Protein and enzyme release from human leukocytes: Influence of phenothiazine derivatives

Lahrichi, M.; Houpert, Y; Tarallo, P; Loppinet, V.; Siest, Gérard

doi:10.1016/0009-2797(77)90029-1

Cited by 14 publications

(3 citation statements)

References 23 publications

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“…Fluidity changes could stem from the perturbation of the interactions between the main membrane components: proteins, phospholipids, cholesterol, and even calcium ions. CPZ is known to bind to proteins (Chatelain et al, 1979; Leterrier et al, 1976; Testylier & Leterrier, 1980) and even to release them from some membranes (Leterrier et al, 1974;Ogiso et al, 1977;Lahrichi et al, 1977), and proteins are recognized as important modulators of the membrane fluidity (Cornell et al, 1978;Owicki & McConnell, 1979;Heyn et al, 1981). CPZ interacts also with phospholipids, sometimes increasing (Breton et al, 1977;Jones & Woodbury, 1978) and sometimes decreasing (Chatelain et al, 1979;Lee, 1977) order and internal microviscosity.…”

Section: Discussionmentioning

confidence: 99%

Modulation of adenylate cyclase activity by the physical state of pigeon erythrocyte membrane: 1. Parallel drug-induced changes in the bilayer fluidity and adenylate cyclase activity

Salesse¹,

Garnier²,

Leterrier³

et al. 1982

Biochemistry

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The fluorescence anisotropy probe perylene and the spin-labels 5-doxylsterate and 16-doxylstearate were used to estimate the order and internal microviscosity of the pigeon erythrocyte membrane upon perturbation by cationic or neutral amphipathic drugs (chlorpromazine, methochlorpromazine, tetracaine, and octanol) and an anionic drug, octanoic acid. Both methods gave identical results. The fluidity changes were found to strictly correlate with those of adenylate cyclase activity in the presence of GTP when perturbed by the drugs [Salesse, R., & Garnier, J. (1979) Biochim. Biophys. Acta 554, 102-113]. The cationic or neutral drugs, in an intermediate range of concentration, decreased the degree of organization and the internal microviscosity of the lipids together with the activity of the adenylate cyclase. At a higher concentration they reincreased them up to or higher than their initial level before the final destruction of the membrane structure and functions. This concentration effect was time dependent with tetracaine. The quaternary amine methochlorpromazine acted as chlorpromazine only on open ghosts. On intact cells, it inhibited catecholamine receptors at higher concentration and monotonously decreased the order and microviscosity, as the anionic amphipath octanoic acid did. This is taken as evidence that the inner leaflet of the bilayer is the seat for the observed multiphasic changes of viscosity and the control of adenylate cyclase and catecholamine receptors. This could stem from either a preferential intercalation or a surface effect of the amphipaths in the inner leaflet of the membrane. Since the basal activity of adenylate cyclase was not affected in the presence of drugs, it may be inferred that the enzyme holds its activity but that its stimulation is modulated by the membrane physical state.

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Section: Discussionmentioning

confidence: 99%

Modulation of adenylate cyclase activity by the physical state of pigeon erythrocyte membrane: 1. Parallel drug-induced changes in the bilayer fluidity and adenylate cyclase activity

Salesse¹,

Garnier²,

Leterrier³

et al. 1982

Biochemistry

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“…It has been shown that the primary site of chlorpromazine action is the cellular membrane (Lahrichi, Houpert, Tarallo, Loppinet and Siest 1977) . It inhibits ATPase and glyceraldehyde phosphate dehydrogenase (Squires 1965, Lahrichi et al 1977.…”

Section: Discussionmentioning

confidence: 99%

“…It inhibits ATPase and glyceraldehyde phosphate dehydrogenase (Squires 1965, Lahrichi et al 1977. The sulphhydryl groups of these enzymes have been shown to be implicated in the chlorpromazine action (Squires 1965).…”

Section: Discussionmentioning

confidence: 99%

Hypoxic Cytotoxicity of Chlorpromazine and the Modification of Radiation Response inE. ColiB/r

Shenoy

Singh

1978

International Journal of Radiation Biology and Related Studies

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Lactate dehydrogenase and cell injury

Danpure

1984

Cell Biochemistry & Function

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Serum total and isoenzyme lactate dehydrogenase activity in American Burkitt's lymphoma patients. Am. J. Clin. PathoI. 78, 712-717 88 Brereton, H. D., Simon, R. and Pomeroy, T. C. (1975) Pre-treatment serum lactic dehydrogenase predicting metastatic spread in Ewing's sarcoma. Ann. Intern. Med. 83, 352-354 89 Fritsche, H. A.. Trujillo, J. M. and Samuels, M. L. (1982) Serum lactate dehydrogenase isoenzyme-l in patients with advanced testicular cancer. Am. J. Clin. PathoI. 78, 178-183 90 Paloheimo, J. A. and Ikkala, E. (1965) Serum lactic dehydrogenase activity and isoenzyme patterns in some haematological disease. Correlation of serum lactic dehydrogenase activity with the clinical status of patients with cancer, lymphoma and the leukaemias. Cancer Res. 17,660-667 92 Usher, D. J., Shepherd, R. J. and Deegan. T. (1974) Serum lactate dehydrogenase isoenzyme activity in patients with asthma. Thorax 29,685-689 93 Kalk, H., Schmidt, E., Schmidt, F. W. and Wildhirt, E. (1960) Zur beteilung der leber bei der infektiosen mononucleose. KIin. Wochenschr. 38, 421428 94 Olislaegers, P., Van Caillie, B., Wils, P.(1981) High values for lactate dehydrogenase in measles. Clin. Chem. 27, 641 95 West, M. and Zimmerman, H. J. (1958) Serum enzymes in disease IV Lactic dehydrogenase and glutamic oxaloacetic transaminase levels in renal diseases. J. Lab. CIin. Med. 52, 185192 96 Bridman, D. R., Lackner, H., Berczeller, P. and Silber, R. (1981) The diagnostic value of the serum lactic dehydrogenase determination in the evaluation of unexplained thrombocytosis. Am. J. Clin. Pathol. 75, 840-843 McLean. D., Murison, J. and Griffiths, P. D. (1974) Serum enzyme activities in accidental hypothermia and hypothermic myxoedema. C h . Chim. Acta 52, 197-201 98 Feldman. W. F. (1975) Cerebrospinal fluid lactate dehydrogenase activity. Am. J. Dis. Child 129, 77-80 99 Knight, J. A., Dudek, S. M. and Haymond, R. E. (1981) Early (chemical) diagnosis of bacterial meningitiscerebrospinal fluid 91 97 100 101 102 103 104 105 106 107 108glucose, lactate and lactate dehydrogenase compared. Clin. Chem.

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Protein and enzyme release from human leukocytes: Influence of phenothiazine derivatives

Cited by 14 publications

References 23 publications

Modulation of adenylate cyclase activity by the physical state of pigeon erythrocyte membrane: 1. Parallel drug-induced changes in the bilayer fluidity and adenylate cyclase activity

Modulation of adenylate cyclase activity by the physical state of pigeon erythrocyte membrane: 1. Parallel drug-induced changes in the bilayer fluidity and adenylate cyclase activity

Hypoxic Cytotoxicity of Chlorpromazine and the Modification of Radiation Response inE. ColiB/r

Lactate dehydrogenase and cell injury

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