Recombinant Neural Protein PrP Can Bind with Both Recombinant and Native Apolipoprotein E In Vitro

作     者：Chen GAO~1 Yan-Jun LEI~(1,2) Jun HAN~1 Qi SHI~1 Lan CHEN~(1,3) Yan GUO~(1,4) Yong-Jun GAO~1 Jian-Ming CHEN~1 Hui-Ying JIANG~1 Wei ZHOU~1 Xiao-Ping DONG~1* 1 State Key Laboratory for Infectious Disease Prevention and Control,National Institute for Viral Disease Control and Prevention,Chinese Center for Disease Control and Prevention,Beijing 100052,China 2 School of Medicine,Xi'an Jiaotong University,Xi'an 710061,China 3 National Laboratory of Medical Molecular Biology,Institute of Basic Medical Science,Chinese Academy of Medical Sciences and Peking Union Medical College,Beijing 100005,China 4 College of Science and Veterinary Medicine,Northwest Agriculture and Forest University,Yangling 712100,China 

作者机构：State Key Laboratory for Infectious Disease Prevention and Control National Institute for Viral Disease Control and Prevention Chinese Center for Disease Control and PreventionBeijing 100052 China School of Medicine Xi'an Jiaotong UniversityXi'an 710061 China National Laboratory of Medical Molecular Biology Institute of Basic Medical Science Chinese Academy of Medical Sciences and Peking Union Medical CollegeBeijing 100005 China College of Science and Veterinary Medicine Northwest Agriculture and Forest UniversityYangling 712100 China 

出 版 物：《Acta Biochimica et Biophysica Sinica》 (生物化学与生物物理学报(英文版))

年 卷 期：2006年第38卷第9期

页      面：593-601页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 08[工学] 09[农学] 071007[理学-遗传学] 0901[农学-作物学] 0836[工学-生物工程] 090102[农学-作物遗传育种] 

基　　金：国家自然科学基金 国家863计划 国家科技支撑计划项目 欧盟项目 

主　　题：prion disease PrP apolipoprotein E protein interaction caveolae-like domain 

摘      要：The most essential and crucial step during the pathogenesis of transmissible spongiformencephalopathy is the conformational change of cellular prion protein （PrPC） to pathologic isoform (PrPSc).Alot of data revealed that caveolae-like domains （CLDs） in the cell surface were the probable place where theconversion of PrP proteins *** E （ApoE） is an apolipoprotein which is considered toplay an important role in the development of Alzheimer s disease and other neurodegenerative diseases byforming protein complex through binding to the receptor located in the clathrin-coated pits of the cell *** this study,a 914-bp cDNA sequence encoding human ApoE3 was amplified from neuroblastoma cell *** human ApoE isomers were expressed and purified from Escherichia ***-specificantiserum was prepared by immunizing rabbits with the purified ***/His pull-down assay,immunoprecipitation and ELISA revealed that three full-length ApoE isomers interact with the recombinantfull-length PrP protein in *** regions corresponding to protein binding were mapped in the N-terminalsegment of ApoE （amino acid 1-194） and the N-terminal of PrP （amino acid 23-90）.Moreover,the recombinantPrP showed the ability to form a complex with the native ApoE from liver *** data provided directevidence of molecular interaction between ApoE and *** also supplied scientific clues for assessing thesignificance of CLDs on the surface of cellular membrane in the process of conformational conversion fromPrPCto PrPScand probing into the pathogenesis of transmissible spongiform encephalopathy.