scholarly journals Synthesis of ophthalmic acid in liver and kidney in vivo

1978 ◽  
Vol 170 (2) ◽  
pp. 415-419 ◽  
Author(s):  
M Orlowski ◽  
S Wilk
Keyword(s):  
Amino Acids ◽  
Mouse Liver ◽  
Significant Proportion ◽  
Rapid Synthesis ◽  
Gamma Glutamyl ◽  
Liver And Kidney ◽  
G 14

The synthesis of ophthalmic acid, an analogue of glutathione, was studied in vivo in mouse liver and kidney after administration of either L-alpha-aminobutyrate or L-gamma-glutamyl-L-alpha-aminobutyrate as precursor. L-alpha-aminobutyrate accumulated to a much greater extent, and induced a much greater synthesis of ophthalmic acid in the liver than in the kidney. In contrast, L-gamma-glutamyl-L-alpha-aminobutyrate initiated a large and more rapid synthesis of ophthalmic acid in the kidney than in the liver. Experiments with L-gamma-[G(-14)C]glutamyl-L-alpha-aminobutyrate showed that, although part of the dipeptide is degraded to its constituent amino acids, a significant proportion is directly incorporated into kidney ophthalmic acid. In contrast L-gamma-glutamyl-L-alpha-aminobutyrate serves poorly as a direct precursor of liver ophthalmic acid. The present results show that kidney gamma-glutamyl tripeptide synthesis can proceed directly from an exogenous gamma-glutamyl dipeptide precursor.

Organ-specific gene masking in mammalian chromosomes

1970 ◽  
Vol 176 (1044) ◽  
pp. 277-285 ◽  
Keyword(s):  
Cell Division ◽  
Dna Synthesis ◽  
Dna Hybridization ◽  
Mouse Liver ◽  
Early Event ◽  
Specific Gene ◽  
Histone Proteins ◽  
Organ Specific ◽  
Liver And Kidney

Chromatin (chromosomal nucleoprotein) from mammalian colls is used as a template for the synthesis of RNA which is characterized and compared with other RNA by RNA-DNA hybridization. It is found to be transcribed from a restricted set of sequences and cannot be distinguished from natural RNA from the same organ as the chromatin. In contrast, it is different from RNA from other organs. Hence, DNA is masked in an organ-specific way in vivo and the masking is preserved on isolation. When cell division is induced in mouse liver and kidney a very early event is a change in masking in chromatin. This precedes changes in RNA populations; both precede DNA synthesis. Chromatin can be accurately reconstructed from DNA, histones and non-histone proteins. Experiments using this system indicate that histones non-specifically mask DNA; non-histone proteins are essential to reverse masking in a specific way.

EFFECT OF LITHIUM ON DEIODINATING ACTIVITY OF VARIOUS RAT TISSUES IN VITRO

1974 ◽  
Vol 76 (2) ◽  
pp. 260-272 ◽  
Author(s):  
P. T. Männistö
Keyword(s):  
Amino Acids ◽  
Lithium Chloride ◽  
Half Life ◽  
Rat Tissues ◽  
Biological Half Life ◽  
Liver And Kidney ◽  
Licl Treatment

ABSTRACT The effect of lithium chloride (LiCl) on the deiodination of iodotyrosines, on the degradation of 125I-L-thyroxine (125I-L-T4) in vitro and on the disappearance of exogenous 125I-L4 and 125I-rat-TSH in vivo was studied in rats. Iodotyrosine deiodination was studied in vitro with three techniques. The whole thyroid lobes were not satisfactory as substrate. When a diluted mixture of prelabelled iodo-amino acids was used as substrate, thyroid homogenates deiodinated iodotyrosines. The reaction was inhibited by boiling and by 3,5-dinitro-L-tyrosine (DNT), but LiCl (2 × 10−2 m) had no effect. When 125I-3-iodo-L-tyrosine (125I-L-MIT) served as substrate, increasing concentrations of thyroid homogenates showed an increasing deicdinating activity, which was stimulated by NADP (1.5 × 10−4 m). Inhibitors of dehalogenase DNT (10−4 and 10 −3 m) and menandione (10−4 m) inhibited deiodination, but LiCl (5×10−3 − 0.1 m) was again without effect. The degradation of 125I-L-T4 by liver and kidney homogenates was inhibited by LiCl (5 × 10−3 − 0.1 m). The disappearance of 125I-L-T4 was studied in rats treated with LiCl for 1 – 4 or 60 – 64 days in vivo. The half-lives were as follows: at 1 –4 days, the control rats 15.9 ± 1.3 h and the LiCl treated rats 19.1 ± 2.1 h (P < 0.05) and at 60 – 64 days 11.2 ± 2.0 h and 66.8 ± 12.3 h (P < respectively. The prolonged half-life in the LiCl treated rats was not due to the decreased excretion of radioactivity in the urine or faeces. The biological half-life of 125I-rat-TSH (11.4 ± 3.2 min) was not modified by LiCl treatment for 5 days. It can be concluded that the antithyroid effect of LiCl neither originates from the inhibition of iodotyrosine deiodination nor from the change in the half-life of TSH. The half-life of thyroxine is prolonged by LiCl, an effect which is perhaps due to the decreased degradation of thyroxine by tissues.

In vivo antioxidative effect of isoquercitrin on cadmium-induced oxidative damage to mouse liver and kidney

2011 ◽  
Vol 383 (5) ◽  
pp. 437-445 ◽  
Author(s):  
Ruijin Li ◽  
Chao Yuan ◽  
Chuan Dong ◽  
Shaomin Shuang ◽  
Martin M. F. Choi
Keyword(s):  
Oxidative Damage ◽  
Mouse Liver ◽  
Antioxidative Effect ◽  
Liver And Kidney

scholarly journals In Vivo Toxicity, and Glutathione, Ascorbic Acid and Copper Level Changes Induced in Mouse Liver and Kidney by Copper(II) Gluconate, a Nutrient Supplement

2000 ◽  
Vol 120 (3) ◽  
pp. 311-314
Author(s):  
Yasuji HOJO ◽  
Ikuko HASHIMOTO ◽  
Yoko MIYAMOTO ◽  
Sadahiro KAWAZOE ◽  
Tamio MIZUTANI
Keyword(s):  
Ascorbic Acid ◽  
Mouse Liver ◽  
Copper Level ◽  
In Vivo Toxicity ◽  
Nutrient Supplement ◽  
Liver And Kidney

A Histopathological Evaluation of Amino Acids-Capped Silver Nanoconjugates (AgNCs) Against Cadmium-Induced Toxicity in Albino Mice

2021 ◽  
pp. 1-10
Author(s):  
Sarwar Allah Ditta ◽  
Atif Yaqub ◽  
Fouzia Tanvir ◽  
Rehan Ullah ◽  
Muhammad Rashid ◽  
...  
Keyword(s):  
Amino Acids ◽  
Serum Creatinine ◽  
Surface Chemistry ◽  
Histological Analysis ◽  
Cellular Structures ◽  
Control Group ◽  
Protective Effects ◽  
Histopathological Evaluation ◽  
Liver And Kidney

Various molecules may modify the surface chemistry of commonly used nanomaterials (NMs), resulting in the synthesis of novel and safer NMs. The current study was delineated to evaluate the in vivo toxicity profiling of the silver nanoconjugates (AgNCs) conjugated with different amino acids. The L-glycine capped-AgNCs exhibited toxicity and caused tissue damage, while L-cystine and L-tyrosine capped-AgNCs showed protective effects against cadmium-induced toxicity. L-cystine-capped-AgNCs performed well as compared to other amino acids-AgNCs. The level of serum creatinine, ALT, AST, ALP, and blood urea increased (p<0.05) in G2, G3, and G5 in comparison to G1 (control group). While an increase in bilirubin for G2 was statistically non-significant (p>0.05). The ALT and AST elevated (p<0.05) in G4, however, other serological parameters in G4 and G6 didn’t show any noticeable change in their values. Histological analysis showed disturbed and deformed cellular structures in liver and kidney tissues of G2, G3, and G5. However, G4 and G6 samples demonstrated minute changes in comparison to G1. It is concluded that L-cystine and L-tyrosine-capped-AgNCs exhibited protective effects and should be tested further for developing safer nanoconjugates for biomedical uses.

scholarly journals Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species

1978 ◽  
Vol 169 (1) ◽  
pp. 113-122 ◽  
Author(s):  
T Noguchi ◽  
E Okuno ◽  
Y Takada ◽  
Y Minatogawa ◽  
K Okai ◽  
...  
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Physical Properties ◽  
Mouse Liver ◽  
Mammalian Species ◽  
The Other ◽  
Enzyme Preparations ◽  
Amino Donor ◽  
Glyoxylate Aminotransferase

Mitochondrial extracts of dog, cat, rat and mouse liver contain two forms of alanine-glyoxylate aminotransferase (EC 2.6.1.44): one, designated isoenzyme 1, has mol.wt. approx. 80 000 and predominates in dog and cat liver; the other, designated isoenzyme 2, has mol.wt. approx. 175 000 and predominates in rat and mouse liver. In rat and mouse liver, isoenzyme 1 activity was increased by the injection in vivo of glucagon, but not isoenzyme 2 activity. Isoenzyme 1 was purified and characterized from liver mitochondrial extracts of the four species. Both rat and mouse enzyme preparations catalysed transamination between a number of L-amino acids and glyoxylate, and with L-alanine as amino donor the effective amino acceptors were glyoxylate, phenylpyruvate and hydroxypyruvate. In contrast, both dog and cat enzyme preparations were specific for L-alanine and L-serine with glyoxylate, and used glyoxylate and hydroxypyruvate as effective amino acceptors with L-alanine. Evidence that isoenzyme 1 is identical with serine-pyruvate aminotransferase (EC 2.6.1.51) was obtained. Isoenzyme 2 was partially purified from mitochondrial extracts of rat and mouse liver. Both enzyme preparations were specific for L-alanine and glyoxylate. On the basis of physical properties and substrate specificity, it was concluded that isoenzyme 2 is a separate enzyme. Some other properties of isoenzymes 1 and 2 are described.

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