W. Wasco et al., ISOLATION AND CHARACTERIZATION OF APLP2 ENCODING A HOMOLOG OF THE ALZHEIMERS ASSOCIATED AMYLOID BETA-PROTEIN PRECURSOR, Nature genetics, 5(1), 1993, pp. 95-100
Familial Alzheimer's disease (FAD) is a genetically heterogeneous diso
rder that includes a rare early-onset form linked to mutations in the
amyloid b protein precursor (APP) gene. Clues to the function of APP d
erive from the recent finding that it is a member of a highly conserve
d protein family that includes the mammalian amyloid precursor-like pr
otein (APLP1) gene which maps to the same general region of human chro
mosome 19 linked to late-onset FAD. Here we report the isolation of th
e human APLP2 gene. We show that APLP2 is a close relative of APP and
exhibits a very similar pattern of expression in the brain and through
out the body. Like APP, APLP2 contains a cytoplasmic domain predicted
to couple with the GTP-binding protein G(o) indicating that it may be
an additional cell surface activator of this G protein.