Rat Liver Histidase: Glucose Repression and Half-life after Casein Hydrolysate Feeding

Lee, Shih Ching; Tews, Jean K.; Morris, M. L.; Harper, Alfred E.

doi:10.1093/jn/102.3.319

Cited by 13 publications

(2 citation statements)

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“…Indeed there is considerable evidence relating glucagon and cyclic AMP to the neonatal development of a good many gluconeogenic and amino acid metabolizing enzymes (23-25, 31, 32, 68, 69). Lee et al (40,41), have demonstrated induction of hepatic histidase by glucagon and cyclic AMP in young males. We have further investigated the roles which glucagon and cyclic AMP might assume in the regulation of histidase during its postnatal developmental course.…”

Section: Glucagonmentioning

confidence: 99%

“…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%

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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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Section: Glucagonmentioning

confidence: 99%