Tetrahydrobiopterin‐dependent stabilization of neuronal nitric oxide synthase dimer reduces susceptibility to phosphorylation by protein kinase C in vitro

FEBS Letters

Okada, Daisuke¹ 

[1] Laboratory for Synaptic Functions, Frontier Research Program, The Institute of Physical and Chemical Research, 2-1 Hirosawa, Wako, Saitama 351-01, Japan

关键词: Tetrahydrobiopterin;    Nitric oxide synthase;    Protein kinase C;    Phosphorylation;   

DOI  :  10.1016/S0014-5793(98)00993-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Binding of (6R)-5,6,7,8-tetrahydro-l-biopterin (H₄B) stabilizes the homodimeric structure of neuronal nitric oxide synthase (nNOS). In the present study, low-temperature sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed differential susceptibility of stabilized and non-stabilized dimers to in vitro phosphorylation by protein kinase C. Protein kinase C preferentially phosphorylated the non-stabilized dimer. Although a low extent of phosphorylation was detected in the stabilized dimer, most of it was estimated to be due to phosphorylation of the dimer before its stabilization. Phosphorylation did not affect the stabilizing effect of H₄B. These results indicate that H₄B-dependent dimer stabilization prevents nNOS from protein kinase C-dependent phosphorylation in vitro.

【 授权许可】

Unknown