[HTML][HTML] Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice
T Itoh, T Ikeda, H Gomi, S Nakao, T Suzuki… - Journal of Biological …, 1997 - ASBMB
The β-amyloid peptide, which forms extracellular cerebral deposits in Alzheimer's disease, is
derived from a large membrane-spanning glycoprotein referred to as the β-amyloid
precursor protein (APP). The APP is normally cleaved within the β-amyloid region by a
putative proteinase (α-secretase) to generate large soluble amino-terminal derivatives of
APP, and this event prevents the β-amyloid peptide formation. It has been suggested that the
gelatinase A (matrix metalloproteinase 2, a 72-kDa type IV collagenase) may act either as α …
derived from a large membrane-spanning glycoprotein referred to as the β-amyloid
precursor protein (APP). The APP is normally cleaved within the β-amyloid region by a
putative proteinase (α-secretase) to generate large soluble amino-terminal derivatives of
APP, and this event prevents the β-amyloid peptide formation. It has been suggested that the
gelatinase A (matrix metalloproteinase 2, a 72-kDa type IV collagenase) may act either as α …
