Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Consumption of ethanol by rats during pregnancy reduces the body and brain weight of their fetuses and pups. The reduction is greater if the offspring are kept with their alcohol-fed mothers rather than with control surrogate mothers during lactation. The activity of several enzymes of the neuronal cell membranes (Na+, K+-ATPase, Ca2+-ATPase, acetylcholinesterase, 5'-nucleotidase) is also reduced. This decrease in enzyme activity may be related to the decrease in neuronal development and could produce profound alterations in brain function. Altered hypothalamic-hypophysial function may be partly responsible for developmental anomalies found in the fetal alcohol syndrome. The levels of plasma luteinizing hormone are lower in pups exposed prenatally to ethanol, and prolactin levels are much higher. Concentrations of ethanol were essentially the same in maternal blood and in the fetus. Acetaldehyde levels in the placenta, amniotic fluid and the remaining fetal tissue at days 15 and 19 of gestation were about 40-50% of those in maternal blood. Acetaldehyde may be important in the pathogenesis of the fetal alcohol syndrome.
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PMID:Growth, enzymes and hormonal changes in offspring of alcohol-fed rats. 656 94

The acute effects of ethanol on the nervous system are thought to be associated with disturbance of neural membrane function. In the present study the effects of ethanol, its immediate metabolite, acetyldehyde, and tertiary butanol which is not further metabolized to an aldehyde, on selected membrane-bound enzymes were examined in vitro in rat brain. The enzymes included acetylcholinesterase, succinate dehydrogenase, Na+K+-ATPase and cytochrome c oxidase. At concentrations ranging from 0.07 - 2% w/v (15 - 435 mM) ethanol did not produce significant inhibition of any of the enzymes tested. On the other hand acetaldehyde at concentrations ranging from 0.01 - 0.5% w/v (2 - 114 mM) showed marked inhibition of all the abovementioned enzymes except acetylcholinesterase. The responses of the various enzymes to tertiary butanol were intermediate between those obtained with ethanol and acetaldehyde. Further studies are in progress to evaluate the significance of these findings to the understanding of alcohol intoxication, tolerance and dependence in man.
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PMID:Effect of ethanol and acetaldehyde on membrane-bound enzymes in rat brain. 742 41

The sarcoplasmic reticulum (SR) of rabbit skeletal muscle was irradiated with ultraviolet light (UV) in the presence of vanadate plus 2 mM EGTA, 10 mM MgCl2, 20% DMSO, and 50 mM PIPES (pH 6.5) at room temperature. In the presence of 100 microM vanadate, the Ca(2+)-uptake activity of SR rapidly decreased and was almost lost in 20 min. The activity was inhibited as a function of vanadate concentration with an apparent Ki of about 20 microM. On the other hand, Ca(2+)-dependent ATP hydrolytic activity as well as phosphoenzyme (EP) formation activity decreased very slowly, and more than 50% of these activities remained 20 min after initiation of the vanadate-UV treatment. Half inhibition of these activities required about 100 microM vanadate. The loss of the relationship between Ca(2+)-uptake and ATPase reaction was found to be mainly caused by an increase in the Ca2+ permeability of the SR membrane, which was raised by increasing the vanadate concentration or UV irradiation time in a manner similar to that observed for the Ca2+ uptake. No rise in Ca2+ permeability occurred in liposomes reconstituted from SR lipid when they were irradiated with UV in the presence of 100 microM vanadate. When the vanadate-UV-treated SR was allowed to react with fluoral-P (4-amino-3-penten-2-one), an indicator of aldehyde, and the membrane proteins were separated by HPLC in the presence of SDS, the fluorescent probe was found to be closely associated with the Ca(2+)-ATPase fraction.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Irradiation with ultraviolet light in the presence of vanadate increases Ca2+ permeability of the sarcoplasmic reticulum membrane via Ca(2+)-ATPase. 760 20

It has been shown that alcohol administration causes baroreceptor reflex inhibition. The site of action of alcohol could reside anywhere within the baroreceptor reflex arc. Therefore, the goal of this study was to determine the effects of acute administration of alcohol on carotid sinus baroreceptor discharge characteristics. In pentobarbital-anesthetized dogs, the carotid sinus was isolated and perfused. Single unit baroreceptor discharge was recorded from the carotid sinus nerve along with carotid sinus diameter using sonomicrometry. Carotid sinus pressure-baroreceptor discharge and carotid sinus pressure-diameter curves were constructed. Perfusion of the carotid sinus with alcohol (100 mmol/L) significantly decreased the pressure threshold from 91.1 +/- 2.8 to 86.4 +/- 2.9 mm Hg (p < 0.05) and increased the peak discharge rate from 45.8 +/- 3.4 to 52.8 +/- 3.6 spikes per second (p < 0.01). The same phenomenon was seen during perfusion of the carotid sinus with acetaldehyde (2.5 mmol/L) but was not seen during perfusion with acetate (2.5 mmol/L). During perfusion of the carotid sinus with alcohol, the carotid sinus pressure-carotid sinus diameter relation did not change. The baroreceptor sensitization induced by alcohol is not an endothelium-dependent mechanism, because endothelial denudation did not block this alcohol-induced effect. Measurement of the duration of postexcitatory depression of carotid sinus baroreceptors, which is related to Na+,K(+)-ATPase activity, showed that perfusion of the carotid sinus with alcohol or acetaldehyde significantly reduced the duration of postexcitatory depression, indicating that the alcohol- and acetaldehyde-induced effect on baroreceptor discharge is most likely mediated by an inhibition of Na+,K(+)-ATPase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Acute alcohol administration stimulates baroreceptor discharge in the dog. 849 3

Peroxidation of membrane lipids results in release of the aldehyde 4-hydroxynonenal (HNE), which is known to conjugate to specific amino acids of proteins and may alter their function. Because accumulating data indicate that free radicals mediate injury and death of neurons in Alzheimer's disease (AD) and because amyloid beta-peptide (A beta) can promote free radical production, we tested the hypothesis that HNE mediates A beta 25-35-induced disruption of neuronal ion homeostasis and cell death. A beta induced large increases in levels of free and protein-bound HNE in cultured hippocampal cells. HNE was neurotoxic in a time- and concentration-dependent manner, and this toxicity was specific in that other aldehydic lipid peroxidation products were not neurotoxic. HNE impaired Na+, K(+)-ATPase activity and induced an increase of neuronal intracellular free Ca2+ concentration. HNE increased neuronal vulnerability to glutamate toxicity, and HNE toxicity was partially attenuated by NMDA receptor antagonists, suggesting an excitotoxic component to HNE neurotoxicity. Glutathione, which was previously shown to play a key role in HNE metabolism in nonneuronal cells, attenuated the neurotoxicities of both A beta and HNE. The antioxidant propyl gallate protected neurons against A beta toxicity but was less effective in protecting against HNE toxicity. Collectively, the data suggest that HNE mediates A beta-induced oxidative damage to neuronal membrane proteins, which, in turn, leads to disruption of ion homeostasis and cell degeneration.
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PMID:A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide. 897 33

The oxyntic, or parietal cell has two characteristic membrane systems. The mammalian intracellular canaliculi are specialized networks of narrow channels lined with numerous microvilli. The other common to all oxyntic cells is the tubulovesicles, a system of tubules and vesicles. The tubulovesicular compartment is drastically depleted during maximal gastric acid secretion and this is coincident with an increase in the cell surface membrane area. A plausible explanation of this process is the fusion and transfer of tubulovesicular membranes to the plasma membrane. However, for many years there was no convincing evidence of the connections between these two membrane systems. How the tubulovesicular membranes transform into plasma membrane without demonstrable connections has been an enigma to electron microscopists. Recent ultra-high resolution scanning electron microscopic observation on the rat oxyntic cell treated with aldehyde-osmium-aldehyde method revealed that in the resting stage, the tubulovesicles were isolated spherical vesicles. But after tetragastrin stimulation, they were interconnected by slender connecting tubules forming a tubulovesicular network. Then this network was fused to the intracellular canaliculus at relatively few points. These connections between the tubulovesicles and luminal surface membrane was also demonstrated in the frog oxynticopeptic cells. In this review, these membrane transformations as well as changes of the H+/K(+)-ATPase, the lectin binding glycocalyx and the cytoskeleton during secretion will be illustrated and discussed.
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PMID:Gastric oxyntic cell structure as related to secretory activity. 922 57

Interaction of many infectious agents with eukaryotic host cells is known to cause activation of the ubiquitous transcription factor nuclear factor kappaB (NF-kappaB) (U. Siebenlist, G. Franzoso, and K. Brown, Annu. Rev. Cell Biol. 10:405-455, 1994). Recently, we reported a biphasic pattern of NF-kappaB activation in cultured human umbilical vein endothelial cells consequent to infection with Rickettsia rickettsii, an obligate intracellular gram-negative bacterium and the etiologic agent of Rocky Mountain spotted fever (L. A. Sporn, S. K. Sahni, N. B. Lerner, V. J. Marder, D. J. Silverman, L. C. Turpin, and A. L. Schwab, Infect. Immun. 65:2786-2791, 1997). In the present study, we describe activation of NF-kappaB in a cell-free system, accomplished by addition of partially purified R. rickettsii to endothelial cell cytoplasmic extracts. This activation was rapid, reaching maximal levels at 60 min, and was dependent on the number of R. rickettsii organisms added. Antibody supershift assays using monospecific antisera against NF-kappaB subunits (p50 and p65) confirmed the authenticity of the gel-shifted complexes and identified both p50-p50 homodimers and p50-p65 heterodimers as constituents of the activated NF-kappaB pool. Activation occurred independently of the presence of endothelial cell membranes and was not inhibited by removal of the endothelial cell proteasome. Lack of involvement of the proteasome was further confirmed in assays using the peptide-aldehyde proteasome inhibitor MG 132. Activation was not ATP dependent since no change in activation resulted from addition of an excess of the unhydrolyzable ATP analog ATPgammaS, supplementation with exogenous ATP, or hydrolysis of endogenous ATP with ATPase. Furthermore, Western blot analysis before and after in vitro activation failed to demonstrate phosphorylation of serine 32 or degradation of the cytoplasmic pool of IkappaB alpha. This lack of IkappaB alpha involvement was supported by the finding that R. rickettsii can induce NF-kappaB activation in cytoplasmic extracts prepared from T24 bladder carcinoma cells and human embryo fibroblasts stably transfected with a superrepressor phosphorylation mutant of IkappaB alpha, rendering NF-kappaB inactivatable by many known signals. Thus, evidence is provided for a potentially novel NF-kappaB activation pathway wherein R. rickettsii may interact with and activate host cell transcriptional machinery independently of the involvement of the proteasome or known signal transduction pathways.
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PMID:Proteasome-independent activation of nuclear factor kappaB in cytoplasmic extracts from human endothelial cells by Rickettsia rickettsii. 957 57

20S proteasomes were purified from Streptomyces coelicolor A3(2) and shown to be built from one alpha-type subunit (PrcA) and one beta-type subunit (PrcB). The enzyme displayed chymotrypsin-like activity on synthetic substrates and was sensitive to peptide aldehyde and peptide vinyl sulfone inhibitors and to the Streptomyces metabolite lactacystin. Characterization of the structural genes revealed an operon-like gene organization (prcBA) similar to Rhodococcus and Mycobacterium spp. and showed that the beta subunit is encoded with a 53-amino-acid propeptide which is removed during proteasome assembly. The upstream DNA region contains the conserved orf7 and an AAA ATPase gene (arc).
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PMID:The 20S proteasome of Streptomyces coelicolor. 976 79

Ethanol may alter the homeostasis of water and electrolytes before the occurrence of liver damage able to explain these disorders. How the kidney may become involved in water diuresis or sodium and potassium retention has not been well elucidated. During the last decade, an increasing body of evidence has guided interest toward the relevance of the biochemical basis of ethanol-induced injury to the kidney. Multiple functional abnormalities of renal tubules may be associated with ethanol-induced changes in membrane composition and lipid peroxidation of these epithelial cells. Ethanol interferes with the carrier function by decreasing (Na+K)-ATPase activity, but this activity is enhanced by chronic exposure. Recently, it was reported that ethanol oxidation by the kidney is favored in chronic ethanol-treated rats, thereby suggesting a pathogenic role for acetaldehyde in the nephrotoxic effect of ethanol ingestion. Also, increased reactive oxygen species, partly generated from acetaldehyde oxidation, may contribute to the occurrence of oxidative stress. The pathophysiology of renal regulation of water and electrolytes of alcoholic disease is analyzed on the basis of recent advances in our knowledge concerning the biochemical effects of ethanol on the kidney.
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PMID:Effect of ethanol ingestion on renal regulation of water and electrolytes. 977 53

We have examined lipid peroxidation (LPO) and fatty acid acyl chain dynamics in synaptosomal membranes isolated from aged rat (Fischer 344 x Brown Norway F1 hybrids) brains, correlating these results with measurements of enzymatic activity of the synaptic plasma membrane Ca2(+)-ATPase (PMCA). Calcium-dependent ATPase activity in these membranes exhibits progressive decreases with a maximal loss of activity with age of approximately 35%. The sensitivity of this membrane-bound ion transporter to the lipid composition of the surrounding membrane, as well as the high abundance of oxidatively sensitive polyunsaturated fatty acyl chains in synaptosomal membranes, suggests that this age-related loss in catalytic turnover may result from LPO-mediated protein modification and/or changes in the physical structure of the bilayer. However, high-performance liquid chromatography analysis of 2,4-dinitrophenylhydrazone derivatives reveals no significant age-related increases in the content of reactive aldehydes (malondialdehyde, formaldehyde, acetaldehyde or acetone) which comprise breakdown products of lipid peroxidation. Electron paramagnetic resonance measurements employing 5- and 12-stearic acid spin labels with the nitroxide reporter groups at two depths in the bilayer were used to assess the fatty acyl chain dynamics (fluidity) of synaptosomal membranes. The resulting spectra demonstrate anisotropic lipid dynamics of two populations of lipids, i.e. lipids in direct association with membrane proteins (boundary lipids) and bulk lipids that do not directly associate with proteins. The nanosecond dynamics of both lipid populations is unaltered with age indicating that any compositional changes occurring with age are insufficient to result in alterations in bilayer fluidity relevant to PMCA activity. Thus, the observed age-related decline in PMCA activity may be explained by direct modification of membrane protein.
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PMID:Decrease in Ca-ATPase activity in aged synaptosomal membranes is not associated with changes in fatty acyl chain dynamics. 986 36


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