Project/Area Number |
03833033
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
分子細胞生物学
|
Research Institution | Fukuoka University |
Principal Investigator |
ODA Kimimitsu Fukuoka University School of Medicine, Associate professor, 医学部, 助教授 (10122681)
|
Co-Investigator(Kenkyū-buntansha) |
FUJIWARA Toshiyuki Fukuoka University School of Medicine, Assistant professor, 医学部, 助手 (80190099)
MISUMI Yoshio Fukuoka University School of Medicine, Assistant professor, 医学部, 助手 (10148877)
|
Project Period (FY) |
1991 – 1992
|
Project Status |
Completed (Fiscal Year 1992)
|
Budget Amount *help |
¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 1992: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1991: ¥800,000 (Direct Cost: ¥800,000)
|
Keywords | Furin / Golgi apparatus / Proalbuimin / Pro-C3 / Proteolytic processing / Calcium-dependent protease / Plasma protein precursor / Secretion / プロセシング酵素 / カルシウム要求性 / 血漿蛋白質前駆体 / ブレフェルジンA / 初代培養ラット肝細胞 / フュ-リン / 補体成分3前駆体 / カルシウム依存性プロテア-ゼ / トランスフェクション / 部位特異的突然変異法 |
Research Abstract |
1. Furin is found to be localized at the Golgi apparatus and enhance the cleavage of both pro-albumin and the proform of the third component of complement (C3) into mature albumin and C3, when coexpressed in the COS cells either with proalbumin or with pro-C3. In this study we further showed that the purified soluble furin from which the putative trans-membrane and cytoplasmic tail were deleted, is able to convert the precursors into mature proteins in vitro, suggesing that furin is a good candidate a long-sought processing protease at the Golgi apparatus. 2. When hepatocytes or HepG2 cells were cultured under the conditions where intracellular calcium ion was depleted, proalbumin and pro-C3 were found to be secreted instead of mature proteins. The precursor of the fourth component of complement was also secreted into the medium from the calcium-depleted HepG2 cells. These results suggest that calcium ion-dependent protease is involved in the processing of plasma protein precursors.
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