Journal
JOURNAL OF CLINICAL INVESTIGATION
Volume 115, Issue 5, Pages 1121-1129Publisher
AMER SOC CLINICAL INVESTIGATION INC
DOI: 10.1172/JCI200525100
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Funding
- NIA NIH HHS [P01 AG010491-14, P01 AG010491, P01 AG10491] Funding Source: Medline
- NINDS NIH HHS [R01 NS41017, R01 NS041017] Funding Source: Medline
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For approximately 80 years following Alzheirner ' s description of the disease that bears his name, a gulf divided researchers who believed that extracellular deposits of the amyloid beta (A beta) peptide were pathogenic from those who believed that the deposits were secondary detritus. Since 1990, the discoveries of missense mutations in the AP peptide precursor (APP) and the APP-cleaving enzyme presenifin 1 (PS1) have enabled much progress in understanding the molecular, cellular, and tissue pathology of the aggregates that accumulate in the interstices of the brains of patients with autosomal dominant familial Alzheimer disease (AD). Clarification of the molecular basis of common forms of AD has been more elusive. The central questions in common AD focus on whether cerebral and cerebrovascular A beta accumulation is (a) a final neurotoxic pathway, common to all forms of AD; (b) a toxic by-product of an independent primary metabolic lesion that, by itself, is also neurotoxic; or (c) an inert by-product of an independent primary neurotoxic reaction. Antiamyloid medications are entering clinical trials so that researchers can evaluate whether abolition of cerebral amyloidosis can mitigate, treat, or prevent the dementia associated with common forms of AD. Successful development of antiamyloid medications is critical for elucidating the role of A beta in common AD.
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