Physicochemical mechanism on formation and metabolism of HDL particles by apolipoproteins

2016 Fiscal Year Final Research Report

• Project/Area Number: 25293006
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Physical pharmacy
• Research Institution: Kyoto Pharmaceutical University (2016); The University of Tokushima (2013-2015)
• Principal Investigator: Saito Hiroyuki 京都薬科大学, 薬学部, 教授 (60300919)
• Co-Investigator(Kenkyū-buntansha): 笠原 二郎 徳島大学, 大学院医歯薬学研究部, 准教授 (10295131) ; 長尾 耕治郎 徳島大学, ヘルスバイオサイエンス研究部, 助教 (40587325)
• Co-Investigator(Renkei-kenkyūsha): AKAJI Kenichi 京都薬科大学, 薬学部, 教授 (60142296) ; OTAKA Akira 徳島大学, 大学院医歯薬学研究部, 教授 (20201973) ; OKAMURA Emiko 姫路獨協大学, 薬学部, 教授 (00160705) ; KOBAYASHI Norihiro 神戸薬科大学, 薬学部, 教授 (90205477) ; KITAGAWA Shuji 神戸薬科大学, 薬学部, 教授 (00108911) ; MICHIKAWA Makoto 名古屋市立大学, 医学研究科, 教授 (40270912)
• Project Period (FY): 2013-04-01 – 2017-03-31
• Keywords: アポリポタンパク質 / HDL / コンフォメーション / 抗体 / アミロイド / 脂質膜 / 糖鎖

Outline of Final Research Achievements

In this study, we have focused on the exchangeable helical apolipoproteins such as apoA-I and apoE that regulate cholesterol metabolism in plasma and brain. We mainly performed the following three projects: (1) fluorescence analyses of dynamic conformations of apolipoproteins between lipid-free and HDL-bound forms, (2) development of the novel method to detect HDL formation based on physicochemical studies of ABCA1-mediated formation of HDL particles, and (3) physicochemical mechanism of gene mutation-induced structural disorder and dysfunction of apolipoproteins. Our results provide novel and useful insights to understand structural basis for apolipoprotein-mediated HDL formation and metabolism.

Free Research Field

生物物理化学