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Volume 17, Number 18, Issue of September 15, 1997 pp. 6947-6951
Copyright ©1997 Society for Neuroscience

Protein Phosphorylation and Taurine Biosynthesis In Vivo and In Vitro

Received May 1, 1997; revised June 24, 1997; accepted July 9, 1997.

Xiao Wen Tang¹, Che-Chang Hsu¹, John V. Schloss², Morris D. Faiman³, Elliott Wu⁴, Chao-Yuh Yang⁴, and Jang-Yen Wu¹

Departments of ¹ Physiology and Cell Biology, ² Medicinal Chemistry, and ³ Pharmacology and Toxicology, University of Kansas, Lawrence, Kansas 66045-2106, and ⁴ Department of Medicine, Baylor College of Medicine, Houston, Texas 77030

Taurine is known to be involved in many important physiological functions. Here we report that both in vivo and in vitro the taurine-synthesizing enzyme in the brain, namely cysteine sulfinic acid decarboxylase (CSAD), is activated when phosphorylated and inhibited when dephosphorylated. Furthermore, protein kinase C and protein phosphatase 2C have been identified as the enzymes responsible for phosphorylation and dephosphorylation of CSAD, respectively. In addition, the effect of neuronal depolarization on CSAD activity and ³²P incorporation into CSAD in neuronal cultures is also included. A model to link neuronal excitation and CSAD activation by a Ca²⁺-dependent protein kinase is proposed.

Key words: taurine; cysteine sulfinic acid decarboxylase; protein kinase C; protein phosphatase 2C; protein phosphorylation; protein dephosphorylation

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