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At least 379 records · Page 21Linked to original sources
PubMed1987

Influence of cadmium chloride, mercuric chloride, and sodium vanadate on the glutathione-conjugating enzyme system in liver, kidney, and brain of mice.

Sublethal doses of CdCl2 (3 mg/kg iv), HgCl2 (2 mg/kg iv), or NaVO3 (6 mg/kg iv) did not alter the content of reduced glutathione (GSH) in the livers of mice during the 24-h observation period. In the kidneys, a tendency to increased GSH content was seen, especially after HgCl2 treatment; in lung and brain the GSH levels were significantly lowered upon the treatment with all three metals. The activities of GSH S-transferase toward an aryl substrate (CDNB; 1-chloro-2,4-dinitrobenzene) was enhanced in all tissues by the administration of HgCl2 greater than NaVO3 greater than CdCl2. The activity of GSH S-transferase toward an epoxide substrate [1,2-epoxy-3-(p-nitrophenoxy)propane was only measurable in the livers and was inhibited 1 and 2 h after the administration of HgCl2 and NaVO3. It is concluded that sublethal doses of CdCl2, HgCl2, or NaVO3 do not impair the GSH concentration and GSH-conjugating enzyme activities toward the aryl substrate in different target organs of their toxicity, which is in contrast to results obtained in vitro.

Animals↗
PubMed1997

Effect of electrical stimulation in combination with calcium chloride or sodium chloride treatments at constant ionic strength on moisture binding and textural quality of early-harvested breast fillets.

The objective of this study was to assess the effects of a CaCl2 or NaCl treatment combined with electrical stimulation (ES) on textural and moisture binding of early-harvested chicken breast fillets. During exsanguination, half the birds were subjected to ES, and then all carcasses were aged for 30, 60, 90, or 120 min before excising both Pectoralis major muscles. Half the muscles were chilled with a NaCl solution and half with a CaCl2 solution. Effects of ES and chill medium composition on meat pH, moisture absorption, cooking loss, and shear value of the fillets were assessed. The ES reduced meat pH for the NaCl-treated muscles, but had no effect on those treated with CaCl2 of on moisture absorbed during chilling. Cooking loss was greater for the CaCl2-treated than NaCl-treated muscles and for muscles from stimulated birds that were excised more than 30 min post-mortem. Shear values were unaffected by chilling medium composition. However, even though shear values for both ES and unstimulated birds declined as aging time increased, the rate of decline was greater, and ultimate shear value lower, for muscles from ES birds. Results indicate that, although ES might offer some advantage in improving the tenderness of early-harvested breast fillets, combining ES with CaCl2 treatment offers no real advantage. Moreover, reductions in moisture binding properties by these technologies might limit applicability in some commercial environments.

Absorption↗
PubMed1998

Comparative effects of added sodium chloride, ammonium chloride, or potassium bicarbonate in the drinking water of broilers, and feed restriction, on the development of the ascites syndrome.

A hypothesis that the ionic composition of drinking water might affect development of the ascites syndrome in broilers was investigated in two trials. The first trial comprised four groups of 650 male chicks. A control treatment was normal tap water and the other three treatments comprised the addition to the tap water of 1,000 mg/L sodium as NaCl, 5,000 mg/L NH4Cl, or 5,000 mg/L KHCO3, supplied from age 2 to 47 d. At Day 28, equally sized subsets of these groups were moved to individual cages, where they received a severe exposure to ambient cold. The development of the ascites syndrome was monitored by measurements of hematocrit and arterial blood oxygen saturation (PaO2) by oximetry, body weight, and examination of dead birds for cause of death. Mortality from ascites in cold-exposed birds from Days 28 to 47 was 28, 48, 40, and 16% in the tap water, NaCl, NH4Cl, and KHCO3 groups, respectively; only the NaCl mortality was significantly different from the tap water mortality. The KHCO3 treatment increased PaO2 (compared with tap water treatment) at Day 28 by 5.5% and at Day 35 by 10.5%, but not at Day 42. The KHCO3 caused a reduction in body weight, which was 13% less than the tap water group at Day 42, probably due to a chronic toxicity. The second trial specifically examined the same parameters with lower water levels of KHCO3 (3,000 and 1,000 mg/L), in comparison to a 10% feed restriction protocol, in order to clarify whether the increased PaO2 was due to a specific effect of the KHCO3 or was a metabolic manifestation of a reduced growth rate. The 3,000 mg/L KHCO3 treatment had no effect on PaO2, but the 1,000 mg/L treatment augmented PaO2 by 5.3% at Day 35 (but not at Days 28 or 42), without reducing the final body weight. The feed restriction group showed an elevated PaO2 of 5.4% at Day 35 (but not at Days 28 or 42), with no reduction in the final body weight. The inclusion of 1,000 mg/L of KHCO3 into the drinking water of broilers or a temporary 10% feed restriction may be means to augment PaO2.

Ammonium Chloride↗
PubMed1999

Chloride dependence of hyperpolarization-activated chloride channel gates.

1. ClC proteins are a class of voltage-dependent Cl- channels with several members mutated in human diseases. The prototype ClC-0 Torpedo channel is a dimeric protein; each subunit forms a pore that can gate independently from the other one. A common slower gating mechanism acts on both pores simultaneously; slow gating activates ClC-0 at hyperpolarized voltages. The ClC-2 Cl- channel is also activated by hyperpolarization, as are some ClC-1 mutants (e.g. D136G) and wild-type (WT) ClC-1 at certain pH values. 2. We studied the dependence on internal Cl- ([Cl-]i) of the hyperpolarization-activated gates of several ClC channels (WT ClC-0, ClC-0 mutant P522G, ClC-1 mutant D136G and an N-terminal deletion mutant of ClC-2), by patch clamping channels expressed in Xenopus oocytes. 3. With all these channels, reducing [Cl-]i shifted activation to more negative voltages and reduced the maximal activation at most negative voltages. 4. We also investigated the external halide dependence of WT ClC-2 using two-electrode voltage-clamp recording. Reducing external Cl- ([Cl-]o) activated ClC-2 currents. Replacing [Cl-]o by the less permeant Br- reduced channel activity and accelerated deactivation. 5. Gating of the ClC-2 mutant K566Q in normal [Cl-]o resembled that of WT ClC-2 in low [Cl-]o, i.e. channels had a considerable open probability (Po) at resting membrane potential. Substituting external Cl- by Br- or I- led to a decrease in Po. 6. The [Cl-]i dependence of the hyperpolarization-activated gates of various ClC channels suggests a similar gating mechanism, and raises the possibility that the gating charge for the hyperpolarization-activated gate is provided by Cl-. 7. The external halide dependence of hyperpolarization-activated gating of ClC-2 suggests that it is mediated or modulated by anions as in other ClC channels. In contrast to the depolarization-activated fast gates of ClC-0 and ClC-1, the absence of Cl- favours channel opening. Lysine 556 may be important for the relevant binding site.

Animals↗
PubMed2003

A conserved pore-lining glutamate as a voltage- and chloride-dependent gate in the ClC-2 chloride channel.

ClC-2 is a ubiquitously expressed, two-pore homodimeric Cl- channel opened by hyperpolarisation. Little is known about its gating mechanisms. Crystallographic and functional studies in other ClC channels suggest that a conserved glutamate residue carboxylate side-chain can close protopores by interacting with a Cl--binding site in the pore. Competition for this site is thought to provide the molecular basis for gating by extracellular Cl-. We now show that ClC-2 gating depends upon intra- but not extracellular Cl- and that neutralisation of E217, the homologous pore glutamate, leads to loss of sensitivity to intracellular Cl- and voltage. Experiments testing for transient activation by extracellular protons demonstrate that E217 is not available for protonation in the closed channel state but becomes so after opening by hyperpolarisation. The results suggest that E217 is a hyperpolarisation-dependent protopore gate in ClC-2 and that access of intracellular Cl- to a site normally occupied by its side-chain in the pore stabilises the open state. A remaining hyperpolarisation-dependent gate might correspond to that closing both pores simultaneously in other ClC channels.

Amino Acid Substitution↗
PubMed2003

The effects of calcium chloride and sodium chloride on the electroporation-mediated skin permeation of fluorescein isothiocyanate (FITC)-dextrans in vitro.

We previously reported the substantial synergic effects of electroporation and electrolytes, particularly those containing CaCl(2) on the skin permeation of the model low-molecular weight compound, calcein. We then investigated the effects of electroporation (300 V, 10 msx10 times) and 150 mM NaCl or CaCl(2) on skin permeation of higher molecular weight compounds, fluorescein isothiocyanate (FITC)-dextrans (FD-4, FD-10 and FD-40; average molecular weight, 4.4, 9.6 and 35.6 kDa, respectively) using excised hairless rat skin. The observed steady state flux of FD-4 was 1.3 pmol/cm(2)/h after electroporation without NaCl or CaCl(2). The flux did not differ greatly from that without electroporation. In contrast, a much higher steady state flux was observed after electroporation with NaCl or CaCl(2) (2.5 and 8.2 pmol/cm(2)/h, respectively). For FD-10 and FD-40, no flux was detected with electroporation in water (without electrolytes) or without electroporation. On the other hand, high skin permeation was observed after electroporation in NaCl or CaCl(2) solution (FD-10: 7.5 and 18.2 pmol/cm(2)/h, FD-40: 4.5 and 9.3 pmol/cm(2)/h in NaCl and CaCl(2), respectively). The effects of CaCl(2) on FD permeation were greater than those of NaCl. The present finding suggests that electroporation application in the presence of electrolytes, particularly CaCl(2), was very effective in increasing transdermal delivery of water-soluble macromolecules.

Animals↗
PubMed1981

Results of sputum, cytology among workers exposed to vinyl chloride monomer and to poly(vinyl chloride).

The results of systematic cytological sputum examinations of 3,380 Italian VC-PVC industry workers and of 2,287 workers in other industries at different potential risk and chosen as control groups are reported. The results indicate an increase in cellular abnormalities and dysplasias in the epithelium of the respiratory tract among VC-PVC workers. These data are in line with experimental results showing that VC produces lung tumors in mice and with early epidemiological evidence among exposed workers.

Humans↗
PubMed2004

Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel.

The ClC family of anion channels mediates the efficient, selective permeation of Cl(-) across the biological membranes of living cells under the driving force of an electrochemical gradient. In some eukaryotes, these channels are known to exhibit a unique gating mechanism, which appears to be triggered by the permeant Cl(-) anion. We infer details of this gating mechanism by studying the free energetics of Cl(-) occupancy in the pore of a prokaryotic ClC homolog. These free energetics were gleaned from 30 ns of molecular dynamics simulation on an approximately 133,000-atom system consisting of a hydrated membrane embedded StClC transporter. The binding sites for Cl(-) in the transporter were determined for the cases where the putative gating residue, Glu(148), was protonated and unprotonated. When the glutamate gate is protonated, Cl(-) favorably occupies an exterior site, S(ext), to form a queue of anions in the pore. However, when the glutamate gate is unprotonated, Cl(-) cannot occupy this site nor, consequently, pass through the pore. An additional, previously undetected, site was found in the pore near the outer membrane that exists regardless of the protonation state of Glu(148). Although this suggests that, for the prokaryotic homolog, protonation of Glu(148) may be the first step in transporting Cl(-) at the expense of H(+) transport in the opposite direction, an evolutionary argument might suggest that Cl(-) opens the ClC gate in eukaryotic channels by inducing the conserved glutamate's protonation. During an additional 20 ns free dynamics simulation, the newly discovered outermost site, S(out), and the innermost site, S(int), were seen to allow spontaneous exchange of Cl(-) ions with the bulk electrolyte while under depolarization conditions.

Algorithms↗