Investigation of the Potential Role of FKBP12 in APP Processing

• Main Authors: Tzung-Harn Hsieh, 謝宗涵
• Other Authors: Fan-Lu Kung
• Format: Others
• Language: zh-TW
• Published: 2009
• Online Access: http://ndltd.ncl.edu.tw/handle/48161009305785840359

碩士 === 國立臺灣大學 === 藥學研究所 === 97 === Previous studies indicated some chaperones could interact with AICD, such as peptidyl-prolyl cis-trans isomerase (PPIase) Pin1. Pin1 has been reported to be involved in the amyloidogenic APP processing. Another PPIase FK506-binding protein 12 (also one of immunophilins) has been shown to interact with AICD via various biochemical approaches. Our results showed that overexpression of FKBP12 altered the ratio of C83 to C99 in HEK293T. Another FK506 binding protein 52 is also under investigation. Here we present FKBP12 may regulate APP processing; FKBP12 might accelerate APP undergo amyloidogenic pathway when APPThr668 was phosphorylated. However, FKBP52 might also alter the expression level of C83, C99, and their relative ratio, but it would accelerate APP undergo non-amyloidogenic pathway during the same conditions. FKBP52 showed neuroprotection ability, whether this effect was due to FK506 still under investigation.