Dataset of why inclusion matters for Alzheimer's disease biomarker discovery in plasma
Mostafa J. Khan,
Heather Desaire,
Oscar L. Lopez,
M. Ilyas Kamboh,
Renã A.S. Robinson
Affiliations
Mostafa J. Khan
Department of Chemistry, Vanderbilt University, 5423 Stevenson Center, Nashville, TN 37235, United States
Heather Desaire
Department of Chemistry, University of Kansas, Lawrence, KS 66045, United States
Oscar L. Lopez
Department of Neurology, University of Pittsburgh, Pittsburgh, PA 15213, United States; Department of Psychiatry, University of Pittsburgh, Pittsburgh, PA 15213, United States
M. Ilyas Kamboh
Department of Psychiatry, University of Pittsburgh, Pittsburgh, PA 15213, United States; Department of Human Genetics, University of Pittsburgh, Pittsburgh, PA 15213, United States; Department of Epidemiology, University of Pittsburgh, Pittsburgh, PA 15213, United States
Renã A.S. Robinson
Department of Chemistry, Vanderbilt University, 5423 Stevenson Center, Nashville, TN 37235, United States; Vanderbilt Memory and Alzheimer's Center, Vanderbilt University Medical Center, Nashville, TN 37212, United States; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37232, United States; Vanderbilt Brain Institute, Vanderbilt University Medical Center, Nashville, TN 37232, United States; Department of Neurology, Vanderbilt University Medical Center, Nashville, TN 37232, United States; Corresponding author at: Department of Chemistry, Vanderbilt University, 5423 Stevenson Center, Nashville, TN 37235, United States.
Here we present a plasma proteomics dataset that was generated to understand the importance of self-reported race for biomarker discovery in Alzheimer's disease. This dataset is related to the article “Why inclusion matters for Alzheimer's disease biomarker discovery in plasma” [1]. Plasma samples were obtained from clinically diagnosed Alzheimer's disease and cognitively normal adults of African American/Black and non-Hispanic White racial and ethnic backgrounds. Plasma was immunodepleted, digested, and isobarically tagged with commercial reagents. Tagged peptides were fractionated using high pH fractionation and resulting fractions analysed by liquid chromatography – mass spectrometry (LC-MS/MS & MS3) analysis on an Orbitrap Fusion Lumos mass spectrometer. The resulting data was processed using Proteome Discoverer to produce a list of identified proteins with corresponding tandem mass tag (TMT) intensity information.
