Literature DB >> 7903300

Biological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids.

A D'Aniello1, G D'Onofrio, M Pischetola, G D'Aniello, A Vetere, L Petrucelli, G H Fisher.   

Abstract

D-Amino acids administered to animals are absorbed by the intestine and transported through the blood-stream to solid tissues where they are oxidized in vivo by D-amino acid oxidase and D-aspartate oxidase to produce the same compounds they do in vitro; i.e. NH3, H2O2, and the keto acid corresponding to the amino acid ingested. In the liver and kidneys of the animals, an inverse relationship exists between the occurrence of D-amino acids and these oxidative enzymes. For example, younger animals have lower amounts of these oxidases and consequently higher concentrations of free D-amino acids compared to adult animals. If the ingested D-amino acids are not metabolized by these enzymes, they will accumulate in the tissues and may provoke serious damage, e.g. suppression of the synthesis of other essential enzymes and inhibition of the growth rate of the animals. A specific enzyme induction for these D-amino acid oxidases exists in young rats following ingestion of free D-amino acids by the mother. Specifically, when a mother rat ingests D-Ala or D-Asp during pregnancy and suckling, an increase in D-amino acid oxidase or D-aspartate oxidase is observed in the liver and kidneys of the baby rats. These results suggest that the in vivo biological role of these oxidases in animals is to act as detoxifying agents to metabolize D-amino acids which may have accumulated during aging.

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Year:  1993        PMID: 7903300

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  44 in total

1.  D-Amino acid oxidase-mediated increase in spinal hydrogen peroxide is mainly responsible for formalin-induced tonic pain.

Authors:  Jin-Miao Lu; Nian Gong; Yan-Chao Wang; Yong-Xiang Wang
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2.  Protective role of D-amino acid oxidase against Staphylococcus aureus infection.

Authors:  Hideaki Nakamura; Jun Fang; Hiroshi Maeda
Journal:  Infect Immun       Date:  2012-01-23       Impact factor: 3.441

3.  D-Aspartyl residue in a peptide can be liberated and metabolized by pig kidney enzymes.

Authors:  Y Kera; K Funabashi; T Matsumoto; T Watanabe; H Nagasaki; R Yamada
Journal:  Amino Acids       Date:  1996-06       Impact factor: 3.520

4.  Cell selective conditional null mutations of serine racemase demonstrate a predominate localization in cortical glutamatergic neurons.

Authors:  Michael A Benneyworth; Yan Li; Alo C Basu; Vadim Y Bolshakov; Joseph T Coyle
Journal:  Cell Mol Neurobiol       Date:  2012-02-24       Impact factor: 5.046

Review 5.  D-Aspartate acts as a signaling molecule in nervous and neuroendocrine systems.

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Journal:  Amino Acids       Date:  2012-08-08       Impact factor: 3.520

6.  A new strategy to decrease N-methyl-D-aspartate (NMDA) receptor coactivation: inhibition of D-serine synthesis by converting serine racemase into an eliminase.

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Journal:  Br J Pharmacol       Date:  1996-09       Impact factor: 8.739

8.  Trends in DNA Methylation with Age Replicate Across Diverse Human Populations.

Authors:  Shyamalika Gopalan; Oana Carja; Maud Fagny; Etienne Patin; Justin W Myrick; Lisa M McEwen; Sarah M Mah; Michael S Kobor; Alain Froment; Marcus W Feldman; Lluis Quintana-Murci; Brenna M Henn
Journal:  Genetics       Date:  2017-05-22       Impact factor: 4.562

Review 9.  Exploiting oxidative microenvironments in the body as triggers for drug delivery systems.

Authors:  Shivanjali Joshi-Barr; Caroline de Gracia Lux; Enas Mahmoud; Adah Almutairi
Journal:  Antioxid Redox Signal       Date:  2014-04-15       Impact factor: 8.401

10.  Inhibition of D-amino-Acid oxidase activity induces pain relief in mice.

Authors:  Wenjuan Zhao; Ryuichi Konno; Xiang-Jun Zhou; Ming Yin; Yong-Xiang Wang
Journal:  Cell Mol Neurobiol       Date:  2007-09-15       Impact factor: 5.046

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