Evidence against a role for rare ADAM10 mutations in sporadic Alzheimer Disease

Guiqing Cai, Gil Atzmon, Adam C. Naj, Gary W. Beecham, Nir Barzilai, Jonathan L. Haines, Mary Sano, Margaret Pericak-Vance, Joseph D. Buxbaum

Research output: Contribution to journalArticlepeer-review

Abstract

The Alzheimer amyloid protein precursor (APP) is subject to proteolysis by ADAM10 and ADAM17, precluding the formation of Aβ. Recently, coding variations in ADAM10 resulting in altered function have been reported in familial Alzheimer disease (AD). The authors carried out a large-scale (n = 576: Controls, 271; AD, 305) resequencing study of ADAM10 in sporadic AD. The results do not support a significant role for ADAM10 mutations in AD. The results also make it clear that the careful examination of ancestry required in any case-control comparison is especially true with rare variations, where even a very small number of variations might form the basis of scientific conclusions.

Original languageEnglish
Pages (from-to)416-417.e3
JournalNeurobiology of Aging
Volume33
Issue number2
DOIs
StatePublished - Feb 2012
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by grants from the National Institute on Aging of the National Institutes of Health ( AG010491 and AG002219 , as well as pilot award to GC from the Mount Sinai Alzheimer disease Research Center / AG005138 ). The longevity study was supported by AG027734 , AG018728 , RR012248 , DK020541 , and RR012248 and a grant from the Glenn Foundation . JDB is the G. Harold and Leila Y. Mathers Professor of Geriatrics and Adult Development.

Keywords

  • Association
  • Genetics
  • Mutation
  • Rare variation

ASJC Scopus subject areas

  • General Neuroscience
  • Aging
  • Developmental Biology
  • Clinical Neurology
  • Geriatrics and Gerontology

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