| Project/Area Number |
18590873
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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 |
Respiratory organ internal medicine
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| Research Institution | Kinki University |
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Principal Investigator |
MUNAKATA Hiroshi Kinki University, Sch Med, Professor (90111294)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUDA Toshirou Kinki University, Hospital, Lecturer (80411586)
HAYAKAWA Sumio Hokkaidou University, 遺伝子病制御研究所, Assist Prof (00368292)
YOSHIDA Koji Kinki University, Sch Med, Associate Professor (60230736)
SAITO Akio Kinki University, Sch Med, Lecturer (40153788)
佐藤 真弓 近畿大学, 医学部, 助手 (90388512)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,830,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥330,000)
Fiscal Year 2007: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2006: ¥2,400,000 (Direct Cost: ¥2,400,000)
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| Keywords | Proteome / Myofibroblast / Activation / 繊維化 / transforming growth factor |
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| Research Abstract |
Previously we showed that the expression of integrin aω, β1, β3 in MRC-5 cells increased by TGF-β. Increased expression of fibronectin and focal adhesion kinase was also shown. Here, we show the results of proteomics analysis of activation and inactivation of myofibroblast cell line, MRC-5. Transforming growth factor-b stimulated MRC-5 cell extract was compared with that from non-stimulated cells. Several proteins differentially expressed between stimulated and non-stimulated cells including actin-bindin proteins and molecular chaperones.
As previously reported the culture supernatant of A-549 inactivates myofibroblast MRC-5. RNA was obtained from MRC-5 cells after inactivation by the conditioned medium of A-549 and the expressions were analyzed using low density arrays. Expression of some proteins concerned in cell protrusions was increased. The cells treated with forskolin were subjected to proteome analysis. Inceased expression of actin capping protein was observed.
These results, together with previous our findings, suggests that signal transduction mediated by interantions between extracellular matrix and integrins are important in activation and inactivation of myofibroblasts.
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