New Zealand blackcurrant extract modulates the heat shock response in men during exercise in hot ambient conditions.

Purpose: To determine if 7d of New Zealand blackcurrant (NZBC) extract alters the heat shock, inflammatory and apoptotic response during prolonged exertional-heat stress.

Methods: Ten men (Age: 29 ± 2 years, Stature: 1.82 ± 0.

United States National Postdoc Survey results and the interaction of gender, career choice and mentor impact.

The postdoctoral community is an essential component of the academic and scientific workforce, but a lack of data about this community has made it difficult to develop policies to address concerns about salaries, working conditions, diversity and career development, and to evaluate the impact of existing policies. Here we present comprehensive survey results from 7,603 postdocs based at 351 US academic and non-academic (e.g.

Mapping Soluble Guanylyl Cyclase and Protein Disulfide Isomerase Regions of Interaction.

Soluble guanylyl cyclase (sGC) is a heterodimeric nitric oxide (NO) receptor that produces cyclic GMP. This signaling mechanism is a key component in the cardiovascular system. NO binds to heme in the β subunit and stimulates the catalytic conversion of GTP to cGMP several hundred fold.

Protein disulfide-isomerase interacts with soluble guanylyl cyclase via a redox-based mechanism and modulates its activity.

NO binds to the receptor sGC (soluble guanylyl cyclase), stimulating cGMP production. The NO-sGC-cGMP pathway is a key component in the cardiovascular system. Discrepancies in sGC activation and deactivation in vitro compared with in vivo have led to a search for endogenous factors that regulate sGC or assist in cellular localization.

Identification of residues in the heme domain of soluble guanylyl cyclase that are important for basal and stimulated catalytic activity.

Nitric oxide signals through activation of soluble guanylyl cyclase (sGC), a heme-containing heterodimer. NO binds to the heme domain located in the N-terminal part of the β subunit of sGC resulting in increased production of cGMP in the catalytic domain located at the C-terminal part of sGC. Little is known about the mechanism by which the NO signaling is propagated from the receptor domain (heme domain) to the effector domain (catalytic domain), in particular events subsequent to the breakage of the bond between the heme iron and Histidine 105 (H105) of the β subunit.

Aspartate 102 in the heme domain of soluble guanylyl cyclase has a key role in NO activation.

Nitric oxide (NO) is involved in the physiology and pathophysiology of the cardiovascular and neuronal systems via activation of soluble guanylyl cyclase (sGC), a heme-containing heterodimer. Recent structural studies have allowed a better understanding of the residues that dictate the affinity and binding of NO to the heme and the resulting breakage of the bond between the heme iron and histidine 105 (H105) of the β subunit of sGC. Still, it is unknown how the breakage of the iron-His bond translates into NO-dependent increased catalysis.

QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.

Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins. Human QSOX1 is a multi-domain, monomeric enzyme containing a module related to the single-domain sulfhydryl oxidases of the Erv family. A partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv enzymes.

Evaluation of the pharmacotherapeutic efficacy of Garcinia cambogia plus Amorphophallus konjac for the treatment of obesity.

Hydroxycitric acid (HCA), the main compound of Garcinia cambogia extract, is a competitive blocker of ATP-citrate-lyase, presenting a potential inhibition of fatty acid biosynthesis. Glucomannan fibers, abundant in Amorphophallus konjac, seem to reduce the absorption kinetics of dietary fat. Therefore, the aim of this double-blind randomized study was to evaluate the pharmacotherapeutic efficacy of standardized extracts of G.

Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis.

The flavoprotein quiescin-sulfhydryl oxidase (QSOX) rapidly inserts disulfide bonds into unfolded, reduced proteins with the concomitant reduction of oxygen to hydrogen peroxide. This study reports the first heterologous expression and enzymological characterization of a human QSOX1 isoform. Like QSOX isolated from avian egg white, recombinant HsQSOX1 is highly active toward reduced ribonuclease A (RNase) and dithiothreitol but shows a >100-fold lower k cat/ K m for reduced glutathione.

Generating disulfides with the Quiescin-sulfhydryl oxidases.

The Quiescin-sulfhydryl oxidase (QSOX) family of flavoenzymes catalyzes the direct and facile insertion of disulfide bonds into unfolded reduced proteins with concomitant reduction of oxygen to hydrogen peroxide. This review discusses the chemical mechanism of these enzymes and the involvement of thioredoxin and flavin-binding domains in catalysis. The variability of CxxC motifs in the QSOX family is highlighted and attention is drawn to the steric factors that may promote efficient thiol/disulfide exchange during oxidative protein folding.

Inhibition of cytochrome P450-dependent monooxygenases by an alkaloid fraction from Helietta apiculata markedly potentiate the hypnotic action of pentobarbital.

Crude alkaloid fraction (CAF) isolated from the leaves of Helietta apiculata showed the presence of furoquinolines. The extract was investigated to determine if it can enhance the sensitivity of the central nervous system (CNS) to the hypnotic action of pentobarbital. Administration of CAF to mice in a dose range of 300-500 mg/kg prior to an injection of pentobarbital (40 mg/kg, i.