γ-secretase-dependent proteolysis of transmembrane domain of amyloid precursor protein: successive tri- and tetrapeptide release in amyloid β-protein production

Clicks: 338
ID: 144956
2012
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Abstract
γ-Secretase cleaves the carboxyl-terminal fragment (βCTF) of APP not only in the middle of the transmembrane domain (γ-cleavage), but also at sites close to the membrane/cytoplasm boundary (ε-cleavage), to produce the amyloid β protein (Aβ) and the APP intracellular domain (AICD), respectively. The AICD49–99 and AICD50–99 species were identified as counterparts of the long Aβ species Aβ48 and Aβ49, respectively. We found that Aβ40 and AICD50–99 were the predominant species in cells expressing wild-type APP and presenilin, whereas the production of Aβ42 and AICD49–99 was enhanced in cells expressing familial Alzheimer’s disease mutants of APP and presenilin. These long Aβ species were identified in cell lysates and mouse brain extracts, which suggests that ε-cleavage is the first cleavage of βCTF to produce Aβ by γ-secretase. Here, we review the progress of research on the mechanism underlying the proteolysis of the APP transmembrane domain based on tri- and tetrapeptide release.
Reference Key
takami2012international-secretase-dependent Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Mako Takami;Satoru Funamoto
Journal advanced biomedical research
Year 2012
DOI
10.1155/2012/591392
URL
http://dx.doi.org/10.1155/2012/591392
Keywords
neurosciences biological psychiatry neuropsychiatrygeriatrics

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