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- 주제어 : Synaptobrevin (검색결과 2 건)
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Association of VAMP-2 and Syntaxin 1A Genes with Adult Attention Deficit Hyperactivity Disorder
Ay˚e Nur Inci Kenar,Özlem I˙zci Ay,Hasan Herken,Mehmet Emin Erdal 대한신경정신의학회 2014 PSYCHIATRY INVESTIGATION Vol.11 No.1
Objective The etiology of attention deficit hyperactivity disorder (ADHD) has not been entirely clarified yet. Structural and metabolicdifferences at the prefrontal striatal cerebellary system and the interaction of gene and environment are the main factors that thought toplay roles in the etiology. Genetic investigations are performed especially about the dopamine pathways and receptors. In this study; itwas aimed to investigate the association of the synaptobrevin-2 (VAMP-2) gene Ins/Del polymorphism and syntaxin 1A gene intron7 polymorphism, which take place in encoding presynaptic protein, with adult ADHD. Methods One hundred thirty-nine patients, having ADHD aging between 18 and 60 years and 106 healthy people as controls were includedinto the study. DNA samples were extracted from whole blood and genetic analysis were performed. ResultsaaA significant difference was determined between ADHD and VAMP-2 Ins/Del polymorphism and syntaxin 1A intron 7 polymorphismaccording to the control group. These polymorphisms were found not to be associated with subtypes of ADHD. Conclusion It is supposed that synaptic protein genes together with dopaminergic genes might have roles in the etiology of ADHD.
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Synaptobrevin (VAMP)유전자의 대장균에서의 발현 및 Clostridium botulinum type B 독소에 의한 절단
정현호,양기혁,이상달,양규환 한국독성학회 1997 Toxicological Research Vol.13 No.4
Synaptobrevin is a kind of vesicle associated membrane proteins (VAMPs) which plays a secretary role in the neuronal synapse and was recently known as the biochemical target of botulinum neurotoxin type B. The structural gene of the synaptobrevin was cloned from mouse brain using RT-PCR technique and was seqrtenced. The deduced amino acid sequence showed that the synaptobrevin protein from mouse brain is exactly the same with that of the rat brain in the amino acid level. The synaptobrevin gene was subcloned into pET3a vector and expressed in E. coli. The molecular weight of the recombinant protein was 19 kDa as expected. Moreover, when the recombinant synaptobrevin protein was incubated with the native neurotoxin of Clostridium botulinum type B, it was cleaved by the toxin in a time dependent manner. This implies that the recombinant synaptobrevin protein and the native toxin are reacted in the same way as the native synaptobrevin did in the neuronal cells.
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