Expression and analysis of heparin‐binding regions of the amyloid precursor protein of Alzheimer's disease

FEBS Letters

Galatis, Denise³  Clarris, Heidi J³  Mok, Su San³  Beyreuther, Konrad²  Sawyer, William H¹  Masters, Colin L³  Cappai, Roberto³  Sberna, Gian³  Heffernan, Damien³  Small, David H³ 

[1]Department of Biochemistry and Molecular Biology, The University of Melbourne, Parkville, Victoria 3052, Australia

[2]The Center for Molecular Biology, The University of Heidelberg, D-6900 Heidelberg, Germany

[3]Department of Pathology, The University of Melbourne, Parkville, Victoria 3052, Australia

关键词: APP;    Heparin binding;    Alzheimer's disease;    Peptide;    Secondary structure;    Aβ;    the amyloid protein obtained from APP cleavage;    AD;    Alzheimer's disease;    APP;    amyloid precursor protein;    APP695;    the 695 amino acid isoform of the amyloid precursor protein;    HSPG(s);    heparan sulphate proteoglycan(s);    PMSF;    phenylmethylsulfonyl fluoride;    EDTA;    ethylenediaminetetraaceticacid disodium salt;    SDS-PAGE;    sodium dodecyl sulphate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(97)01146-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Deletion mutagenesis studies have suggested that there are two domains within APP which bind heparan sulphate. These domains have been cloned and expressed in the yeast Pichia pastoris. Both recombinant proteins bound to heparin. One domain (APP316–447) was further characterised by binding studies with peptides encompassing this region. Peptides homologous to APP316–346 and APP416–447 were found to bind heparin. Circular dichroism studies show that APP416–447 shifted towards an α-helical conformation in the presence of heparin. This study suggests that heparin-binding domains may lie within regions high in α-helical structure.

【 授权许可】

Unknown