In Vitro Interaction of Heavy Metals with Ouabain Receptors in Rat Brain Microsomes

1993 ◽  
Vol 16 (1) ◽  
pp. 101-110 ◽  
Author(s):  
C. S. Chetty ◽  
T. C. Stewart ◽  
A. Cooper ◽  
B. Rajanna ◽  
S. Rajanna
Peptides ◽  
1986 ◽  
Vol 7 (3) ◽  
pp. 425-429 ◽  
Author(s):  
Jeroen A.D.M. Tonnaer ◽  
Marianna Van Vugt ◽  
Joop S. De Graaf

1998 ◽  
Vol 17 (6) ◽  
pp. 619-630 ◽  
Author(s):  
Devendra Parmar ◽  
Alok Dhawan ◽  
Monika Dayal ◽  
Prahlad K. Seth

Expression of P450 1A1l 1A2 and 2 B1l 2B2 isoenzymes in rat brain was studied by Western blotting, using polyclonal antibodies raised against hepatic P450 1A1l 1A2 and 2B1l 2B2 isoenzymes. In addition, biochemical characterizations of the catalytic activities, pen toxyresorufin O-dealkylation (PROD) and ethoxyre-sorufin O-deethylation (EROD), selective for P450 2B1l 2B2 (PROD) and P450 1A1l 1A2 (EROD), were performed with rat brain microsomes. Control rat brain microsomes did not crossreact with either of the antibodies, whereas microsomes obtained from 3-methylcholanthrene (MC)-pretreated rats revealed significant immunoreactivity with anti-P450 1A1l 1A2. Similar results were observed with phenobarbital (PB)-pretreated rats, with the brain microsomes exhibiting significant immunoreactivity with anti-P450 2B1l 2B2. The induction in the P450 isoenzymes after PB or MC pretreatment was much less in the brain in comparison to the liver. Enzymatic studies indicated that the activities of PROD and EROD were induced in brain 3—4 fold by PB and MC pretreatment, respectively, and were almost completely inhibited on in vitro addition of anti-P450 2B1l 2B2 and 1A1l 1A2. These data demonstrate the expression of P4501A1l 1A2 and 2B1l 2B2 isoenzymes in the brain and indicate that, as in liver, these isoenzymes catalyze EROD and PROD, respectively, in the rat brain.


2015 ◽  
Vol 8 (3) ◽  
pp. 139-145 ◽  
Author(s):  
Ayodele J. Akinyemi ◽  
Ganiyu Oboh ◽  
Adedayo O. Ademiluyi

Abstract Evidence has shown that ingestion of heavy metals can lead to neurodegenerative diseases. This study aimed to investigate the neurotoxic potential of salt substitutes (Obu-Otoyo); salt A (made by burning palm kernel shaft then soaked in water overnight and the extract from the resulting residue is used as the salt substitute) and salt B (an unrefined salt mined from a local site at Ilobu town, Osun-State, Nigeria) by assessing their effect on some key enzymes linked with neurodegenerative disease [acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activities] as well as on malondialdehyde (MDA) content of the rat brain. Salt substitutes were fed to normal rats as dietary inclusion at doses of 0.5 and 1.0% for 30 days. Thereafter, the effect of the salt substitutes on AChE and BChE activities as well as on MDA level in the rat brain was determined. The results revealed that the salt substitutes caused a significant (p<0.05) increase in both AChE and BChE activity and also induced lipid peroxidation in the brain of rats in vivo as well as under in vitro condition in a dose-dependent manner. The effect of the salt substitutes on AChE and BChE activities could be attributed to the presence of some toxic heavy metals. Therefore, the ability of the salt substitutes to induce lipid peroxidation and activate AChE and BChE activities could provide some possible mechanism for their neurotoxic effect.


Life Sciences ◽  
1984 ◽  
Vol 35 (4) ◽  
pp. 365-371 ◽  
Author(s):  
D. Barone ◽  
G. Colombo ◽  
A. Glasser ◽  
F. Luzzani ◽  
T. Mennini

1972 ◽  
Vol 50 (11) ◽  
pp. 1080-1085 ◽  
Author(s):  
S. P. Bhatnagar

The effect of chlorpromazine, amitryptyline, amphetamine, diphenhydramine, and iproniazid on the in vitro oxidation of dopamine to melanin by rat brain mitochondrial preparation was investigated. Chlorpromazine and amitryptyline very markedly inhibited the oxidation (ED50 60 and 180 μM, respectively) while iproniazid was ineffective. Other drugs were moderately active. The reaction was enzyme catalyzed and could not be ascribed to the anionic component. Chronic administration of chlorpromazine and amitryptyline (19 and 9.5 mg/kg, i.p.) produced a biphasic response characterized by stimulation of melanogenesis during the first 2–3 weeks followed by inhibition. On the other hand, physostigmine and choline markedly stimulated the oxidation process. The chronic ingestion of heavy metals; mercury, lead, and cadmium, up to toxic levels had no effect on the in vitro oxidation of dopamine.


1974 ◽  
Vol 71 (1) ◽  
pp. 183-186
Author(s):  
M. Gary Hadfield ◽  
James E. Bosworth

2012 ◽  
Vol 518 (2) ◽  
pp. 101-105 ◽  
Author(s):  
Cesare Mancuso ◽  
Eugenio Barone ◽  
Pina Guido ◽  
Fiorella Miceli ◽  
Fabio Di Domenico ◽  
...  

Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.


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