作者: Sangram S. Sisodia , Gopal Thinakaran , Cornelia S. von Koch , Hilda H. Slunt , A. Jane I. Roskams
DOI: 10.1007/978-1-4899-0209-2_12
关键词: APLP1 、 Transmembrane protein 、 Amyloid precursor protein 、 APLP2 、 Complementary DNA 、 Cell biology 、 Transgene 、 Homology (biology) 、 Membrane glycoproteins 、 Biology
摘要: A principal pathological feature of Alzheimer’s disease is the deposition s-amyloid protein (As) in brain parenchyma.1–3 As, an ~4-kD polypeptide, derived from larger type I integral membrane glycoproteins, termed amyloid precursor proteins (APP).4–9 APP a member family homologous precursor-like (APLPs), including APLP110 and APLP2.11–13 APP, APLP1, APLP2 show considerable homology N-terminal cysteine-rich domain, cytoplasmic tail transmembrane sequences, but APLPs differ by conspicuous absence As region. homologues have also been identified C. elegans (apl-l)14 Drosophila (appl),15 these molecules lack region as well. Flies with deleted APPL gene are viable defective fast phototaxis response, behavior that partially rescued introduction human cDNA. The biological functions mammalian nervous system far clear, although several studies suggested play roles cell-cell or cell-matrix interactions,16–18 calcium hemostasis,19 growth promoting activities,20 formation/maintenance synapses vivo. 21 More recently, investigations cultured cells22 transgenic animals23 provided support to notion neuroprotective.