RGS4 protein was not altered in short-term opiate abusers but, in long-term abusers it was significantly up-regulated (Delta = 29 +/- 6%). RGS10 protein expression was significantly decreased in short-term (Delta = -42 +/- 7%) but remained unaltered in long-term opiate abusers. RGS9 protein levels in opiate abusers did not differ from matched controls either in the short-term or in the long-term opiate abuser groups. RGS4, RGS9 and RGS10 levels were also studied in brains (frontal cortex) of rats submitted to acute and chronic morphine treatment and to spontaneous and naloxone-precipitated opiate withdrawal. Chronic

morphine treatment in rats was associated with an increase in RGS4 protein immunoreactivity (Delta = 28 +/- 7%), which persisted in spontaneous (Delta = 35 +/- 8%) and naloxone-precipitated withdrawal (Delta = 30 +/- 9%) without significant changes in RGS9 and RGS10 proteins. The specific modulation of RGS4 and RGS10 selleckchem protein expression observed in the prefrontal cortex of opiate abusers might be relevant in the neurobiology of opiate tolerance, dependence and withdrawal.

This article is part of a Special Issue entitled ‘Post-Traumatic Stress Disorder’. (C) 2011 Elsevier Ltd. All rights reserved.”
“Regulators of G protein signaling (RGS) proteins are important modulators of G protein-coupled receptors and, therefore, critical for cardiovascular functions. One family member, RGS5, has recently been identified

as a key regulator of vascular remodeling and pericyte maturation in tumors. Here, Fludarabine manufacturer we discuss a potential role for RGS5 and its relatives, RGS2 and 4, within the cardiovascular system. Insights into RGS5 signaling are likely to be highly significant for vascular pathologies such as hypertension, atherosclerosis, and angiogenesis. this website (Trends Cardiovasc Med 2009;19:26-30) (C) 2009, Elsevier Inc.”
“The oxidative folding of frog onconase (ONC), a member of the ribonuclease A family, was examined and shows markedly different behavior compared to its

structural homologue bovine pancreatic ribonuclease A (RNase A) under similar conditions. Application of a reduction pulse (using a small amount of reduced dithiothreitol) during the oxidative regeneration of ONC indicated the survival of the native protein along with three other (structured) species, I-1, I-2 and I-3, with the rest of the unstructured species being converted to fully reduced protein. Mass spectrometry indicates that I-1 has two disulfide bonds, whereas I-2 and I-3 have three disulfide bonds each. A disulfide mapping method, based on cyanylation, was used to identify I-2 and I-3 as des-[30-75] and des-[19-68], respectively. On enzymatic digestion using trypsin, I-1 was identified as des-[19-68, 30-75]. Differences in the intermediates that are generated during the oxidative folding of the two structural homologues, RNase A and ONC, demonstrate that regenerative pathways are not necessarily influenced by tertiary structure.