Axonal transport of British and Danish amyloid peptides via secretory vesicles 1 SEUNG-IL CHOI * , RUBEN VIDAL § , BLAS FRANGIONE * and EFRAT LEVY * ,† ,‡ ,|| ,2 * Departments of Pathology, † Psychiatry and ‡ Pharmacology, New York University School of Medicine, New York, New York, USA; § Indiana Alzheimer Disease Center, Indiana University School of Medicine, Indianapolis, Indiana, USA; and || Nathan Kline Institute, New York University School of Medicine, Orangeburg, New York, USA 2 Correspondence: Nathan Kline Institute, New York University School of Medicine, 140 Old Orangeburg Rd., Orangeburg, NY 10962, USA. E-mail: elevy@nki.rfmh.org <h3>SPECIFIC AIMS</h3> Amyloid peptides deposited in familial British and Danish neurodegenerative disorders (FBD and FDD, respectively) are generated by proteolytic processing of mutant forms of the precursor protein BRI 2 , ABriPP, and ADanPP. We have investigated endoproteolytic processing, subcellular localization, and normal biological function of wild-type and mutant forms of BRI 2 . <h3>PRINCIPAL FINDINGS</h3> 1. Proteolytic processing of BRI 2 Tissue culture cell lines were transiently transfected with amino-terminal myc epitope-tagged BRI 2 (wild-type British cDNA), BRI 2 -B (British variant of BRI 2 ), or BRI 2 -D (Danish variant of BRI 2 ) cDNAs.
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Axonal transport of British and Danish amyloid peptides via secretory vesicles
CHOI, SEUNG-IL; VIDAL, RUBEN; FRANGIONE, BLAS; LEVY, EFRAT
Follow The FASEB Journal
, Volume 18 (2): 373
Fed of American Socs for Experimental Biology – Feb 1, 2004
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