| Budget Amount *help |
¥3,790,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥390,000)
Fiscal Year 2007: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2006: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Research Abstract |
Synemin is a muscle intermediate filament protein that was originally identified in birds. Recently, the human α- and β-synemin orthologues have been cloned, the latter of which was previously termed human desmuslin. Both human synemin isoforms derive from the same gene as a result of differential splicing between exons 4 and 5 such that the β-synemin protein is 312 amino acids shorter at its C-terminus. Both β-synemin mRNA and protein are highly expressed in skeletal and cardiac muscles, while northern blot analysis shows weak doublet in brain, indicating that there are two different types of synemin present in brain on the basis of mRNA level. We consider that β-synemin plays a role in maintaining the cytoskeletal structure in skeletal muscle, while α-synemin is also involving to role of the morphological maintenance of neuron and glia. We think that it is of great importance to elucidate the proteins involving α-synemin in brain. Therefore, we decided to examine human brain cDNA library to find a new sequence that interacts with the specific region to α-synemin, 312 amino acids sequences, using Matchmaker Two-hybrid system 3.
Last year, we examined the expression of α- and β-synemin mRNA and found that both synemin mRNAs are expressed in the large neurons of dorsal side of pons and midbrain using in situ hybridization. This year, we further recognized that both synemin mRNA and its protein are co-localized in the same large neurons by in situ hybridization and immunohistochemical analysis.
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