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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Although supplemental fatty acids have been shown to alter the susceptibility of experimental animals to oxidant gases, the relationship between the degree of tissue fatty acyl unsaturation and resistance to oxidant exposure remains undefined. Because vascular endothelial cells have been demonstrated to be sensitive cellular targets in oxidant-induced lung injury, we evaluated the effects of a supplemental fatty acid on the lipid composition and oxidant susceptibility of pulmonary artery endothelial cells (PAEC) in monolayer culture. PAEC were incubated in culture medium supplemented with an ethanolic solution of 0.1 mM cis-vaccenic acid (CVA), an 18-carbon monounsaturated fatty acid, or with the ethanol vehicle alone for 3 h. Cells were then exposed to either control or oxidant (hyperoxia: 95% O2; or hydrogen peroxide: 100 microM) conditions. Oxidant-induced cell injury was assessed by phase-contrast microscopy and by measuring the release of intracellular lactate dehydrogenase. Incubation with CVA increased the CVA content of PAEC lipids and protected cells from oxidant-induced injury for up to 72 h after supplementation. CVA had no effect on nonoxidant-induced cell injury. Although the mechanism by which CVA protects cells against oxidant injury remains undefined, evidence is presented that indicates the mechanism does not involve induction of antioxidant enzyme activity, alterations in the physical state of PAEC membranes, or enhancement of PAEC nucleic acid repair mechanisms. These results define a useful model for exploring the relationship between lipid composition and oxidant susceptibility and suggest that fatty acid modifications may constitute an important strategy for protecting cells against oxidant injury.
Am J Respir Cell Mol Biol 1990 Nov
PMID:Fatty acid supplementation protects pulmonary artery endothelial cells from oxidant injury. 222 2

In this review the results of the interaction of the active dyes used in the USSR textile industry with microbial enzymes and blood serum proteins are discussed. The complexity of dye/protein interaction and the dependence of this interaction on different factors is demonstrated. Some practical aspects of the use of dye containing sorbents are presented and discussed. Their suitability for RNA ligase and DNA ligase, acetate kinase, alcohol dehydrogenase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase purification and blood serum protein fractionation is demonstrated.
J Mol Recognit 1990 Jun
PMID:Investigation of dye/protein interaction and its application to enzyme purification. 222 63

In normoxic hearts a limited number of multilamellar vesicles was found in both endothelial cells and myocytes. The total number of multilamellar vesicles observed in myocytes, particularly those extruded from mitochondria, significantly increased in hearts rendered ischemic for at least 60 mins. The number of multilamellar vesicles extruded from sarcolemma was increased in hearts reperfused after this period of ischemia. The number of multilamellar vesicles in or adjacent to lipid droplets was independent of the duration of ischemia. Multilamellar vesicles were similar in size and periodicity of the lamellae. It is proposed that the number of multilamellar vesicles can be used to quantitate ischemic membrane injury. The formation of multilamellar vesicles was significantly related in time to (a) the accumulation of arachidonic acid and total fatty acids; (b) a decrease in the tissue content of ATP and (c) the release of lactate dehydrogenase (LDH). No significant alterations in the total tissue content of triacylglycerols and phospholipids were detected. The amount of arachidonic acid accumulated in the hearts reflects the degradation of only a minor fraction of the phospholipid pool. Assuming a close relationship between phospholipid degradation, induction of multilamellar vesicles and loss of cellular integrity, the present findings might indicate that the loss of a small part of phospholipids might have serious pathophysiological consequences, as indicated by the morphological changes in cellular membranes and the release of cytoplasmic macromolecules.
J Mol Cell Cardiol 1990 Jun
PMID:Ischemia and reperfusion induced multilamellar vesicles in isolated rabbit hearts: time correlation between morphometric data and metabolic alterations. 223 35

UIe effects of propranolol and atenolol on free radical mediated injury in myocytes were examined. Freshly isolated adult canine myocytes were incubated with a superoxide generating (from dihydroxyfumarate) and Fe-catalyzed free radical system. Exposure of the myocytes to free radicals for 20 min resulted in more than a 5-fold increase in thiobarbituric acid reactant (peroxide) formation and elevated levels of lactate dehydrogenase (LDH) activity released into the media compared to controls. Ultrastructurally, severe sarcolemmal damage, mitochondrial and myofibril derangements were evident. At 40 min, cellular viability (trypan blue exclusion) in the samples exposed to free radicals decreased to about one-third of controls; concomitantly, major losses in total cellular phospholipids occurred. When the cells were pretreated with 200 microM propranolol before the addition of free radicals, both peroxide formation and increased LDH release were inhibited; in agreement, complete ultrastructural preservation was observed. In addition, the subsequent losses in cellular viability and phospholipids were prevented. For comparison, the more water soluble beta-blocker, atenolol at 200 microM was shown ineffective in providing significant protection against the induced injury. The results suggest that propranolol may provide antiperoxidative protection to myocytes when elevated levels of free radicals are present.
J Mol Cell Cardiol 1990 Jun
PMID:Oxygen radical-mediated injury of myocytes-protection by propranolol. 223 36

The controversial subject of the subcellular location of myocardial adenosine production was studied employing density gradient fractionation of heart muscle combined with a novel method for analyzing distribution profiles based on multiple regression (correlation) analysis. Bungarotoxin binding, N-acetyl-beta-D-glucosaminidase, cytochrome c oxidase, NADPH-dependent cytochrome c reductase and lactate dehydrogenase were used as markers for the plasma membrane, lysosomes, mitochondria, sarcoplasmic reticulum and cytosol, respectively. The normalized distribution frequencies (fraction of total) of 5'-nucleotidase in mitochondria, lysosomes, plasma membranes, sarcoplasmic reticulum and cytosol in the 50 x g supernatant of total homogenate of heart muscle were found to be 0, 0.25, 0.44, 0.08 and 0.23, respectively. To increase the resolution power of this approach with respect to mitochondria, a crude mitochondrial fraction was also studied, in which the normalized distribution of 5'-nucleotidase in the homogenate was 0, 0.16 and 0.84 in mitochondria, plasma membranes and lysosomes, respectively. This mainly lysosomal 5'-nucleotidase activity was 61% inhibited by the alpha,beta-methylene analog of ADP, indicating that although the latter has been considered specific to the plasma membrane enzyme, it also inhibits the lysosomal enzyme. The intercellular distribution of 5'-nucleotidase was not studied, but the lack of this enzyme in the mitochondria indicate that the adenosine production observed during mitochondrial AMP production, e.g. during acetate oxidation in intact heart muscle, must involve AMP transport out from the mitochondria.
J Mol Cell Cardiol 1990 Jul
PMID:Subcellular distribution of myocardial 5'-nucleotidase. 223 47

Menadione bisulfite is a hepatotoxicant that damages periportal regions of the lobule in perfused liver in an oxygen-dependent manner. The effect of ethanol on menadione bisulfite toxicity was examined in perfused rat liver. Addition of menadione bisulfite (3 mM) alone to the perfusate increased oxygen uptake by 20-30 mumols/g/hr. Lactate dehydrogenase was released into the effluent after 60 min of perfusion and reached values around 100 units/g/hr. Under these conditions, trypan blue was taken up exclusively in periportal regions of the liver lobule; 44% of periportal cells were stained. In the presence of ethanol, maximal increases in oxygen uptake due to menadione bisulfite were much larger (about 90 mumols/g/hr), and lactate dehydrogenase release occurred earlier and reached higher maximal values (330 units/g/hr). Trypan blue staining was also more extensive; 90% of periportal cells were stained. The effect of ethanol on menadione bisulfite-induced oxygen uptake required metabolism via alcohol dehydrogenase (ADH), because ethanol increased oxygen uptake due to menadione bisulfite from 44 to 81 mumols/g/hr in deermice with ADH but had no effect in deermice lacking ADH. Other agents that increase NADH (xylitol and 2-ethyl-1-hexanol) also potentiated the stimulation of oxygen uptake due to menadione bisulfite, suggesting that ethanol was working by increasing the NADH redox state. Cyanide abolished the increase in oxygen uptake due to menadione bisulfite, both in the absence and in the presence of ethanol, supporting the hypothesis that the effect of ethanol on menadione bisulfite-mediated oxygen uptake involves the mitochondrial respiratory chain. Further, the stimulation of oxygen uptake by menadione bisulfite in isolated mitochondria was enhanced when matrix NADH was increased by addition of beta-hydroxybutyrate. These data indicate that ethanol potentiates oxygen uptake and toxicity due to menadione bisulfite most likely by generation of NADH for redox cycling of this model quinone.
Mol Pharmacol 1990 Dec
PMID:Ethanol potentiates oxygen uptake and toxicity due to menadione bisulfite in perfused rat liver. 225 Jun 68

Aspartate (AST) and alanine (ALT) aminotransferase together with lactate dehydrogenase (LD) from the tissue homogenate of the Biomphalaria alexandrina snails, were partially characterized by measuring the Michaelis constant (km) and the maximum velocity (Vmax). The isoenzymatic pattern of lactate dehydrogenase was investigated through polyacrylamide gel electrophoresis.
Cell Mol Biol 1990
PMID:Kinetic properties of two transaminases and lactate dehydrogenase of Biomphalaria alexandrina snails, intermediate hosts of Schistosoma mansoni. 227 60

The early structural changes of F344 rat hepatocytes exposed to the hepatocarcinogen 1,2-dimethylhydrazine (DMH) were characterized in short-term monolayer cultures. Continuous exposure of monolayers to DMH (2-16 mM) caused cytoplasmic vacuoles visible by phase-contrast microscopy in all hepatocytes within 6 hr of exposure. These changes preceded maximal release of lactate dehydrogenase (LDH) which occurred after 48 hr of continuous exposure to cytocidal concentrations of DMH (8-16 mM). Ultrastructurally, hepatocytes exposed to DMH (4 mM, 6 hr) showed a twofold increase in mitochondrial diameter from 340 +/- 70 nm in control hepatocytes to 800 +/- 140 nm in DMH-exposed cells. Hepatocyte monolayers exposed to DMH (4 mM, 6 hr) with subsequent removal of DMH attained normal phase-contrast appearance within 6 hr. Ultrastructural studies showed no significant differences when compared with control hepatocytes and mitochondrial diameters (330 +/- 70 nm) were comparable with control hepatocytes. Pretreatment of hepatocytes with depletors of cellular reduced glutathione concentration, including 1,3-bis(2-chloroethyl)-1-nitrosourea (40 microM) and diethyl maleate (160 microM), did not potentiate hepatocellular vacuolation nor release of LDH from hepatocytes exposed to DMH (0-16 mM, 48 hr). These studies demonstrate a distinctive form of reversible high-amplitude mitochondrial swelling that can be monitored by phase-contrast microscopy of cultured hepatocytes in monolayers. Since DMH-induced mitochondrial swelling and its progression to irreversible injury are not potentiated by depletors of reduced thiols, this response appears distinct from prelethal mitochondrial swelling in hepatocytes subjected to oxyradical-mediated mechanisms of injury.
Exp Mol Pathol 1990 Apr
PMID:Reversible mitochondrial swelling in cultured rat hepatocytes exposed to 1,2-dimethylhydrazine. 233 34

Formation of C5b-9 channels in the plasma membrane can lead to erythrocyte lysis or nucleated cell death. Lysis of erythrocytes by complement occurs as a result of colloid osmotic swelling and rupture of the plasma membrane, due to the unregulated flux of ions and water through C5b-9 channels. This colloid osmotic mechanism of lysis is largely based on the evidence that the extent of hemolysis is reduced, when macromolecules are placed in the medium to balance the osmotic gradient created by intracellular macromolecules, which are too large to diffuse through complement channels. The role of colloid osmotic deregulation, as a cause of nucleated cell killing by C5b-9, however, has been recently questioned [Kim S., Carney D. F. and Shin M. L. J. Immun. 138, 1530 (1987)]. In the present study, we investigated the effect of osmotic protection, with an 81,000 mol. wt dextran or bovine serum albumin, on Ehrlich cell killing by complement channels. The results indicated that prevention of cell swelling by dextran did not reduce the extent or rate of nucleated cell killing by either small (C5b-9l), or large (C5b-9m), complement channels when assessed by vital dye stain. The release of cytoplasmic lactate dehydrogenase as an alternative measure of cell death, however, was retarded and/or reduced, in the presence of dextran or albumin, at concns that prevented cell swelling. These results indicate that C5b-9 can kill nucleated cells effectively, in the absence of colloidal osmotic cell swelling, and that release of cytoplasmic macromolecules may not be a reliable indicator of cell death, when osmotic protectants are employed.
Mol Immunol 1989 Mar
PMID:Effect of osmotic protection on nucleated cell killing by C5b-9: cell death is not affected by the prevention of cell swelling. 246 81

The activities of aspartate aminotransferase (AST) (EC.2.6.1.1.) I, alanine aminotransferase (ALT) (EC.2.6.1.2) II and lactate dehydrogenase (LD) (EC.1.1.1.27) III have been measured in tissue homogenate and in haemolymph of Biomphalaria alexandrina snails, the specific intermediate host for the human parasitic disease schistosomiasis due to Schistosoma mansoni.
Cell Mol Biol 1989
PMID:Selected enzymatic activities in fresh water snails, specific intermediate host for human schistosomiasis. 249 22


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