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The βA4 amyloid precursor protein binding to copper
Author(s) -
Hesse Lars,
Beher Dirk,
Masters Colin L.,
Multhaup Gerd
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00658-x
Subject(s) - chemistry , amyloid precursor protein , binding site , laminin , biochemistry , transmembrane domain , cysteine , extracellular , copper , binding protein , transmembrane protein , extracellular matrix , amino acid , alzheimer's disease , receptor , enzyme , medicine , disease , organic chemistry , pathology , gene
Previously it has been shown that the extracellular domain of transmembrane βA4 amyloid precursor protein (APP) includes binding sites for zine(II) and for molecules of the extracellular matrix such as collagen, laminin and the heparin sulfate chains of proteoglycans (HSPGs). Here we report that APP also binds copper ions. A copper type II binding site was located within residues 135–155 of the cysteine‐rich domain of APP 695 which is present in all eight APP splice isoforms known so far. The two essential histidines in the type II copper binding site of APP are conserved in the related protein APLP 2 . Copper(II) binding is shown to inhibit homophilic APP binding. The identification of a copper(II) binding site in APP suggests that APP and APLP 2 may be involved in electron transfer and radical reactions.