corso nelle Aree della Ricerca di Pisa, Padova e Montelibretti. L’evento ha rappresentato un importante momento d’incontro e di confronto tra i tecnici ed i ricercatori coinvolti a vario titolo nella tematica della gestione energetica, gli energy manager, i responsabili delle Aree della Ricerca e l’Amministrazione centrale. Questa edizione del convegno è stata organizzata dal Gruppo di Lavoro del progetto Energy+, vincitore del Premio Innovazione CNR 2013, e dal Dipartimento Ingegneria, ICT e Tecnologie per l’Energia e i Trasporti, in collaborazione con la rete degli Energy Manager del CNR (Dicembre 2015)

Controlling Self-Assembly of a Peptide-Based Material via Metal-Ion Induced Registry Shift

Peptide <b>TZ1C2</b> can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure