TY - JOUR
T1 - Distinct regional distribution in the brain of messenger RNAs for the two isoforms of synaphin associated with the docking/fusion complex
AU - Ishizuka, T.
AU - Saisu, H.
AU - Odani, S.
AU - Kumanishi, T.
AU - Abe, T.
N1 - Funding Information:
We thank K. Kobayashi and T. Ichikawa for technical assistance in in situ hybridizations. Thanks are also due to M. Takahashi for a kind gift of a monoclonal antibody against synaptotagmin. This study was supported by grants (to T. A.) from the Ministry of Education, Science, Sports and Culture, Japan. T. I. was supported by a Research Fellowship for Young Scientists from the Japan Society for the Promotion of Science.
PY - 1999/1
Y1 - 1999/1
N2 - Synaphin is a 19,000 mol. wt cytosolic protein we first found to co- purify with the docking/fusion complex crucial to neurotransmitter release from presynaptic terminals. Two isoforms of synaphin (synaphins I and 2)(also called complexins II and I, respectively) exist in the rat brain. On density gradient centrifugation of a Triton X-100 extract of brain membranes, synaphin was found to be associated with the 7S complex that contains synaptotagmin, syntaxin, synaptosomal-associated protein of 25,000 mol. wt and vesicle-associated membrane protein. A smaller complex devoid of synaphins was also identified by immunoprecipitation with a monoclonal antibody against synaptosomal-associated protein of 25,000 mol. wt. Messenger RNAs for synaphins 1 and 2 were expressed predominantly in the brain. In situ hybridization using probes specific to synaphins 1 and 2 indicated that the distribution of their mRNAs was significantly different in brain regions such as olfactory bulb, hippocampus, cerebral cortex, piriform cortex; cerebellum, thalamus and facial nuclei. These results show synaphin as a component of the 7S complex and suggest different physiological implications for the two isoforms.
AB - Synaphin is a 19,000 mol. wt cytosolic protein we first found to co- purify with the docking/fusion complex crucial to neurotransmitter release from presynaptic terminals. Two isoforms of synaphin (synaphins I and 2)(also called complexins II and I, respectively) exist in the rat brain. On density gradient centrifugation of a Triton X-100 extract of brain membranes, synaphin was found to be associated with the 7S complex that contains synaptotagmin, syntaxin, synaptosomal-associated protein of 25,000 mol. wt and vesicle-associated membrane protein. A smaller complex devoid of synaphins was also identified by immunoprecipitation with a monoclonal antibody against synaptosomal-associated protein of 25,000 mol. wt. Messenger RNAs for synaphins 1 and 2 were expressed predominantly in the brain. In situ hybridization using probes specific to synaphins 1 and 2 indicated that the distribution of their mRNAs was significantly different in brain regions such as olfactory bulb, hippocampus, cerebral cortex, piriform cortex; cerebellum, thalamus and facial nuclei. These results show synaphin as a component of the 7S complex and suggest different physiological implications for the two isoforms.
KW - Docking/fusion complex
KW - In situ hybridization
KW - Neurotransmitter release
KW - SNAREs
KW - Synaphinl/complexin
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U2 - 10.1016/S0306-4522(98)00223-1
DO - 10.1016/S0306-4522(98)00223-1
M3 - Article
C2 - 10051208
AN - SCOPUS:0032889591
VL - 88
SP - 295
EP - 306
JO - Neuroscience
JF - Neuroscience
SN - 0306-4522
IS - 1
ER -