Additional file 1:

Separation of pooled urea samples by SDS-PAGE for proteomic analysis. (a) SDS-PAGE gel of urea fractions extracted from AD, FTLD-U, and control pooled frontal cortex homogenates (10 cases each). (b) SDS-PAGE gel of 4 pooled FTLD-U or 4 pooled control samples after addition of heavy labeled cell lysate. The gels were stained with Coomassie Blue G-250 and gel lanes were excised in 5 pieces as indicated (F1-F5 or C1-C5).

Format: PDF Size: 171KB Download file

This file can be viewed with: Adobe Acrobat Reader

Additional file 2:

Statistical evaluation and filtering of label-free proteomics data. (a) Abundance ratios for FTLD-U/Control comparison were transformed (logarithmic base 2) and plotted with each point corresponding to the number of proteins in 0.3 unit windows (black line). A Gaussian curve was subsequently fitted to the data (red line) and used to determine significance levels for protein change. (b) Fitted normal distributions for all possible pair-wise comparisons. Statistical means, standard deviations, and regression coefficients are presented in Additional File 3.

Format: PDF Size: 50KB Download file

This file can be viewed with: Adobe Acrobat Reader

Additional file 3:

Statistical data for fitted normal distributions. Table detailing the specific properties of each fitted normal distribution used for proteomic data analysis.

Format: XLS Size: 27KB Download file

This file can be viewed with: Microsoft Excel Viewer

Additional file 4:

Statistical evaluation and filtering of CDIT proteomics data. Abundance ratios for FTLD-U/Control comparison were transformed (logarithmic base 2) and plotted with each point corresponding to the number of proteins in 0.4 unit windows (black line). A Gaussian curve was subsequently fitted to the data (red line) and used to determine significance levels for protein change.

Format: PDF Size: 44KB Download file

This file can be viewed with: Adobe Acrobat Reader

Additional file 5:

Peptide map of SEPT11. Amino acid sequence of full length SEPT11 (429 aa) marked with peptides identified in shotgun proteomics approaches (solid underline), mapped unique peptides in targeted proteomics (red color), peptides quantified using targeted proteomics (bold), and immunizing peptide used in development of in-house SEPT11 rabbit polyclonal antibody (dotted underline).

Format: PDF Size: 10KB Download file

This file can be viewed with: Adobe Acrobat Reader

Additional file 6:

SEPT11 peptides selected for targeted proteomics. Table detailing properties of SEPT11 peptides selected for targeted proteomics.

Format: XLS Size: 66KB Download file

This file can be viewed with: Microsoft Excel Viewer

Additional file 7:

Assessment of SEPT11 in detergent-soluble fractions by immunoblotting. Triton X-100 (a) and Sarkosyl (b) fractions extracted from frontal cortex samples of individual FTLD-U and control cases were immunoblotted with an N-terminus specific rabbit polyclonal SEPT11 antibody. While full-length SEPT11 (49 kDa) is abundant in both detergent-soluble fractions, the low molecular weight fragments noted in the urea fractions (Figure 3) were decreased or absent in these fractions. The band noted at ~40 kDa is non-specific as determined by preabsorption studies using the immunizing peptide.

Format: PDF Size: 86KB Download file

This file can be viewed with: Adobe Acrobat Reader

Additional file 8:

Individual Case Demographic and Scoring Information. Table detailing specific demographic data and scoring results for all cases analyzed by immunohistochemistry.

Format: XLS Size: 39KB Download file

This file can be viewed with: Microsoft Excel Viewer