Genetic control of glucuronidase induction in mice

Swank, Richard T.; Paigen, Kenneth; Ganschow, Roger E.

doi:10.1016/0022-2836(73)90191-5

Cited by 160 publications

(61 citation statements)

References 31 publications

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“…For example, androgens induce activities of both arginase [237][238][239] and ODC [239][240][241] in kidneys of female or castrated male mice. Hypertrophy generally occurs under these conditions, although there is no direct correlation between the increase in kidney size and renal arginase activity [236].…”

Section: Arginase and Polyamine Synthesismentioning

confidence: 99%

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,430

2,036

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Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified

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Section: Arginase and Polyamine Synthesismentioning

confidence: 99%

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,430

2,036

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“…(Berger et al, 1984). Glucuronidase protein level and synthetic rates (Swank et al, 1973), and glucuronidase mRNA activity and concentration (Paigen et al, 1979;Watson et al, 1982;198.5;Catterall and Leary. 1983 ;Palmer et al, 1983) …”

Section: Discussionmentioning

confidence: 99%

Androgen induction of alcohol dehydrogenase in mouse kidney. Studies with a cDNA probe confirmed by nucleotide sequence analysis

Lawther

Duester

et al. 1986

Gene

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“…Using inbred house mice and Drosophila, many workers have directed their studies towards elucidating the function of so-called regulatory genes (Swank et al 1973;Paigen et al 1975Paigen et al ,1976Dickinson 1975) and the genetic organization of regulatory genes in relation to structural genes (Chovnic et al 1976;Abraham and Doane 1978), but much remains still obscure. On the other hand, it has been proposed that adaptive evolution mainly occurs through changes in regulatory systems rather than those in structural genes (Wilson 1976).…”

Section: Introductionmentioning

confidence: 99%

Genetic regulation of amylase activity in Drosophila virilis. I. Activity variation among laboratory strains.

Tejima

Ohba

1981

The Japanese journal of genetics

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Extensive variation of amylase activity in adults and 3rd instar larvae was found among D. virilis strains homozygous for both Amy' allele and Amys allele. The activity in adult is not correlated with that in larva, suggesting that the amylase activity is differently regulated between the two stages, although the same amylase locus is expressed. Cross experiments between the strain with the highest activity and the strain with the lowest activity reveal that amylase activity in adult is an additive character and that amylase activity co-segregates with amylase genotype. Electrophoretic zymogram of the F1 progeny and the mixture of the parents suggested that the genetic factors for amylase activity are probably not identical to the Amy and that they are likely to operate on the activity determination in a trans-active manner.

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Genetic control of glucuronidase induction in mice

Cited by 160 publications

References 31 publications

Arginine metabolism: nitric oxide and beyond

Arginine metabolism: nitric oxide and beyond

Androgen induction of alcohol dehydrogenase in mouse kidney. Studies with a cDNA probe confirmed by nucleotide sequence analysis

Genetic regulation of amylase activity in Drosophila virilis. I. Activity variation among laboratory strains.

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