Study for the physiological functions of cytoskeleton-related calmodulin-binding proteins.
| Project/Area Number |
60440104
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Osaka University Medical School |
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Principal Investigator |
SOBUE Kenji Professor, Osaka University Medical School, 医学部, 教授 (20112047)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Toshihiko Assistant professor, Osaka University Medical Scool, 医学部, 助手 (20163545)
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| Project Period (FY) |
1985 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥18,200,000 (Direct Cost: ¥18,200,000)
Fiscal Year 1987: ¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 1986: ¥5,800,000 (Direct Cost: ¥5,800,000)
Fiscal Year 1985: ¥9,000,000 (Direct Cost: ¥9,000,000)
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| Keywords | Cytoskeleton / Plasma membrane / Transformation / Smooth Muscle / Synapse / Calmodulin / Actin-Myosin Interaction / 癌化 / アクチン / カルデスモン / カルスペクチン / 細胞膜裏打ち構造 / 血管平滑筋 / ミオシン / カルモデュリン結合蛋白質 / ミオシン軽鎖キナーゼ / 微小管付属蛋白質 / チューブリン |
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| Research Abstract |
Ca^<2+> is one of the most important intracelluar messenger in many cellular functions including contraction, endocytosis, exocytosis and cell division. Ca^<2+> signals are mediated by Ca^<2+>-receptive proteins such as troponin C and calmodulin. Cytoskeleton is the three-dimensional intracelluar meshwork of protein filaments which are molecular bases of these celluar functions. We have been studing the Ca^<2+>-dependent regulation of these functions, and have discovered a group of calmodulin-bindig proteins which also interact with cytoskeleton. In this study, we have investigated the Ca^<2+>-calmodulin dependent regulatory mechanism of cytoskeleton mediated by the cytoskeleton-interacting calmodulin-binding proteins:
1. Regulation of MAPs-actin interaction by Ca^<2+> and calmodulin.
2. Redistribution of caldesmon associated with Con A receptor capping on splenic T-lymphocytes.
3. Reorganization of actin and calspectin in 3T3 cells induced by TPA treatment.
4. Ca^<2+>-dependent regulation
… More
of subemembranous cytoskeleton.
5. Regulation of spectrin-actin interaction by protein 4.1-calmodulin complex.
6. Function of cytosynalin, a 35 kDa cytoskeleton-interacting and calmodulin-binding protein.
7. Identification of a new 84/82 kDa calmodulin-binding protein as synapsin I.
8. Purification of an 80 kDa Ca^<2+>-dependent actin-severing protein from bovein adrenal medulla.
9. Crosslinking of F-actin caused by caldesmon aggregates, not by its dimers.
10. Relationship of the multiple phosphorylation of myosin light chain and myosin ATPase activity.
11. Regulation of the tropomyosin-enhanced myosin ATPase activity by caldesmon.
12. Dual regulation of the actin-myosin interaction in adrenal medullary actomyosin.
13. Characterization of caldesmon and myosin light chain kinase from arterial smooth muscle.
14. Isolation of the 35 kDa functional fragment of -caldesmon.
15. Role of tropomyosin in the actin-filamin interaction.
16. Regulation of the tree-dimentional contraction by caldesmon.
17. Expression of - and -caldesmons during phenotype chage of smooth muscle cells. Less
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Report
(3 results)
Research Products
(23 results)
