Acylphosphatase Levels In Alzheimer’s Disease Cultured Skin Fibroblasts

Abstract

Alzheimer’s disease (AD) is a degenerative disorder of the central nervous system which causes progressive cognitive decline during mid to late adult life. The primary causes of AD have not yet been identified. Mutated genes have been located on chromosomes 21,14, and 1, leading to the early onset familial form of the disease (EOFAD) (Shellenberg, 1995; Sorbi, 1993). The first presenile AD gene encoding for β-amyloid precursor protein (APP) was identified in 1991 (Goate et al., 1991). The most frequent pathogenic mutation in exon 17, a Val-Ile substitution at codon 717, has been described in more than 10 families (Levy-Lahad et al., 1996). The largest portion of early onset FAD cases have been associated with mutations in Presenilin 1 (PS1) gene and Presenilin 2 (PS2) gene (Van Broeckhoven, 1995; Rogaev et al., 1995; Levy-Lahad et al., 1995). Fibroblasts from patients and pre-symptomatic carriers of mutations in PS1 and PS2 contain increased amounts of Aβ 1-42 peptide (Scheuner et al., 1996). Moreover, the allele E4 of APOE gene has been associated with increased risk for late-onset familial form of AD (Saunders et al., 1993). Apolipoprotein E is the first identified genetic susceptibility factor for sporadic AD. The familial AD form account for 10% of all AD cases (Van Broeckhoven, 1995).