Grant-in-Aid for Overseas Scientific Survey.
|Research Institution||Niigata University|
ONO Teruo Niigata Univ.Sch.of Med., Professor, 医学部, 教授 (00000927)
榊原 順 新潟大学, 医学部, 助手 (90242403)
藤井 博 新潟大学, 医学部, 助教授 (90165340)
井関 尚一 金沢大学, 医学部, 教授 (50167251)
鈴木 利光 福島県立医科大学, 教授 (80018952)
近藤 尚武 東北大学, 医学部, 教授 (20004723)
JUDITH Storc Rutgers大学, 栄養学部, 助教授
STORCH Judit Rutgers大学, 栄養学部, 助教授
SUZUKI Toshimitsu Fukushima Medical College, Professor
ISEKI Shoichi Kanazawa Univ.Sch.of Med., Professor
STORCH Judith Rutgers University, Associate Professor
KONDO Hisatake Tohoku Univ.Sch.of Med., Professor
SAKAKIBARA Jun Niigata Univ.Sch.of Med., Research Associate
FUJII Hiroshi Niigata Univ.Sch.of Med., Associate Professor
|Project Fiscal Year
1993 – 1994
Completed(Fiscal Year 1994)
|Budget Amount *help
¥6,500,000 (Direct Cost : ¥6,500,000)
Fiscal Year 1994 : ¥3,000,000 (Direct Cost : ¥3,000,000)
Fiscal Year 1993 : ¥3,500,000 (Direct Cost : ¥3,500,000)
|Keywords||Fatty Acid-Binding Protein (FABP) / H-FABP / C-FABP / I-FABP / I-15P / Diabetes Mellitus / Ischaemic Intestinal Diseases / Fluorescent Fatty Acid / 脂肪酸結合蛋白(FABP) / 糖尿病 / 虚血性腸疾患 / 蛍光脂肪酸プローブ / L-FABP / 心筋梗塞 / 脂肪酸 / ステロイド産生臓器|
We have studied on functional roles of cellular fatty acid-binding proteins (FABPs) in the following aspects.
(1) Transfer mechanism of FABP bound-fatty acids to membranes :
Using an in vitro fluorescence energy transfer assay, we presented the evidence that H-FABP and L-FABP bound-fatty acids are transferred to membranes through different mechanism. Fatty acids from H-FABP was transferred by collisional interaction, while the rate limiting step from L-FABP was the dissociation rate of fatty acids to aqueous medium.
(2) A new FABP (C-FABP) from rat skin :
We have purified a new subtype of H-FABP from rat skin and cloned this protein. The deduced amino acid sequence of the cDNA clone comprises residues yielding a molecular mass for the polypeptide of 15 kDa and the primary structure is homologus to H-FABP family proteins. Interestingly, it has six cysteines and two intramolecular disulfide bridges are present. This is the first presentation of disulfide formed protein among FABPs superfamily. Three dimensional structure of this new type of FABP may afford a new sight of functional roles of this protein family in the future.
(3) Regulatory mechanism of H-FABP expression in aorta :
We have analyzed the H-FABP expression in diabetic rat aorta and provided the evidence that the H-FABP gene in aorta is specifically and uniquely regulated by insulin when compared to the H-FABP expression in heart tissue. Insulin regulated H-FABP expression in aorta may be involved in diabetic complications of blood vessels.
(4) Clinical application of I-FABP :
Taking the advantage of specific expression of I-FABP limited in intestinal tissue, we have applied the I-FABP as a diagnostic tool. We have showed that the I-FABP is released into the circulation in the acute phase of intestinal ischaemia. Accordingly, the measurement of I-FABP in serum can be used in establishing the diagnosis of ischaemic intestinal diseases.