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γ  -Secretase cleaves the carboxyl-terminal fragment (  β  CTF) 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 (A  β  ) and the APP intracellular domain (AICD), respectively. The AICD49–99 and AICD50–99 species were identified as counterparts of the long A  β   species A  β  48 and A  β  49, respectively. We found that A  β  40 and AICD50–99 were the predominant species in cells expressing wild-type APP and presenilin, whereas the production of A  β  42 and AICD49–99 was enhanced in cells expressing familial Alzheimer's disease mutants of APP and presenilin. These long A  β   species were identified in cell lysates and mouse brain extracts, which suggests that   ε  -cleavage is the first cleavage of   β  CTF to produce A  β   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.

international journal of alzheimer's disease

<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="M1"><mml:mrow><mml:mi>γ</mml:mi></mml:mrow></mml:math>-Secretase-Dependent Proteolysis of Transmembrane Domain of Amyloid Precursor Protein: Successive Tri- and Tetrapeptide Release in Amyloid<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="M2"><mml:mrow><mml:mi>β</mml:mi></mml:mrow></mml:math>-Protein Production

γ-Secretase-Dependent Proteolysis of Transmembrane Domain of Amyloid Precursor Protein: Successive Tri- and Tetrapeptide Release in Amyloidβ-Protein Production