1999 Fiscal Year Final Research Report Summary
Gene expression of muscle proteins and molecular mechanisms of contractile structure formation
| Project/Area Number |
09670002
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General anatomy (including Histology/Embryology)
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| Research Institution | Chiba University |
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Principal Investigator |
SHIMADA Yutaka School of Medicine, Chiba University Professor, 医学部, 教授 (70009116)
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| Co-Investigator(Kenkyū-buntansha) |
KOMIYAMA Msatoshi School of Medicine, Chiba University Research Associate, 医学部, 助手 (70175339)
YOYOTA Naoji School of Medicine, Chiba University Lecturer, 医学部, 講師 (00188822)
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| Project Period (FY) |
1997 – 1999
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| Keywords | myofibril / stress fiber / actin / myosin / nebulin / α-actinin / connectin / myomesi |
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| Research Abstract |
1. Developmental relationship of myosin binding proteins to myosin during myofibrillogenesis :
Immunofluorescence microscopy of embryonic skeletal muscle revealed that myomesin, connectin and C-protein play an important role for assembly and regular alignment of myosin molecules. It has also been suggested that a mechanism works to remore transiently expressed embryonic isoforms (non-muscle actin and cardiac C-protein) from functional structures after they play some unknown role(s) for structure formation.
2. Dynamics of actin during myofibrillogenesis :
Rhodamine (rh)-labeled actin was microinjected into cultured skeletal muscle cells and stained with anti-nebulin and anti-connectin. It was found that nebulin plays an important role for incorporaton of actin into and exchange of actin in nascent myofibrils, but connectin does not have such a role. This was confirmed by injection of anti-nebulin and anti-connectin to rh-actin injection.
3. Dynamics of actin and α-actinin in myofibrils and stress fibers:
Co-injection of fluorescently labeled actin and α-actinin into cultured cardiomyocytes revealed difference in exchangeability between both proteins in developing myofibrils. This difference seems to be related to the formation of I-Z-I structure of myofibrils. Exchangeability of bothproteins in stress fibers of fibroblasts was high, and thus myofibrils and stress fibers are different structures although they are similar in appearance and composition.
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[Publications] Begum,S., Komiyama,M., Toyota,N., Obinata,T., Maruyama,K., and Shimada,Y.: "Differentiation of muscle-specific proteins in chicken somites as studied by immunofluorescence microscopy"Cell Tissue Res.. 293. 305-311 (1998)
Description
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