THE EFFECTS OF X-IRRADIATION ON PROTEIN METABOLISM OF THE BRAIN

1965 ◽  
Vol 43 (7) ◽  
pp. 1091-1098 ◽  
Author(s):  
Shozo Nakazawa ◽  
Takao Hara ◽  
Komei Ueki
Keyword(s):  
Rat Brain ◽  
Protein Metabolism ◽  
Leucine Incorporation ◽  
Adult Rats ◽  
Rat Brain And Liver ◽  
Glucose Incorporation ◽  
X Irradiation ◽  
Total Body ◽  
The Brain

The effects of X-irradiation on the metabolism of rat brain, liver, and spleen have been studied. C14-Glucose incorporation into protein of the brain of newborn rats was affected significantly by total body X-irradiation (250 r each day for 4 days). C14-Leucine incorporation into protein of the brain, liver, and spleen of adult rats was also reduced by total body X-irradiation (300 r each day for 4 days).X-irradiation of the head (500 r each day for 6 days) affected C14-leucine incorporation into protein of rat brain and liver, but it did not affect that of spleen.X-irradiation in vitro (5000 r) did not have any effect on protein metabolism of rat brain. The mode of action of X-irradiation on protein metabolism is discussed.

Metabolic Studies on the Mechanisms of Increased Susceptibility of Weanling Rats to Parathion

1972 ◽  
Vol 50 (9) ◽  
pp. 902-915 ◽  
Author(s):  
Jacques Gagné ◽  
Jules Brodeur
Keyword(s):  
Toxic Effects ◽  
Intravenous Route ◽  
Toxic Metabolite ◽  
Adult Males ◽  
Adult Rats ◽  
Renal Handling ◽  
Weanling Rats ◽  
The Brain ◽  
Increased Susceptibility

Equitoxic doses of 32P-parathion (1.5 mg/kg in weanlings of both sexes, 2.0 mg/kg in adult females, and 3.1 mg/kg in adult males) were given by the intravenous route to immature and adult rats in order to investigate the respective contribution of biotransformation, distribution, and excretion phenomena to the increased susceptibility of weanling rats to the acute toxic effects of parathion. At various intervals, the animals were sacrified and the amounts of parathion, paraoxon, diethylphosphorothioic acid, and diethylphosphoric acid in the liver, kidneys, tibial muscle, plasma, brain, adipose tissue, and urine were determined. In vitro metabolism of 32P-parathion by liver homogenates was also investigated. The results obtained suggest that weanlings are more susceptible to parathion than adults mainly because of deficient hepatic mechanisms for degradation of parathion and its toxic metabolite, paraoxon. In addition, the brain tissue of weanlings appears to be more sensitive to the toxic effects of paraoxon than the brain of male adults. On the other hand, the passage of parathion and paraoxon across the blood–brain barrier does not seem to be facilitated in weanlings by comparison with adults. Finally, there is no evidence that the renal handling of parathion and its metabolites might influence the acute toxicity of parathion in weanling and adult rats.

Subcellular Distribution of DNA Polymerase Activity in Newborn Rat Brain and Liver

1971 ◽  
Vol 49 (12) ◽  
pp. 1285-1291 ◽  
Author(s):  
M. R. V. Murthy ◽  
A. D. Bharucha
Keyword(s):  
Enzyme Activity ◽  
Rat Brain ◽  
Dna Polymerase ◽  
Subcellular Fraction ◽  
Polymerase Activity ◽  
Particulate Material ◽  
Newborn Rat ◽  
Newborn Brain ◽  
Rat Brain And Liver ◽  
The Brain

DNA polymerase activities were determined in the cytoplasmic soluble, the nuclear soluble, and the nuclear particulate fractions of newborn rat brain and liver. The results indicate that a majority of the brain nuclear enzyme may be bound to particulate material while a majority of the liver nuclear enzyme may be free or only loosely bound. Although the subcellular distributions of DNA polymerase activity are widely different in newborn brain and liver, the enzyme activity in any given subcellular fraction is higher in liver than in brain.

scholarly journals Functional expression of mammalian glucose transporters in Xenopus laevis oocytes: evidence for cell-dependent insulin sensitivity.

1989 ◽  
Vol 9 (10) ◽  
pp. 4187-4195 ◽  
Author(s):  
J C Vera ◽  
O M Rosen
Keyword(s):  
Glucose Uptake ◽  
Rat Brain ◽  
Xenopus Oocytes ◽  
Glucose Transporter ◽  
Glucose Transporters ◽  
Functional Expression ◽  
Xenopus Laevis Oocytes ◽  
Rat Brain And Liver ◽  
Insulin Responsiveness

We report the functional expression of two different mammalian facilitative glucose transporters in Xenopus oocytes. The RNAs encoding the rat brain and liver glucose transporters were transcribed in vitro and microinjected into Xenopus oocytes. Microinjected cells showed a marked increase in 2-deoxy-D-glucose uptake as compared with controls injected with water. 2-Deoxy-D-glucose uptake increased during the 5 days after microinjection of the RNAs, and the microinjected RNAs were stable for at least 3 days. The expression of functional glucose transporters was dependent on the amount of RNA injected. The oocyte-expressed transporters could be immunoprecipitated with anti-brain and anti-liver glucose transporter-specific antibodies. Uninjected oocytes expressed an endogenous transporter that appeared to be stereospecific and inhibitable by cytochalasin B. This transporter was kinetically and immunologically distinguishable from both rat brain and liver glucose transporters. The uniqueness of this transporter was confirmed by Northern (RNA) blot analysis. The endogenous oocyte transporter was responsive to insulin and to insulinlike growth factor I. Most interestingly, both the rat brain and liver glucose transporters, which were not insulin sensitive in the tissues from which they were cloned, responded to insulin in the oocyte similarly to the endogenous oocyte transporter. These data suggest that the insulin responsiveness of a given glucose transporter depends on the type of cell in which the protein is expressed. The expression of hexose transporters in the microinjected oocytes may help to identify tissue-specific molecules involved in hormonal alterations in hexose transport activity.

scholarly journals Regional Brain Blood Flow, Blood Volume, and Haematocrit Values in the Adult Rat

1983 ◽  
Vol 3 (2) ◽  
pp. 254-256 ◽  
Author(s):  
Jill E. Cremer ◽  
Malcolm P. Seville
Keyword(s):  
Blood Flow ◽  
Blood Volume ◽  
Brain Regions ◽  
Adult Rats ◽  
Adult Rat ◽  
Systemic Artery ◽  
Significant Difference ◽  
Total Body ◽  
The Brain ◽  
Made In

Measurements of red cell volume, plasma volume, and tissue haematocrit (Hct) were made in 14 brain regions in adult rats using 51Cr-tagged red cells and 125I-labeled human serum albumin. The mean large vessel (systemic artery) Hct was 41.8, total body Hct was 35.3, and of the brain regions, the lowest value (septal nucleus) was 25.91 and the highest (visual cortex) was 32.05. The lowest blood volume was 6.29 μl g−1 (caudate putamen) and the highest was 14.44 μl g−1 (inferior colliculus). There was a significant difference between regions in both blood volume and tissue blood Hct. When brain regions were ranked in order of blood volume, this did not coincide with the order for blood flow.

1,4 Butanediol and ethanol compete for degradation in rat brain and liver in vitro

Alcohol ◽  
1986 ◽  
Vol 3 (6) ◽  
pp. 367-370 ◽  
Author(s):  
Flavio Poldrugo ◽  
O.Carter Snead
Keyword(s):  
Rat Brain ◽  
Rat Brain And Liver

scholarly journals Brain Levels of Catalase Remain Constant through Strain, Developmental, and Chronic Alcohol Challenges

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Dennis E. Rhoads ◽  
Cherly Contreras ◽  
Salma Fathalla
Keyword(s):  
Rat Brain ◽  
Catalase Activity ◽  
Developmental Stages ◽  
Ethanol Consumption ◽  
Chronic Alcohol ◽  
Sprague Dawley ◽  
Adult Rats ◽  
Adult Level ◽  
Long Evans ◽  
The Brain

Catalase (EC 1.11.1.6) oxidizes ethanol to acetaldehyde within the brain and variations in catalase activity may underlie some consequences of ethanol consumption. The goals of this study were to measure catalase activity in subcellular fractions from rat brain and to compare the levels of this enzyme in several important settings. In the first series of studies, levels of catalase were compared between juvenile and adult rats and between the Long-Evans (LE) and Sprague-Dawley (SD) strains. Levels of catalase appear to have achieved the adult level by the preadolescent period defined by postnatal age (P, days) P25–P28, and there were no differences between strains at the developmental stages tested. Thus, variation in catalase activity is unlikely to be responsible for differences in how adolescent and adult rats respond to ethanol. In the second series of studies, periadolescent and adult rats were administered ethanol chronically through an ethanol-containing liquid diet. Diet consumption and blood ethanol concentrations were significantly higher for periadolescent rats. Catalase activities remained unchanged following ethanol consumption, with no significant differences within or between strains. Thus, the brain showed no apparent adaptive changes in levels of catalase, even when faced with the high levels of ethanol consumption characteristic of periadolescent rats.

Immunochemical and Biochemical Evidence for Expression of Phenobarbital-and 3-Methylcholanthrene-Inducible Isoenzymes of Cytochrome P450 in Rat Brain

1998 ◽  
Vol 17 (6) ◽  
pp. 619-630 ◽  
Author(s):  
Devendra Parmar ◽  
Alok Dhawan ◽  
Monika Dayal ◽  
Prahlad K. Seth
Keyword(s):  
Cytochrome P450 ◽  
Rat Brain ◽  
Western Blotting ◽  
Polyclonal Antibodies ◽  
Biochemical Evidence ◽  
Catalytic Activities ◽  
Brain Microsomes ◽  
The Brain

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.

Sign in / Sign up

Export Citation Format

Share Document