scholarly journals Changes in ornithine decarboxylase and antizyme activities in developing mouse brain

1988 ◽  
Vol 250 (3) ◽  
pp. 797-803 ◽  
Author(s):  
H Onoue ◽  
S Matsufuji ◽  
M Nishiyama ◽  
Y Murakami ◽  
S Hayashi
Keyword(s):  
Monoclonal Antibodies ◽  
Ornithine Decarboxylase ◽  
Mouse Brain ◽  
Rat Liver ◽  
Developmental Period ◽  
Kinetic Properties ◽  
Antizyme Inhibitor ◽  
Developing Mouse Brain ◽  
The Brain

A macromolecular inhibitor to ornithine decarboxylase (ODC) present in mouse brain was identified as ODC antizyme [Fong, Heller & Canellakis (1976) Biochim. Biophys. Acta 428, 456-465; Heller, Fong & Canellakis (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 1858-1862] on the basis of kinetic properties, Mr and reversal of its inhibition by antizyme inhibitor. The brain antizyme, however, did not cross-react immunochemically with any of seven monoclonal antibodies to rat liver antizyme. ODC activity in mouse brain rapidly decreased after birth, in parallel with putrescine content, and almost disappeared by 3 weeks of age. Free antizyme activity appeared shortly after birth and increased gradually, whereas ODC-antizyme complex already existed at birth and then gradually decreased. Thus total amount of antizyme remained about the same throughout the developmental period in mouse brain. In addition to ODC-antizyme complex, inactive ODC protein was detected by radioimmunoassay in about the same level as the complex at 3 weeks of age. Upon cycloheximide treatment, both free ODC activity and ODC-antizyme complex rapidly disappeared, although free antizyme and the inactive ODC protein were both quite stable.

scholarly journals A macromolecular inhibitor of the antizyme to ornithine decarboxylase

1982 ◽  
Vol 204 (3) ◽  
pp. 647-652 ◽  
Author(s):  
K Fujita ◽  
Y Murakami ◽  
S Hayashi
Keyword(s):  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Molecular Size ◽  
Antizyme Inhibitor ◽  
Heat Labile

A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, ‘antizyme inhibitor’, was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a complex with antizyme. Therefore the antizyme inhibitor can be used to assay the amount of inactive ODC-antizyme complex formed in vitro. When assayed by this method, the complex was shown to be eluted before ODC from a Sephadex G-100 column. Significant increase in ODC activity was observed when the antizyme inhibitor was added to crude liver extracts from rats that had been injected with 1,3-diaminopropane to cause decay of ODC activity, suggesting the presence of inactive ODC-antizyme complex in the extracts.

scholarly journals Antizyme to ornithine decarboxylase is present in the liver of starved rats

1984 ◽  
Vol 218 (2) ◽  
pp. 557-562 ◽  
Author(s):  
K Fujita ◽  
S Matsufuji ◽  
Y Murakami ◽  
S Hayashi
Keyword(s):  
Molecular Weight ◽  
Ornithine Decarboxylase ◽  
Kinetic Properties ◽  
Average Amount ◽  
Physiological Conditions ◽  
Antizyme Inhibitor ◽  
Ad Libitum

Antizyme to ornithine decarboxylase (ODC) and ODC-antizyme complex were both present in liver cytosols of starved rats. The antizyme was identified by its molecular weight, kinetic properties, formation of a complex with ODC, and reversal of its inhibition by antizyme inhibitor. The average amount of antizyme in liver cytosols of starved rats was 0.1 unit/mg of protein, roughly corresponding to basal hepatic ODC activity in rats fed ad libitum. The presence of ODC-antizyme complex was detected by using antizyme inhibitor. These results indicate that antizyme participates in the regulation of ODC activity in vivo under physiological conditions.

scholarly journals Comparison of the properties of two forms of pyruvate kinase in rat liver and determination of their separate activities during development

1972 ◽  
Vol 127 (4) ◽  
pp. 721-731 ◽  
Author(s):  
Marshall C. Middleton ◽  
Deryck G. Walker
Keyword(s):  
Skeletal Muscle ◽  
Pyruvate Kinase ◽  
Rat Liver ◽  
Developmental Period ◽  
Late Gestation ◽  
Kinetic Properties ◽  
Foetal Rat ◽  
Neonatal Liver ◽  
Developing Rat

1. Two forms of hepatic pyruvate kinase, designated type L and type M, were distinguished on the basis of kinetic, chromatographic, electrophoretic and immunological criteria. They were partially purified and their properties compared with each other and with the purified enzyme from skeletal muscle. 2. In contrast with type L, the type M enzyme showed no marked evidence of co-operative interactions with phosphoenolpyruvate and was not stimulated by fructose diphosphate. 3. The activity profiles of type L and type M enzymes were determined in developing rat liver by utilizing differences in the kinetic properties of the two forms. The high activity of type M enzyme in the early foetal rat decreased in late gestation and immediately after birth to reach a low value, which remained essentially constant for the remainder of the developmental period. The activity of type L enzyme, in contrast, was low in the early foetal and neonatal liver but increased markedly at the onset of weaning. 4. Possible roles of the two forms of hepatic pyruvate kinase in the control of glycolysis and gluconeogenesis are discussed.

The Mode of Action of 6-Methoxy-1,2,3,4-Tetrahydro-β-Carboline on Brain Serotonin

1973 ◽  
Vol 51 (4) ◽  
pp. 482-485 ◽  
Author(s):  
Beng T. Ho ◽  
Dorothy Taylor ◽  
K. E. Walker ◽  
William M. McIsaac
Keyword(s):  
Monoamine Oxidase ◽  
Rat Brain ◽  
Mouse Brain ◽  
Rat Liver ◽  
Mode Of Action ◽  
Tryptophan Hydroxylase ◽  
Rat Plasma ◽  
Concomitant Increase ◽  
Tryptophan Pyrrolase ◽  
The Brain

6-Methoxy-1,2,3,4-tetrahydro-β-carboline (6-MeO-THBC), which specifically elevates serotonin in the brain, exerted no significant effects on mouse brain monoamine oxidase, rat brain tryptophan hydroxylase, and rat liver tryptophan pyrrolase. There was a marked activation of rat plasma and liver 5-hydroxytryptophan decarboxylase and a concomitant increase of serotonin levels in the two tissues. 6-MeO-THBC did not alter the endogenous tryptophan levels in rat plasma and brain. A significant facilitation of the uptake of [3-14C]-5-hydroxytryptophan was observed in brains of mice treated with 6-MeO-THBC. The possibility that the increased serotonin was derived from 6-MeO-THBC itself was ruled out.

Author response for "Hemovasculogenic origin of blood vessels in the developing mouse brain"

2020 ◽  
Author(s):  
Miguel A. Gama Sosa ◽  
Rita De Gasperi ◽  
Gissel M. Perez ◽  
Patrick R. Hof ◽  
Gregory A. Elder
Keyword(s):  
Blood Vessels ◽  
Mouse Brain ◽  
Author Response ◽  
Developing Mouse Brain
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