Induction of histidine-degrading enzymes in protein-starved rats

Sahib, Maharaj K.; Murti, C. R. Krishna

doi:10.1016/0005-2787(67)90197-9

Cited by 11 publications

(5 citation statements)

References 6 publications

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“…Histidine pyruvate aminotransferase was present only in the liver and kidney and the levels of the enzyme were not different in the male and female tissues. It may be inferred from this that sex differ ence affects histidine ammonia-lyase irrespective of the tissue of localization of the enzyme, whereas the increased output of this enzyme during growth and by the protein status of the animal [8,9] is not influenced by the sex of the animal.…”

Section: Discussionmentioning

confidence: 98%

Histidine Uptake and Histidine-degrading Enzymes in Rat Tissues

Mk¹,

Cr²

1970

Enzymol Biol Clin

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The uptake in vitro of histidine was studied using adult male and female rat tissues. In the males the order of maximum uptake was liver>brain>lungs>heart or kidney>skin and in females: liver>lungs>brain>heart>kidney >skin. Female tissue picked up significantly higher amounts of the amino acid than the male tissue. Histidine ammonialyase activity was distributed in the following order: liver>skin>kidney>lungs; here again the female tissues showed higher specific activity than the males. Histidine pyruvate aminotransferase activity was confined to liver and kidney and was of the same order in the male and female. Although brain picked up histidine at rates comparable to liver, histidine ammonialyase and histidine pyruvate aminotransferase were not detected in this tissue.

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Section: Discussionmentioning

confidence: 98%

Histidine Uptake and Histidine-degrading Enzymes in Rat Tissues

Mk¹,

Cr²

1970

Enzymol Biol Clin

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“…Our results suggest that the increased histidase activity observed by Keene and Austic [21] may have been due to increased synthesis of this enzyme. Feeding a high protein diet to rats increases hepatic histidase activity [12][13][14][15], and this increase in activity has also been associated with an increase in hepatic histidase mRNA concentration [14 -16].…”

Section: Discussionmentioning

confidence: 99%

“…The increased activity of hepatic histidase in rats fed a high protein diet, or an imbalancing mixture of amino acids is associated with an increase in the mRNA concentration of hepatic histidase [14,15,19]. Interestingly, dietary protein intake does not increase the activity of skin histidase [12,13,17].…”

Section: Introductionmentioning

confidence: 95%

“…In rats, hepatic histidase activity is increased as dietary protein consumption increases [12][13][14][15][16], but when rats are fed diets supplemented with l-histidine, hepatic histidase activity is not altered [12][13][14]17,18]. The increased activity of hepatic histidase in rats fed a high protein diet, or an imbalancing mixture of amino acids is associated with an increase in the mRNA concentration of hepatic histidase [14,15,19].…”

Section: Introductionmentioning

confidence: 98%

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Molecular cloning of chicken hepatic histidase and the regulation of histidase mRNA expression by dietary protein

Chendrimada

Davis

2005

The Journal of Nutritional Biochemistry

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“…These initial events may be thought to initiate reaction chains, which would involve the cyclic AMP system and perhaps various protein kinases in the case of glucagon in- duction. Since, due to its 2.5 day half-life time (60), the time required to detect substantial alterations in catalytic activity of this enzyme is long (several days), the possibility that glucocorticoid may act on histidase indirectly, through in creased amino acid production (6), cannot be eliminated; high amino acid intake has been shown to result in elevated histidase levels (40,41,50,54,56,57,60). These various individualized chains of inductive events might finally converge to accelerate or de-repress a common rate-limiting step, which may be involved in the transcriptive synthesis of histidase messenger RNA and/or its translation to form the histidase protein.…”

Section: Mechanisms Underlying the Development Of Histidase And Its Hmentioning

confidence: 99%

Multihormonal Regulation of Hepatic Histidase during Postnatal Development

Feigelson¹

1973

Enzyme Protein

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Hepatic histidase of the rat is presented as a model system, wherein multihormonal regulation, effecting a complex postnatal developmental course of an enzyme level, is explored. Three hormonal inducers of rat liver histidase: estrogen, glucocorticoid and glucagon, and several suppressors of this enzyme: pituitary products (including growth hormone and ACTH) and thyroxine, participate in the regulation of the postnatal development of this enzyme. The developmental pattern of competence of the liver to respond to each hormonal inducer is temporally characteristic for each hormone: estrogen being capable of inducing histidase only in animals beyond the neonatal stage, glucocorticoid of inducing the enzyme only during the first two postnatal months, and glucagon being a functional inducer at all postnatal stages. Estrogen is responsible for the rise in histidase levels associated with the female during puberty, glucagon, via cyclic AMP, participates in implementing the neonatal rise in the enzyme; and glucocorticoid is a requirement for both the neonatal and male adolescent elevations of this enzyme. A network of interplay among the hormones is revealed, in which the pituitary is required to mediate estrogenic induction and androgen and the two inducers, glucocorticoid and glucagon, curtail estrogenic induction. Transcriptional and translational processes have been implicated as underlying all the hormonal influences on histidase studied and the normal adolescent developmental rise of the enzyme. It is thus concluded that the complex postnatal developmental course of hepatic histidase is shaped by the resultant of a temporally determined interplay of a variety of stimulatory and suppressive endocrine influences.

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Induction of histidine-degrading enzymes in protein-starved rats

Cited by 11 publications

References 6 publications

Histidine Uptake and Histidine-degrading Enzymes in Rat Tissues

Histidine Uptake and Histidine-degrading Enzymes in Rat Tissues

Molecular cloning of chicken hepatic histidase and the regulation of histidase mRNA expression by dietary protein

Multihormonal Regulation of Hepatic Histidase during Postnatal Development

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