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Title: Inhibition of SNAP-25 phosphorylation at Ser(187) is involved in chronic morphine-induced down-regulation of SNARE complex formation
Author: Xu, NJ ; Yu, YX ; Zhu, JM ; Liu, H ; Shen, L ; Zeng, R ; null(张 旭) ; Pei, G
Source: JOURNAL OF BIOLOGICAL CHEMISTRY
Issued Date: 2004
Volume: 279, Issue:39, Pages:40601-40608
Keyword: PROTEIN-KINASE-C ; SYNAPTOSOME-ASSOCIATED PROTEIN ; RAT PHEOCHROMOCYTOMA CELLS ; SYNAPTIC VESICLE DOCKING ; MEMBRANE-FUSION COMPLEX ; LONG-TERM POTENTIATION ; NEUROTRANSMITTER RELEASE ; OPIOID RECEPTOR ; PC12 CELLS ; DEPENDENT PHOSPHORYLATION
Subject: Biochemistry & Molecular Biology
Corresponding Author: Pei, G (reprint author), Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol,Lab Mol Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China,gpei@sibs.ac.cn
English Abstract: Opiate abuse has been shown to cause adaptive changes in presynaptic release and protein phosphorylation-mediated synaptic plasticity, but the underlying mechanisms remain unclear. Neuronal SNARE proteins serve as important regulatory molecules underlying neural plasticity in view of their major role in the process of neurotransmitter release. In the present study, the expression of SNAP-25, a t-SNARE protein essential for vesicle release, was found to be dramatically regulated in hippocampus after chronic morphine treatment, which was visualized with two-dimensional gel electrophoresis. The spots of SNAP-25 in the gel were shifted along the dimension of isoelectric point, indicating a likely change of the post-transcriptional modification. Immunoblotting analysis with specific antibody to Ser(187), a protein kinase C (PKC) phosphorylation site of SNAP-25, revealed that the specific phosphorylation was correspondingly decreased, which was correlated with morphine-induced inhibition of PKC activity. Moreover, the level of ternary complex of SNARE proteins in either synaptosomes or PC12 cells was significantly reduced after chronic morphine treatment. This suggests a causal relationship between the inhibition of PKC-dependent SNAP-25 phosphorylation and the down-regulation of SNARE complex formation after chronic morphine treatment. Further analysis of SNARE complex formed by transfection of the wild-type or Ser(187) mutants of SNAP-25 showed that only wild-type-formed complex was inhibited by morphine treatment. Thus, these results indicate that chronic morphine treatment inhibits phosphorylation of SNAP-25 at Ser(187) and leads to a down-regulation of SNARE complex formation, which presents a potential molecular mechanism for the alteration of exocytotic process and neural plasticity during opiate abuse.
Indexed Type: sci
Language: 英语
Content Type: 期刊论文
URI: http://ir.sibs.ac.cn/handle/331001/1945
Appears in Collections:神经所(总)_期刊论文
感觉系统研究组_期刊论文

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Recommended Citation:
Xu, NJ; Yu, YX; Zhu, JM; Liu, H; Shen, L; Zeng, R; Zhang, X; Pei, G.Inhibition of SNAP-25 phosphorylation at Ser(187) is involved in chronic morphine-induced down-regulation of SNARE complex formation,JOURNAL OF BIOLOGICAL CHEMISTRY,2004,279(39):40601-40608
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