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227 Molecular cloning of avian synapse-specific proteins
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227
MOLECULAR CLONING OF AVIAN SYNAPSE-SPECIFIC PROTEINS NAOHIRO KIMURA 1, KAZUNORI KONDO I, NORIO KUROSAWA' AND YASUZO TSUKADA 2 ~Department of Bioengineering, Faculty of Engineering,~Institute of Life Science,Soka University, l-236 Tangi-cho,Hachioji,Tokyo 192,JAPAN
To isolate probes for investigating the changes ofgene expresssion of synaptic proteins in the process of imprinting formation in ducklings, we screened cDNA libraries using anti-duck synaptic plasma membrane antibodies and isolated many clones. These clones were characterized by hybridization and partial sequencing. The most abundant were Ca'~/calmodulin dependent protein kinaselI (CaMKII) and neural cell adhesion molecule (NCAM). Others were brain-specific or abundant membrane proteins like contactin, Na/Ca-exchnger, Na/K-ATPase, synapse-specific proteins like synaptotagmine, synapsinI, syntaxin, neurexin and unknown proteins. Northern blot analysis indicated that those unknown proteins were all expressed only in the brain. Several of these unknown proteins were further characterized by nucleotide sequencing and their expressions were investigated immuno-histochemically.
228
p25/smg p25A,
LOCALIZATION
OF r a b 3 A
PROTEIN, PROTEIN,
TARGET PROTEIN, GDI, IN THE RAT
ITS
A SMALL
RABPHILIN, SYNAPSE
AND
GTP-BINDING ITS REGULATORY
rab AKIRAMIZOGTJCHI, CHIZUKA IDE DeBt. of Anatomy. Kobe University School of medicine. Kobe 650 JaDam We have investigated the ultrastructural localization of rab3A p25/smg p25A', a small GTP-binding protein, its target protein, rabphilin, and its regulatory protein rab GDI in the rat neuromuscular junction, rab3A p25 was focally noted on the discrete presynaptic sites corresponding to the active zones. Rabphilin was located homogeniously on synaptic vesicles, r a b G D I was present on the presynaptic plasma membrane and synaptic cytosol. This distinctive distribution of rab3A p25, rabphilin, and r a b G D I suggests that they play differential roles in the exo-endocytotic cycle of synaptic vesicles.
227
MOLECULAR CLONING OF AVIAN SYNAPSE-SPECIFIC PROTEINS NAOHIRO KIMURA 1, KAZUNORI KONDO I, NORIO KUROSAWA' AND YASUZO TSUKADA 2 ~Department of Bioengineering, Faculty of Engineering,~Institute of Life Science,Soka University, l-236 Tangi-cho,Hachioji,Tokyo 192,JAPAN
To isolate probes for investigating the changes ofgene expresssion of synaptic proteins in the process of imprinting formation in ducklings, we screened cDNA libraries using anti-duck synaptic plasma membrane antibodies and isolated many clones. These clones were characterized by hybridization and partial sequencing. The most abundant were Ca'~/calmodulin dependent protein kinaselI (CaMKII) and neural cell adhesion molecule (NCAM). Others were brain-specific or abundant membrane proteins like contactin, Na/Ca-exchnger, Na/K-ATPase, synapse-specific proteins like synaptotagmine, synapsinI, syntaxin, neurexin and unknown proteins. Northern blot analysis indicated that those unknown proteins were all expressed only in the brain. Several of these unknown proteins were further characterized by nucleotide sequencing and their expressions were investigated immuno-histochemically.
228
p25/smg p25A,
LOCALIZATION
OF r a b 3 A
PROTEIN, PROTEIN,
TARGET PROTEIN, GDI, IN THE RAT
ITS
A SMALL
RABPHILIN, SYNAPSE
AND
GTP-BINDING ITS REGULATORY
rab AKIRAMIZOGTJCHI, CHIZUKA IDE DeBt. of Anatomy. Kobe University School of medicine. Kobe 650 JaDam We have investigated the ultrastructural localization of rab3A p25/smg p25A', a small GTP-binding protein, its target protein, rabphilin, and its regulatory protein rab GDI in the rat neuromuscular junction, rab3A p25 was focally noted on the discrete presynaptic sites corresponding to the active zones. Rabphilin was located homogeniously on synaptic vesicles, r a b G D I was present on the presynaptic plasma membrane and synaptic cytosol. This distinctive distribution of rab3A p25, rabphilin, and r a b G D I suggests that they play differential roles in the exo-endocytotic cycle of synaptic vesicles.