IMAGING THE DIMERATION OF BACE IN HELA CELLS
Cleavage of the amyloid precursor protein CAPP) by the aspartyl protease β-site APP-cleaving enzyme (BACE) is the first step in the generation of the amyloid β - peptide. the major constituent of senile plaque in the brain of Alzheimers disease patients. Using blue native gel electrophoresis it has been found that BACE exists as a homodimer, however, it is currently unknown whether in living cells BACE forms homodimer. We addressed this issue using confocal microscopy and fluorescence resonance energy transfer (FRET) to monitor dimenzanon of BACE in intact living cells. We constructed a pair of GFP mutants (modified CFP and YFP, named mCerulean and mCitrine respectively) fusion proteins, mCerulean-and mCitrine-tagged BACE. named BACE/CFP and BACE/ YFP respectively. FRET between CFP-and YFP-tagged BACE was detected by acceptor photobleaching method. The results showed that the BACE could form homodimer in Hela cells.
β- site APP cleaving enzyine(BACE) dimerization FRET acceptor photobleaching
Jinling Lu Zhihong Zhang Jun Chu Jie Yang Shaoqun Zeng Qingming Luo
Wuhan National Laboratory for Optoelectronics-Key Laboratory of Biomedical Photonics of Ministry of Education, Huazhong University of Science and Technology, Wuhan 430074, China
国际会议
The 4th International Forum on Post-genome Technologies(4IFPT)(第四届国际后基因组生命科学技术学术论坛)
杭州
英文
506-508
2006-09-25（万方平台首次上网日期，不代表论文的发表时间）