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J Biol Chem, Vol. 273, Issue 21, 12817-12826, May 22, 1998
From the The cortical deposition of A
Dramatic Aggregation of Alzheimer A
by Cu(II) Is Induced by
Conditions Representing Physiological Acidosis
,,,,,
Department of Psychiatry and Genetics and
Aging Unit and the § Department of Neurology and Genetics
and Aging Unit, Massachusetts General Hospital, Harvard Medical School,
Boston, Massachusetts 02114
is an event that
occurs in Alzheimer's disease, Down's syndrome, head injury, and
normal aging. Previously, in appraising the effects of different
neurochemical factors that impact upon the solubility of A, we
observed that Zn2+ was the predominant bioessential
metal to induce the aggregation of soluble A at pH 7.4 in
vitro and that this reaction is totally reversible with
chelation. We now report that unlike other biometals tested at maximal
biological concentrations, marked Cu2+-induced aggregation
of A1-40 emerged as the solution pH was lowered from
7.4 to 6.8 and that the reaction was completely reversible with either
chelation or alkalinization. This interaction was comparable to the
pH-dependent effect of Cu2+ on insulin
aggregation but was not seen for aprotinin or albumin. A1-40 bound three to four Cu2+ ions when
precipitated at pH 7.0. Rapid, pH-sensitive aggregation occurred at low
nanomolar concentrations of both A1-40 and
A1-42 with submicromolar concentrations of
Cu2+. Unlike A1-40, A1-42
was precipitated by submicromolar Cu2+ concentrations at pH
7.4. Rat A1-40 and histidine-modified human
A1-40 were not aggregated by Zn2+,
Cu2+, or Fe3+, indicating that histidine
residues are essential for metal-mediated A assembly. These results
indicate that H+-induced conformational changes unmask a
metal-binding site on A that mediates reversible assembly of the
peptide. Since a mildly acidic environment together with increased
Zn2+ and Cu2+ are common features of
inflammation, we propose that A aggregation by these factors may be
a response to local injury. Cu2+, Zn2+, and
Fe3+ association with A explains the recently reported
enrichment of these metal ions in amyloid plaques in Alzheimer's
disease.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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