2026-04-03T20:25:26Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/648902025-12-04T21:12:13Zcom_2072_1057col_2072_478781col_2072_478917

00925njm 22002777a 4500 dc Franco Fernández, Rafael author Navarro Brugal, Gemma author Martínez-Pinilla, Eva author Moreno Guillén, Estefanía author 2015-04-10T13:33:39Z 2015-04-10T13:33:39Z 2014-12-29 2015-04-10T13:33:40Z The amyloid precursor protein (APP) is mainly known for being the precursor of the ß-amyloid peptide, which accumulates in plaques found in the brain of Alzheimer's disease patients. Expression in different tissues and the degree of sequence identity among mammals indicate an essential and non-tissue specific physiological function. APP is anchored to the membrane and displays a single C-terminal intracellular domain and a longer N-terminal extracellular domain. The basic biochemical properties and the scattered data on research, not related to production of beta-amyloid peptide, suggest that the protein and the molecules resulting from APP proteolytic cleavage may act as adhesion factors, enzymes, hormones/neurotransmitters and/or protease inhibitors. APP deserves to be known for its quite notable properties and its physiological role(s). Malaltia d'Alzheimer Expressió gènica Proteïnes de membrana Alzheimer's disease Gene expression Membrane proteins Amyloid Beta Precursor Protein: Proper Credit for the Basic Biochemical Properties of the Most Studied Protein in the 21st Century