title: Mitochondrial translocation of amyloid precursor protein and its cleaved products: relevance to mitochondrial dysfunction in Alzheimer's disease.
abstract: Alzheimer's disease (AD) is a multifactorial disorder. Mitochondrial dysfunction is one of the key characteristics of AD pathogenesis. However, the mechanisms underlying the progression of mitochondrial impairment during AD are not clear. Growing evidence suggests a causative role for intracellular accumulation of amyloid precursor protein (APP) and its proteolytic products in the pathogenesis of AD. Furthermore, APP possesses several domains including a mitochondrial targeting sequence. Recent literature suggests that mitochondrial localization of full length APP and its C-terminal proteolytically cleaved derivative beta amyloid (Abeta) are associated with the mitochondrial dysfunction. Here, we review the nature of mitochondrial localization of APP and Abeta and their pathological implications in AD mitochondrial dysfunction.
authors: Department of Animal Biology, School of Veterinary Medicine, University ofPennsylvania, Philadelphia, PA 19104, USA. ann1234@vet.upenn.edu
authors: Hindupur K
authors: HK
authors: Anandatheerthavarada
authors: Latha
authors: L
authors: Devi
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000503:physiopathology; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001057:Apolipoproteins E / Q000378:metabolism; D001921:Brain / Q000378:metabolism* / Q000503:physiopathology; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D028361:Mitochondrial Diseases / Q000378:metabolism* / Q000503:physiopathology; D017434:Protein Structure, Tertiary / Q000502:physiology; D021381:Protein Transport / Q000502:physiology
chemical_list: D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D001057:Apolipoproteins E