Title: Presenilins
Literature References: Integral membrane proteins required for the proteolytic processing of the amyloid precursor protein (APP) to yield amyloid-b peptide (Ab), q.v. Missense mutations in the presenilin genes result in the production of an abnormal form of Ab which is the major component of the amyloid plaques deposited in the brains of patients with Alzheimer's disease (AD). Highly hydrophobic, presenilin 1 (PS1) and its homolog presenilin 2 (PS2), consist of 463 and 448 amino acid residues, respectively. PS1 is believed to be a catalytic subunit of g-secretase. Thought to have 7 or 8 transmembrane domains that span the membranes of the endoplasmic reticulum, nuclear envelope and Golgi apparatus. Identification of the gene for PS1: R. Sherrington et al., Nature 375, 754 (1995); for PS2: E. I. Rogaev et al., ibid. 376, 775 (1995). Characterization of PS1 and distribution in human and rodent brain: G. A. Elder et al., J. Neurosci. Res. 45, 308 (1996). Structural study: N. N. Dewji et al., Proc. Natl. Acad. Sci. USA 101, 1057 (2004). Review of structure, possible physiological functions, and role in Alzheimer's disease: C. Haass, B. De Strooper, Science 286, 916-919 (1999); P. E. Fraser et al., Biochim. Biophys. Acta 1502, 1-15 (2000).

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