| Literature DB >> 16525061 |
Alex S Huang1, Anne Beigneux, Zachary M Weil, Paul M Kim, Mark E Molliver, Seth Blackshaw, Randy J Nelson, Stephen G Young, Solomon H Snyder.
Abstract
D-aspartate, an abundant D-amino acid enriched in neuroendocrine tissues, can be degraded by D-aspartate oxidase (Ddo). To elucidate the function of D-aspartate, we generated mice with targeted deletion of Ddo (Ddo(-/-)) and observe massive but selective augmentations of D-aspartate in various tissues. The pituitary intermediate lobe, normally devoid of D-aspartate from endogenous Ddo expression, manifests pronounced increases of immunoreactive D-aspartate in Ddo(-/-) mice. Ddo(-/-) mice show markedly diminished synthesis and levels of pituitary proopiomelanocortin/alpha-MSH, associated with decreased melanocortin-dependent behaviors. Therefore, Ddo is the endogenous enzyme that degrades D-aspartate, and Ddo-enriched organs, low in D-aspartate, may represent areas of high turnover where D-aspartate may be physiologically important.Entities:
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Year: 2006 PMID： 16525061 PMCID： PMC6675153 DOI： 10.1523/JNEUROSCI.5060-05.2006
Source DB: PubMed Journal: J Neurosci ISSN： 0270-6474 Impact factor: 6.167