The metabolism of histidine. Liver-enzyme changes during development

Makoff, Rhoda; Rc, Baldridge

doi:10.1016/0304-4165(64)90190-4

Cited by 25 publications

(7 citation statements)

References 11 publications

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“…For example, various transaminases have been reported to develop activity in rat liver at the time of birth, including tyrosine transaminase (Auerbach & Waisman, 1959;Kretchmer, Levine, McNamara, & Barnett, 1956;, phenylalanine transaminase (Kenney & Kretchmer, 1959), tryp. tophan tranaminase (Trappit, 1964) and histidine transaminase (Makoff & Baldridge, 1964).…”

Section: Discussionmentioning

confidence: 99%

Gluconeogenesis from amino acids in neonatal rat liver

Yeung¹,

Oliver²

1967

Biochemical Journal

104

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1. The utilization of amino acids for gluconeogenesis by rat liver develops in postnatal life, reaching maximum activity at the fifth day. 2. The activity of aspartate transaminase shows a similar trend in postnatal development and the increased activity appears to be due to the soluble enzyme. 3. The activity of alanine transaminase is low in foetal and postnatal rat liver and increases in activity at about the twentieth day. 4. Aspartate, glutamate and alanine make a major contribution to gluconeogenesis in the postnatal rat liver.

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Section: Discussionmentioning

confidence: 99%

Gluconeogenesis from amino acids in neonatal rat liver

Yeung¹,

Oliver²

1967

Biochemical Journal

104

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“…Variation in histidase and more particularly of urocanase activities were observed even on animals maintained on the same stock casein diet (controls). Makoff & Baldridge (1964) reported that histidase activity, barely detectable at birth, varied with the age of the rat, whereas urocanase activity was higher at the time of parturition and remained fairly constant up to 50 days of age. However, our results (Table 2) indicate that in rats (40-60 days old) histidase and urocanase activities are of similar magnitude and an increase in the urocanase activity was concomitant with an increase in histidase activity in control animals ( Baldridge & Spolter (1963), the transaminase pathway is relatively more important in the rat.…”

Section: Discussionmentioning

confidence: 99%

Histidine metabolism in experimental protein malnutrition in rats

Rao

Deodhar

Hariharan

1965

Biochemical Journal

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1. The activities of the enzymes histidase, urocanase and histidine-pyruvate transaminase were studied in rats under conditions of protein malnutrition. Urocanase and histidase activities in liver were markedly lowered in experimental protein malnutrition, but the activity of histidine-pyruvate transaminase was unaffected. There is a metabolic control in vivo of the enzymes involved in the catabolism of histidine. 2. Significant changes in the urinary excretion of histidine, composition of liver and serum were apparent in the protein-malnourished rat. 3. The changes in the activities of the enzymes and other parameters were of a reversible nature and dependent on the nature of the dietary protein. 4. The significance of these findings is discussed in relation to abnormal histidine metabolism in kwashiorkor.

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“…The developmental course of hepatic histidase had been demonstrated by Auerbach and Waisman (2) and later by Makoff and Baldridge (44) to be polyphasic: the enzyme is detectable initially at parturition, rises slightly thereafter, maintaining relatively low titers for the first two to three postnatal weeks, following which a marked increase in enzymatic activity is manifested in both sexes extending throughout the adolescent period, this secondary rise being of greater magnitude in the female than in the male ( fig. 1).…”

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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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The metabolism of histidine. Liver-enzyme changes during development

Cited by 25 publications

References 11 publications

Gluconeogenesis from amino acids in neonatal rat liver

Gluconeogenesis from amino acids in neonatal rat liver

Histidine metabolism in experimental protein malnutrition in rats

Multihormonal Regulation of Hepatic Histidase during Postnatal Development

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