Possible role of recombinant disintegrin encoded by human-ADAM7 in glucose uptake of 3T3-L1 adipocytes

• Main Authors: Chiang, Ping-Lun, 江秉倫
• Other Authors: 劉鴻文
• Format: Others
• Language: zh-TW
• Published: 2007
• Online Access: http://ndltd.ncl.edu.tw/handle/55992438145886279022

碩士 === 國防醫學院 === 生物及解剖學研究所 === 95 === In previous studies, we identified GP-83, a glycoprotein that was secreted by human epididymis and conjugated to sperm in corpus of epididymis during maturation. Comparing with the known sequences, cDNA sequence of GP-83 exhibited significant homology to monkey ADAM7. Thus, we designated the sequence as human ADAM7. ADAM families, a novel family of transmembrane proteins that contain a disintegrin and metalloprotease domain. Disintegrins are specific ligands of integrin, a major family of cell adhesive molecules that is involved in many signal transduction pathways, and mediates cell recognition and adhesion. Recent studies reveal that snake venom-derived disintegrin may inhibit adipogenesis. In a pilot study, we induced insulin-resistant rats (blood sugar above 150 mg/ ml) by high calories chow and 3% milk. The blood sugar of the rats was decreased and remained within normal level after one intraperitoneal administration of recombinant disintegrin. However, serum insulin and the body weight did not reveal significant difference. This study further investigated possible effect of recombinant disintegrin on glucose uptake in 3T3-L1 adipocytes. Recombinant disintegrin was prepared in E. coli and purified by pull down assay using TALON Resin metal ion. 3T3-L1 preadipocytes were successfully induced into adipocytes by insulin and Sterol-ester (SE). However, recombinant disintegrin did not significantly increase the glucose uptake in 3T3-L1 adipocytes. Since recombinant disintegrin was prepared in E. coli, possible effect of post-translation modification on the function of recombinant disintegrin need to be verified.