Chlorpromazine and other psychoactive drug induced alterations of a membrane bound enzyme in rat brain

1994 ◽  
Vol 14 (3) ◽  
pp. 139-144
Author(s):  
Maitreyi Nag ◽  
Namita Nandi
Keyword(s):  
Alkaline Phosphatase ◽  
Rat Brain ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Drug Induced ◽  
Effective Inhibition ◽  
Membrane Bound ◽  
The Individual ◽  
Membrane Bound Enzymes ◽  
Combined Drugs

Psychoactive drugs like chlorpromazine (CPZ), imipramine, lithium and amphetamine in one way or another affect behaviour. The drug responses are presumably mediated by inducing a change in the activity of membrane bound enzymes. CPZ is very potent in inhibiting the alkaline phosphatase activity in rat brain. The combined effect of CPZ with other drugs shows that CPZ and imipramine together inhibit the enzyme activity significantly greater than the individual inhibition either by CPZ or by imipramine alone. Effective inhibition of the alkaline phosphatase activity with a single drug or combined drugs may lead to a change in neuronal permeability through glucocorticoids thereby affecting mood.

scholarly journals Behaviour and Properties of Membrane-Bound Mouse Uterine Alkaline Phosphatase During Early Pregnancy

1980 ◽  
Vol 33 (5) ◽  
pp. 539 ◽  
Author(s):  
Louise E Buxton ◽  
RN Murdoch
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Early Pregnancy ◽  
Particulate Material ◽  
Mouse Uterus ◽  
Membrane Bound

Most of the alkaline phosphatase activity in the mouse uterus during early pregnancy was found to be membrane-bound and was associated with particulate material when homogenates were centrifuged at 105000 g. The activity of the enzyme increased in both the particulate and cytosol fractions of uterine homogenates during early pregnancy to reach maximum values on day 7 of pregnancy.

Acetaminophen: fatty enhanced toxicity

1986 ◽  
Vol 44 ◽  
pp. 332-333
Author(s):  
S.S. Poolsawat ◽  
C.A. Huerta ◽  
G.A. Miranda ◽  
L.T. Nguyen
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Prescription Drugs ◽  
Alkaline Phosphatase Activity ◽  
Secretory Granules ◽  
Food Additives ◽  
Hepatic Necrosis ◽  
Drug Induced ◽  
Elevated Alkaline Phosphatase ◽  
Cacodylate Buffer

Drug toxicity accounts for 10%-30% of all medical in-patients admissions; some of the drug induced illnesses often occur following hospitalization. 5%-6% of medical in-patients deaths are initiated or induced by drug intake (1-4); about one-third of these cases are caused by non-prescription drugs. Acetaminophen, considered among the safest of all over-the-counter analgesics, has been reported to induce fatal hepatic necrosis both in man and animals (5-8). Frequently, adverse drug reactions arise from hypersensitivity to a drug and its side effects, or to drug interactions with food and food additives. This study is undertaken to observe the effect of acetaminophen on the liver when a fatty diet is simultaneously administered.Swiss Webster mice were individually gavaged with a 286 mg/Kg dosis of acetaminophen for 4 days; control animals received saline alone. Both groups received rat feed plus 20% fat and were euthanized on the 5th day. Liver tissues were either fixed in 2% gluteraldehyde; post-fixed in 1% osmnium tetroxide in 0.1M sodium cacodylate buffer and embedded in Araldite 502 for TEM; or processed for alkaline phosphatase activity (9).Hepatocyte derived from mice exposed to acetaminophen (Fig. 1) showed increased Golgi Apparatus (GA) and secretory granules (SG) activity. These phenomena appear to be responsible for the elevated alkaline phosphatase activity (Fig. 2) in response to acetaminophen detoxification exerted by the hepatocyte. However, when a fatty diet is incorporated into the study: the hepatocyte exhibited generalized cytoplasmic lysis and increased lipid droplets (Fig. 3), localized coagulative necrosis of the hepatocyte normally found in the caudal and right lobes of the liver (Fig. 4) and increased pynotic hepatocytes (Fig. 5) are noted

Activation and inhibition of the brush-border membrane-bound alkaline phosphatase activity of Hymenolepis diminuta (Cestoda) by divalent cations

Parasitology ◽  
1991 ◽  
Vol 102 (1) ◽  
pp. 141-145 ◽  
Author(s):  
P. W. Pappas
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Brush Border ◽  
Divalent Cations ◽  
Hymenolepis Diminuta ◽  
Tetraacetic Acid ◽  
Low Concentrations ◽  
Membrane Bound ◽  
High Concentrations

SUMMARYIn the absence of exogenous divalent cations, the isolated brush-border plasma membrane of Hymenolepis diminuta possesses alkaline phosphatase activity (APA). APA is stimulated in the presence of exogenous Mg2+ and inhibited by low concentrations of Zn2+ or high concentrations of Ca2+, and inhibition of APA by Zn2+ is reversed by both Mg2+ and Ca2+. APA is inhibited by ethylenediamine tetraacetic acid (EDTA), ethyleneglycol-bis-(β-aminoethyl ether) N, N′-tetraacetic acid, and 1, 10-phenanthroline in time- and concentration-dependent fashions, with EDTA being the most effective inhibitor. Following treatment with EDTA, APA is restored by Mg2+ and, to a lesser extent, by Ca2+, but not by Zn2+. Thus, APA represents a Mg2+-dependent enzyme that can be partly activated by Ca2+ but only in the absence of Mg2+.

Studies on the unmasking of membrane-bound alkaline phosphatase during the differentiation of Dictyostelium discoideum

1984 ◽  
Vol 62 (10) ◽  
pp. 970-974 ◽  
Author(s):  
D. V. Mohan Das ◽  
Gerald Weeks
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Dictyostelium Discoideum ◽  
Alkaline Phosphatase Activity ◽  
Developmental Regulation ◽  
Nucleotidase Activity ◽  
Nitrophenyl Phosphate ◽  
Single Protein ◽  
Membrane Bound ◽  
Triton X

Evidence has been presented recently to suggest that the 5′-nucleotidase and alkaline phosphatase activities of culmination phase cells of Dictyostelium discoideum are due to a single protein. However, we find that the membrane bound 5′-nucleotidase activity is only marginally activated by either 50 °C treatment or by dialysis, conditions that markedly activate alkaline phosphatase activity. In contrast, the 5′-nucleotidase activity of Triton X-100 extracts is activated by dialysis to the same extent as alkaline phosphatase activity. The available evidence suggests that, although a single protein is responsible for both alkaline phosphatase and 5′-nucleotidase activities, the characteristics of binding of the two substrates p-nitrophenyl phosphate and AMP to this enzyme are somewhat different. The alkaline phosphatase activity of dialyzed vegetative cell membranes is inhibited by the addition of concentrated dialyzate and this inhibition is reversed by further dialysis. The culmination phase enzyme is also inhibited by concentrated dialyzate from vegetative cells, suggesting that the removal of inhibitor from the enzyme can completely account for the developmental regulation. Dialyzates from culmination phase membranes do not inhibit enzyme activity, indicating the absence of inhibitor in these preparations. Alkaline phosphatase and 5′-nucleotidase activities of a partially purified enzyme preparation are equally inhibited by the addition of the concentrated dialyzate.

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