| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Outline of Final Research Achievements |
Chicken D-serine dehydratase (DSD) degrades D-serine to pyruvate and ammonia. D-Serine is a physiological coagonist that regulates the activity of the NMDA receptor for L-glutamate. We have found in chickens that D-serine is degraded only by DSD in the brain, whereas it is also degraded to 3-hydroxypyruvate by D-amino acid oxidase (DAO) in the kidney and liver. In mammalian brains, D-serine is degraded only by DAO. It has not been clarified why chickens selectively use DSD for the control of D-serine concentrations in the brain.
In the present study, we measured DSD activity in chicken tissues, and examined the cellular localization of DSD using a specific anti-chicken DSD antibody. In chicken brain, cerebellum showed about 6-fold-higher activity than cerebrum. At the cellular level DSD was demonstrated in Bergmann-glia cells of the cerebellum and in astrocytes. The finding of DSD in glial cells seems to be important because D-serine is involved in NMDAR-dependent brain functions.
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