Neuron
Volume 14, Issue 2, February 1995, Pages 457-466
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Article
Dominant and differential deposition of distinct β-amyloid peptide species, AβN3(pE), in senile plaques

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Abstract

We analyzed an amino-terminal modification of β-amyloid (Aβ) peptide in brain, using anti-Aβ antibodies that distinguish distinct molecular species. Examination of cortical sections from 28 aged individuals with a wide range in senile plaque density revealed that a molecular species distinct from the standard Aβ is deposited in the brain in a dominant and differential manner. This modified Aβ peptide (AβN3(pE)) starts at the 3rd amino-terminal residue of the standard Aβ, glutamate, converted to pyroglutamate through intramolecular dehydration. Because plaques composed of AβN3(pE) are present in equivalent or greater densities than those composed of standard Aβ bearing the first aminoterminal residue (AβN1) and because deposition of the former species appears to precede deposition of the latter, as confirmed with specimens from Down's syndrome patients, the processes involved in AβN3(pE) production and retention may play an early and critical role in senile plaque formation.

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