Sylvain E. Lesné, Mathew A. Sherman, Marianne Grant, Michael Kuskowski, Julie A. Schneider, David A. Bennett, Karen H. Ashe. Brain amyloid-β oligomers in ageing and Alzheimer's disease. Brain. 2013;136(5):1383–1398. https://doi.org/10.1093/brain/awt062
The authors apologize for errors in Fig. 1 and Supplementary Figs 1, 3 and 5, as detailed below. The corrected images are provided only in this corrigendum to preserve the published version of record.
Figure 1.
Correction for Fig. 1C in Lesné et al. Original western blotting images for 6E10 in MB protein lysates. Low and high intensity images for the full membrane used to detect human APP/Aβ are shown (top and bottom, respectively). The corrected image for the lower panel of C is shown within the box.
Figure 1
In the published Fig. 1C, the western blot image for 6E10 included in the panel was processed inappropriately. The original image at two intensities, low and high respectively, is provided in Fig. 1. The panel has been corrected accordingly (Fig. 1, boxed image).
The corresponding description of Fig. 1C in the original legend is unchanged.
The correction does not change the scientific conclusions that Aβ*56 is present in membrane-associated lysates of human brain tissue.
Supplementary Figure 1
Figure 2.
Correction for Supplementary Fig. 1 in Lesné et al. Representative western blotting images for PrP and NR1 across protein lysates. (A) Low and high intensity images for the full membrane used to detect PrP using the 8B4 antibody are shown (top and bottom, respectively). (B) Two membranes were used to analyse EC-IC-MB fractions (left) and TBS-TBST fractions (right), respectively. Low and high intensity images for the full membrane used to detect NR1 using the NR1ct antibody are shown (top and bottom, respectively). The image for the correct figure is shown within box and the image areas used to create the corrected panel are indicated by white dashed lines in A and B. Note that, in line with current standards, both NR1ct images are kept separated by a white space to explicitly indicate these images are derived from two separate membranes.
In the published Supplementary Fig. 1, the western blotting images for PrP and NR1ct included in the panel were processed inappropriately. The original unaltered images at two intensities for PrP-8B4 (Fig. 2) and new unaltered images at two intensities for NR1ct (Fig. 2), as the original file could not be retrieved from records, are provided. The figure panel has been corrected accordingly (Fig. 2, boxed image). The correction does not change the scientific conclusions that membrane-associated proteins are better extracted from lipids in the MB lysates of the 4-step extraction than in the TBST fractions of the 3-step extraction protocol.
The corrected Supplementary Fig. 1 legend should read: Comparison of the segregation of membrane-associated proteins from human brain in the 4-step extraction protocol (Lesne et al., 2006; Sherman & Lesné, 2011) and the 3-step extraction protocol (Shankar et al., 2008). Using the 4-step protocol, the NR1 subunit of NMDA receptors, detected using an antibody recognizing the carboxyl-terminal antibody of the NR1 subunit (NR1ct) and prion protein (PrP), both known membrane- (MB)-associated proteins, appear selectively in the MB-enriched fraction. Using the 3-step extraction protocol, these MB-associated proteins segregate into the TBS-T extracts. In contrast, using the 4-step extraction protocol, these proteins selectively appear in the MB-associated fraction, but not the extracellular- (EC)-associated or the intracellular- (IC)-associated fractions. Although PrP can become soluble following cleavage of the glycosylphosphatidylinositol (GPI) lipid tethering PrP to the outer surface of the cell membrane, its absence in the EC-enriched fraction argues against the possibility that the PrP that is present in the TBS extract is soluble PrP. Instead, it indicates that some membrane-associated proteins are present in TBS extracts.
Supplementary Figure 3
Figure 3.
Correction for Supplementary Fig. 3 in Lesné et al. Original western blotting image for APPCter across protein lysates. Low and high intensity images for the full membrane used to detect the C-terminus of APP using the APPCter antibody are shown (top and bottom, respectively). The corrected image for the top panel of Supplementary Fig. 3 is shown within the box and the image area used to create the corrected strip is indicated by the white dashed lines in the top original western blot image.
In the published Supplementary Fig. 3, the western blot image for APPCter included in the panel was processed inappropriately. The original image at two intensities, low and high, respectively, are provided in Fig. 3. The panel has been corrected accordingly (Fig. 3, boxed image). The original Supplementary Fig. 3 legend is unchanged.
While the intensity of the APP bands in the human lysates from this image is lower than that of the published image, this detection pattern could reflect the longer post-mortem interval between mouse and human tissue. Moreover, this APPCter immunoreactivity profile is also consistent with that observed for 22C11 included in the published Supplementary Fig. 3. Thus, the error does not change the scientific conclusions that APPCter antibody does not detect Aβ*56.
Supplementary Figure 5
Figure 4.
Correction for Supplementary Fig. 5 in Lesné et al. Original western blotting image for A11 across protein lysates. Low and high intensity images for the full membrane used to detect putative Aβ oligomers using the A11 antibody are shown (top and bottom, respectively). Note that the blocking step generated a zone of pallor in the middle right portion of the membrane (expanded right delineated in pink). The corrected image for the top panel of Supplementary Fig. 5 is shown within the box and the image area used to create the corrected panel is indicated by the white dashed lines in the top original western blot image.
In Supplementary Fig. 5, the A11 image included in the panel was processed inappropriately. The correct original image at two intensities, low and high, respectively, is provided in Fig. 4. The panel has been corrected accordingly (Fig. 4, boxed image). The original Supplementary Fig. 5 legend is unchanged.
While a zone of pallor likely due to the blocking step preceding antibody probing appeared to affect two lanes within the range of ∼25 to ∼40 kDa, A11 immunoreactive bands were readily detected Aβ*56 in human and transgenic mouse brains. Co-migrating at the level of putative human 6-mers, very faint bands are present in J20 transgenic (Tg) lysates but their detection could be lowered by the blocking parameters in this protein range. As stated in the published corresponding figure legend, ‘A11 [it] also detects oligomers of other proteins; therefore, some bands may represent non-Aβ oligomers’. Moreover the main text referred to this figure as follows: ‘Importantly, the A11 antiserum detected Aβ*56 (Supplementary Fig. 5), providing additional evidence that it is an oligomer comprised of amyloid-β’ (p. 1388); and ‘Here, we noted with great interest a novel 110 kDa A11-immunoreactive band in 6E10-immunocaptured proteins in CSF (Fig. 1B) and brain (Supplementary Fig. 5), which was obscured by full-length or soluble amyloid precursor proteins in our standard protocol’. (p. 1395).
Overall, the correction does not change the scientific conclusions that the A11 antibody detects Aβ*56 in mouse and human brain tissue.