APP669-711 acetate is an N-terminally extended amyloid β peptide ( Aβ (-3)-40) that forms amyloid fibrils and co-deposits with Aβ in brain plaques, and also serves as a plasma biomarker for assessing brain Aβ load. APP669-711 acetate can be used in research on Alzheimer's disease [1] [2] [3].
In Vitro, APP669-711 acetate is produced in HEK293A cells by APPwt and c102 in a DAPT-sensitive manner, is upregulated by ADAMTS4, and is abolished by the Swedish mutation[1]. APP669-711 acetate production in HEK293A cells is enhanced to a greater extent by ADAMTS5 co-expression than by ADAMTS4, requires the ADAMTS5 Sp domain, and is abolished by the E411A catalytic mutation or an ADAMTS5 inhibitor; exogenous ADAMTS5 conditioned medium does not significantly increase APP669-711 acetate[3].
References:
[1]. Matsuzaki M, et al. ADAMTS4 is involved in the production of the Alzheimer disease amyloid biomarker APP669-711. Molecular psychiatry. 2023 Apr;28(4):1802-1812.
[2]. Kaneko N, et al. Novel plasma biomarker surrogating cerebral amyloid deposition. Proceedings of the Japan Academy. Series B, Physical and biological sciences. 2014;90(9):353-64.
[3]. Yokoyama M, et al. Identification of ADAMTS5 as APP-Cleaving Enzyme at the APP669 Site. FASEB journal: official publication of the Federation of American Societies for Experimental Biology. 2026 Apr 15;40(7):e71701.
In Vitro, APP669-711 acetate is produced in HEK293A cells by APPwt and c102 in a DAPT-sensitive manner, is upregulated by ADAMTS4, and is abolished by the Swedish mutation[1]. APP669-711 acetate production in HEK293A cells is enhanced to a greater extent by ADAMTS5 co-expression than by ADAMTS4, requires the ADAMTS5 Sp domain, and is abolished by the E411A catalytic mutation or an ADAMTS5 inhibitor; exogenous ADAMTS5 conditioned medium does not significantly increase APP669-711 acetate[3].
References:
[1]. Matsuzaki M, et al. ADAMTS4 is involved in the production of the Alzheimer disease amyloid biomarker APP669-711. Molecular psychiatry. 2023 Apr;28(4):1802-1812.
[2]. Kaneko N, et al. Novel plasma biomarker surrogating cerebral amyloid deposition. Proceedings of the Japan Academy. Series B, Physical and biological sciences. 2014;90(9):353-64.
[3]. Yokoyama M, et al. Identification of ADAMTS5 as APP-Cleaving Enzyme at the APP669 Site. FASEB journal: official publication of the Federation of American Societies for Experimental Biology. 2026 Apr 15;40(7):e71701.