Action of metabolic inhibitors on the release of intra-cellular enzymes from human and rat lymphocytes and human erythrocytes

Hallak, G J; Wilkinson, J. H.

doi:10.1016/0009-8981(76)90062-0

Cited by 12 publications

(5 citation statements)

References 21 publications

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“…Acosta et al (1978) showed with primary monolayer cultures of postnatal rat myocardial cells that complete deprivation of glucose and oxygen caused marked release of cytoplasmic enzymes, and that enzyme leakage was reversed by a change to complete medium and an atmosphere of 20% 02. Hallak and Wilkinson (1976) examined the effects of various inhibitors of glycolysis and uncouplers of oxidative phosphorylation and found that release of intracellular enzymes was controlled by the energy level of the cells. In contrast to the effects of these compounds on enzyme leakage by primary effects on the intracellular ATP level, the primary effect of CC14 seems to be on lipid peroxidation (Recknagel et al, 1982).…”

Section: Discussionmentioning

confidence: 99%

Enzyme leakage due to change of membrane permeability of primary cultured rat hepatocytes treated with various hepatotoxins and its prevention by glycyrrhizin

1985

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Various hepatotoxins were added to the medium of primary cultures of adult rat hepatocytes and the release of the cytosolic enzymes lactic dehydrogenase, glutamic-oxaloacetic and glutamic-pyruvic aminotransferases were measured 24 h later. CCl4 at low concentrations caused dose-dependent release of soluble enzymes into medium without appreciable cytolysis of the hepatocytes. Mitochondrial enzymes were not released under these conditions. At 5 mM CCl4, both soluble and mitochondrial glutamic-oxaloacetic aminotransferase were found in the culture medium. Glycyrrhizin, a triterpenoid glycoside of licorice roots, prevented the enzyme release caused by CCl4.

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Section: Discussionmentioning

confidence: 99%

Enzyme leakage due to change of membrane permeability of primary cultured rat hepatocytes treated with various hepatotoxins and its prevention by glycyrrhizin

1985

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“…However, it is difficult to reconcile with this theory the protective effect exerted by AMP on human erythrocytes (21) and human lymphocytes (8). marked difference in the adenylate kinase ac tivities of the cells of the two species previously reported (20) was not confirmed, however.…”

Section: Discussionmentioning

confidence: 56%

“…Suggestions that the leakage of intracellular enzymes in pathological conditions is due, at least in part, to diminution of the energy content of the cells affected have been sup ported by studies on intact rat muscles (23), chicken muscle slices (5, 13), human erythro cytes (6,8,17,21), and rat lymphocytes (8,19,20). However, it is difficult to reconcile with this theory the protective effect exerted by AMP on human erythrocytes (21) and human lymphocytes (8).…”

Section: Discussionmentioning

confidence: 99%

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Action of Adenosine Phosphates on the Release of Intracellular Lactate Dehydrogenase from Human and Rat Lymphocytes

Gj¹,

Jh²

1977

Enzyme

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Differences in the action of adenosine phosphates on the release of intracellular enzymes from human and rat lymphocytes have been studied. The protective effect of ATP on the human cells was found to be less than on the rat cells. The greatest discrepancy was exhibited by AMP which exerted a protective effect on human lymphocytes, but increased enzyme efflux from rat lymphocytes. The activities of adenosine kinase, adenylate kinase, phosphoribosyl-pyrophosphate synthetase, pyruvate kinase, phosphoglycerate kinase and creatine kinase were compared in the cells of both species. Although significant differences were observed, they were too small to suggest the presence of a mechanism for the conversion of AMP into ATP in human lymphocytes not found in the rat cells. It seems therefore that the protective effect exerted by AMP on the human cells is not mediated by its conversion into ATP, and hence that some factor other than the intracellular energy content is concerned in controlling the release of intracellular enzymes from human cells.

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“…The lowering of the ATP concentration may lead to a disturbance in the integrity of the plasma membrane of brain cells, resulting in a leakage of intracellular substances in the extracellular fluid (cf. Weed et al (1969), Wilkinson et al Hallak &Wilkinson (1976)).…”

mentioning

confidence: 99%

Adenylate kinase activity in cerebrospinal fluid of schizophrenic and certain other psychiatric symptomatologies

Alm

Frithz

Ronquist

1979

Acta Psychiatr Scand

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Adenylate kinase activity in the cerebrospinal fluid (CSF) was investigated in 29 patients with psychiatric symptomatologies. Such activity was demonstrated in 18 of the 19 individuals with schizophrenic or other psychotic or borderline psychotic symptomatology. No activity was seen in the remaining 10 patients with non-psychotic nervous and/or functional somatic complaints, nor in the 20 persons whose CSF was examined in connection with spinal anaesthesia, nor in four who were treated with neuroleptic drugs on nonpsychiatric indications. The findings are compatible with the assumption that in persons with psychotic or borderline psychotic symptomatology a lowered membrane electrochemical potential may be associated with some of the symptoms exhibited.

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Action of metabolic inhibitors on the release of intra-cellular enzymes from human and rat lymphocytes and human erythrocytes

Cited by 12 publications

References 21 publications

Enzyme leakage due to change of membrane permeability of primary cultured rat hepatocytes treated with various hepatotoxins and its prevention by glycyrrhizin

Enzyme leakage due to change of membrane permeability of primary cultured rat hepatocytes treated with various hepatotoxins and its prevention by glycyrrhizin

Action of Adenosine Phosphates on the Release of Intracellular Lactate Dehydrogenase from Human and Rat Lymphocytes

Adenylate kinase activity in cerebrospinal fluid of schizophrenic and certain other psychiatric symptomatologies

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