Reply: Alzheimer’s disease: Molecular consequences of presenilin-1 mutation

C. Russo, G. Schettini, T. C. Saido, C. Hulette, C. Lippa, L. Lannfelt, Bernardino Ghetti, P. Gambetti, M. Tabaton, J. K. Teller

Research output: Contribution to journalComment/debate

1 Scopus citations


Gandy et al. compare our results with their 1994 findings that the amino-terminally truncated amyloid Aβ11-42 was relatively abundant in two cases of familial Alzheimer′s disease involving two distinct mutations in -APP. However, four important differences should be borne in mind: The authors compare Aβ11-42 with Aβ1-42 and ignore Aβ1-40, although both Aβ1-40 and Aβ1-42 are generated by β-secretase/BACE cleavage at residue Asp 1 (ref. 3); their data are not correlated with features related to disease severity, such as age at onset and duration; they did not examine brains with PS1 mutations (these were not known at that time); and their characterization was based on the use of size-exclusion chromatography and electrospray mass spectrometry to quantify formic-acid-extracted Aβ, whereas we used quantitative analysis of immunoprecipitated water-soluble Aβ on western blots, mass spectrometry to identify Aβ variants, and immunohistochemistry to reveal amino-truncated A peptides in plaques.

Original languageEnglish (US)
Pages (from-to)655
Number of pages1
Issue number6838
StatePublished - Jun 7 2001
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)
  • General

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    Russo, C., Schettini, G., Saido, T. C., Hulette, C., Lippa, C., Lannfelt, L., Ghetti, B., Gambetti, P., Tabaton, M., & Teller, J. K. (2001). Reply: Alzheimer’s disease: Molecular consequences of presenilin-1 mutation. Nature, 411(6838), 655.