2005 Fiscal Year Final Research Report Summary
Study of protein involving with a-synemin in brain
Project/Area Number |
16590812
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Neurology
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Research Institution | Gunma University |
Principal Investigator |
MIZUNO Yuji GUNMA UNIVERSITY, Medicine, Assistant Professor, 医学部, 講師 (20282395)
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Co-Investigator(Kenkyū-buntansha) |
MIZUSHIMA Kazuyuki , 医学部, 助手 (00344945)
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Project Period (FY) |
2004 – 2005
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Keywords | β-synemin / Two-hybrid system / dystrobrevin / desmuslin / intermediate filament / muscular dystrophy |
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 a-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 got only a few positive clones and did not confirm the affinity in-vitro examination. Although we got more than 30 positive clones, some of which overlapped with each other. We are in the process of in-vitro examination to analyse if the sequences of 312 amino acids of α-synemin interact with those of positive clones in-vitro.
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