May 26, 2014 Journal article Open Access

Kummer, Markus P; Heneka, Michael T

DCAT Export

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    <dct:description>&lt;p&gt;Alzheimer&amp;rsquo; s disease pathology is closely connected to the processing of the amyloid precursor protein (APP)&amp;nbsp;resulting in the formation of a variety of amyloid-beta (A&amp;beta; ) peptides. They are found as insoluble aggregates in&amp;nbsp;senile plaques, the histopathological hallmark of the disease. These peptides are also found in soluble, mostly&amp;nbsp;monomeric and dimeric, forms in the interstitial and cerebrospinal fluid. Due to the combination of several&amp;nbsp;enzymatic activities during APP processing, A&amp;beta;&amp;nbsp; peptides exist in multiple isoforms possessing different N-termini&amp;nbsp;and C-termini. These peptides include, to a certain extent, part of the juxtamembrane and transmembrane domain&amp;nbsp;of APP. Besides differences in size, post-translational modifications of A&amp;beta; &amp;ndash;&amp;nbsp; including oxidation, phosphorylation,&amp;nbsp;nitration, racemization, isomerization, pyroglutamylation, and glycosylation &amp;ndash;&amp;nbsp; generate a plethora of peptides with&amp;nbsp;different physiological and pathological properties that may modulate disease progression.&lt;/p&gt;</dct:description>
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