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Biomedical subjects

V V Reddy

Publications and source records attributed to V V Reddy.

At least 55 records · Page 3Linked to original sources
PubMed1982

Estrogen effects on NADH oxidase and superoxide dismutase i prepubertal female rats.

Thirty-four day old, ovariectomised rats were treated with increasing doses of estradiol, 2-hydroxyestradiol 2,3-dimethyl ether (23E2), 4-hydroxyestradiol 3,4-dimethyl ether (34E2) and 4-methoxyestradiol (4ME2) for five days by subcutaneous injection. Superoxide dismutase, phenol activated NADH oxidase and uterine dry weights were determined. Only estradiol was found to be uterotrophic and increased NADH oxidase activity in these experiments. Both 23E2 and 34E2 treatment reduced the enzyme activity significantly. Though 4ME2 showed a decrease in NADH oxidase at 0.05 micrograms/100 gm body weight there was no further decrease at higher dose (5 micrograms/100 gm). The superoxide dismutase (SOD) in uterus and liver was unaffected by estradiol, while 23E2, 34E2, and 4ME2 significantly reduced SOD in both liver and uterus. These results indicate that 23E2, 34E2 and 4ME2, in spite of their nonuterotrophic property property, affect uterine metabolism. Furthermore, in view of the reports indicating the importance of SOD levels in various tumors and since catecholestrogens are observed to reduce SOD levels in liver and uterus, it is suggestive that catecholestrogens may play an important role in the pathophysiology of certain tumors.

Animals↗
PubMed1981

Synthesis of catechol estrogens by human uterus and leiomyoma.

Homogenates of human endometrial, myometrial and leiomyoma tissues were incubated with (2,4,6,7-3H)-estradiol and tritiated catechol estrogens were isolated and identified. Though 2- and 4-hydroxylations were about the same in endometrium, 4-hydroxylation was two to four fold higher than 2-hydroxylation in myometrium and leiomyoma. However, endometrium showed greater capacity to form both 2- and 4-hydroxyestrogens than the other two tissues. Both 2- and 4-hydroxylations were significantly less than in myometrium. In view of the reports indicating that inhibitors of catechol 0-methyl transferase (COMT) might act as antineoplastic agents due to their interference with t-RNA methylases and since catechol estrogens inhibit COMT, the present results suggest that endogenous synthesis of catechol estrogens may play an important role in the pathophysiology of uterine leiomyoma.

Aryl Hydrocarbon Hydroxylases↗
PubMed1981

Oestrogen metabolism in adult rat's brain.

In vitro incubation of pituitary, hypothalamus and cerebral cortex with [3H]oestrogens revealed that the oestrogens are actively metabolized by these tissues. The covalent binding of oestrone and oestradiol to acid precipitable proteins was observed. Pituitary from male rats exhibited higher covalent binding of oestrogens than females. The 2-hydroxylation was found to be greater than 16-hydroxylation. Furthermore, male pituitary exhibited higher 2-hydroxylation of oestrogens than females. No such sexual dimorphism was observed in 16-hydroxylation. C17-reduction was found to be greater than oxidation in these tissues. Furthermore, the C17-reduction in pituitary and hypothalamus from females was greater than males, which is in contradistinction to protein binding and 2-hydroxylation of oestrogens. In both male and female animals the pituitary was metabolically more active than hypothalamus and cortex. In addition, oestradiol was hydroxylated more than oestrone either at 2- or 16-positions. These results indicate that in central nervous system and pituitary the oestrogens are metabolized preferentially by 2-hydroxylation pathway and it is suggested that the in situ metabolism of oestrogens in neuroendocrine tissues may be important in the control of oestrogen effects on neuroendocrine function and sex behaviour.

Age Factors↗
PubMed1980

Estrogen metabolism in neural tissues of six-day-old rats.

In vitro incubation of pituitary, hypothalamus and cerebral cortex from 6-day-old rats with [6,7-3H]estradiol revealed that estradiol is actively metabolized in these tissues. Pituitary was found to be more active than hypothalamus and cerebral cortex in metabolizing estradiol in these animals. Covalent binding of estradiol to acid-precipitable proteins was observed in all these tissues from both sexes. While there was no significant sex difference in protein binding of estradiol in any of the tissues tested, treatment with progesterone or estradiol valerate increased protein binding. 2- and 16-hydroxylation and 17 beta-oxidation were demonstrated in all the tissues tested. While there were no significant sex differences observed in 2,16-hydroxylation, 17 beta-oxidation appeared to be more in males. Progesterone treatment of males increased 2-hydroxylation of estradiol 4-fold in pituitary and doubled the levels in hypothalamus. 16-Hydroxylation and 17-oxidation were also elevated significantly in pituitary and hypothalamus by progesterone treatment. Estradiol valerate treatment, however, decreased 2-hydroxylation and 16-hydroxylation in pituitary and hypothalamus; 17-oxidation was increased in pituitary. These results suggest that the estradiol metabolism, and especially 2-hydroxyestradiol formation, can be increased by progesterone and thereby mediate antagonistic effect of progesterone on estrogen-mediated brain sexual differentiation.

Animals↗
PubMed1979

delta 4-3-Ketosteroid 5 alpha-oxidoreductase in human uterine leiomyoma.

Homogenates of human endometrial, myometrial, and leiomyoma tissues were incubated with (1,2,6,7-3H)-testosterone, and 3H-dihydrotestosterone was subsequently identified, indicating the presence of the enzyme delta 4-3-Ketosteroid 5 alpha-oxidoreductase. The enzyme activity of leiomyoma was higher than that of endometrial and myometrial tissue, while endometrial activity was higher than myometrial activity. The results raise the possibility that 5 alpha-reduced androgens may play a role in the pathophysiology of uterine leiomyoma.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMed1979

Estrogen metabolism in neural tissues of rabbits: 17 beta - hydroxysteroid oxidoreductase activity.

Incubation of adult rabbit neural tissue homogenates with (3H)-estrone and (3H)-estradiol revealed that the conversion of estrone to estradiol is higher in both male and female animals than estradiol to estrone. Both 17 oxidation and reduction are higher in male animals than in females. However, it is observed that the quotient of estrone leads to estradiol/estradiol leads to estrone for pituitary tissue and hypothalamus are higher in females than in males. There is no such dimorphism in cerebral cortex. The overall metabolism in pituitary is higher than in hypothalamus and cortex in both sexes. These results suggest that 17 beta hydroxysteroid oxidoreductase activity may play an important role in the regulation of estrogen function in neuroendocrine tissues.

17-Hydroxysteroid Dehydrogenases↗
PubMed1978

Reduction of testosterone to 5 alpha-dihydrotestosterone by human and rat uterine tissues.

Incubations of adult rat uterine tissue and human endometrial and myometrial homogenates with [1,2,6,7-3H]testosterone resulted in the formation of 5 alpha-[3H]dihydrotestosterone. The rat uterine homogenates showed higher activity than the minced tissue. The activity in human tissue was found to be less than rat tissue on a per unit weight basis. The human endometrium has been found to possess significantly higher activity than myometrium. These results support the hypothesis that androgens may exert their effect on uterus via 5 alpha-reduced metabolites.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗
PubMed1977

Mechanism of C-5 double bond introduction in the biosynthesis of cholesterol by rat liver microsomes.

The dehydrogenation reaction of cholest-7-en-3beta-ol (I) to cholesta-5,7-dien-3beta-ol (II) in the presence of NADH was studied in rat liver microsomes and in microsomal acetone powder preparations, using [3alpha-3H]cholest-7-en-3beta-ol. It was found that the reaction was inhibited by menadione, adenosine diphosphate, potassium ferricyanide, and cytochrome c while p-cresol had no effect. These results indicated the participation of a microsomal electron transport system in the dehydrogenation of cholest-7-en-3beta-ol. The conversion of cholest-7-en-3beta-ol to cholesta-5,7-dien-3beta-ol was also observed in the absence of NADH when ascorbic acid was included in the incubation mixture. However, the ascorbic acid-catalyzed dehydrogenation was not inhibited by potassium ferricyanide. Immunological evidence that microsomal cytochrome b5 is involved in the dehydrogenation of (I) to (II) was obtained. Antibodies specific for rat liver microsomal cytochrome b5 were elicited in rabbits. The anticytochrome b5 immunoglobulin fraction inhibited rat liver microsomal NADH-cytochrome c reductase but not NADPH-cytochrome c reductase. Also, the extent of reduction of cytochrome b5 was not affected by the antibodies. The conversion of (I) to (II) by rat liver microsomes was inhibited (73%) by anticytochrome b5 immunoglobulin at a ratio of microsomal protein:immunoglobulin of 1:5.6. These results are consistent with the participation of microsomal cytochrome b5 in the introduction of the C-5 double bond in cholesterol biosynthesis. A close analogy of the microsomal dehydrogenation of fatty acids and of cholest-7-en-3beta-ol is apparent and this suggests a possible similarity in the mechanisms of the two reactions.

Adenosine Diphosphate↗