TY - JOUR
T1 - Proteomic analysis of eccrine sweat
T2 - Implications for the discovery of schizophrenia biomarker proteins
AU - Raiszadeh, Michelle M.
AU - Ross, Mark M.
AU - Russo, Paul S.
AU - Schaepper, Mary Ann
AU - Zhou, Weidong
AU - Deng, Jianghong
AU - Ng, Daniel
AU - Dickson, April
AU - Dickson, Cindy
AU - Strom, Monica
AU - Osorio, Carolina
AU - Soeprono, Thomas
AU - Wulfkuhle, Julia D.
AU - Petricoin, Emanuel F.
AU - Liotta, Lance A.
AU - Kirsch, Wolff M.
N1 - Pooling of the samples was deemed necessary due to the limited amount of volume and/or protein abundance in each individual sample. Pooling the samples provided us with greater protein abundances that would help enhance our ability to identify and quantitate more proteins.
PY - 2012/4/6
Y1 - 2012/4/6
N2 - Liquid chromatography-tandem mass spectrometry (LC-MS/MS) and multiple reaction monitoring mass spectrometry (MRM-MS) proteomics analyses were performed on eccrine sweat of healthy controls, and the results were compared with those from individuals diagnosed with schizophrenia (SZ). This is the first large scale study of the sweat proteome. First, we performed LC-MS/MS on pooled SZ samples and pooled control samples for global proteomics analysis. Results revealed a high abundance of diverse proteins and peptides in eccrine sweat. Most of the proteins identified from sweat samples were found to be different than the most abundant proteins from serum, which indicates that eccrine sweat is not simply a plasma transudate and may thereby be a source of unique disease-associated biomolecules. A second independent set of patient and control sweat samples were analyzed by LC-MS/MS and spectral counting to determine qualitative protein differential abundances between the control and disease groups. Differential abundances of selected proteins, initially determined by spectral counting, were verified by MRM-MS analyses. Seventeen proteins showed a differential abundance of approximately 2-fold or greater between the SZ pooled sample and the control pooled sample. This study demonstrates the utility of LC-MS/MS and MRM-MS as a viable strategy for the discovery and verification of potential sweat protein disease biomarkers. © 2012 American Chemical Society.
AB - Liquid chromatography-tandem mass spectrometry (LC-MS/MS) and multiple reaction monitoring mass spectrometry (MRM-MS) proteomics analyses were performed on eccrine sweat of healthy controls, and the results were compared with those from individuals diagnosed with schizophrenia (SZ). This is the first large scale study of the sweat proteome. First, we performed LC-MS/MS on pooled SZ samples and pooled control samples for global proteomics analysis. Results revealed a high abundance of diverse proteins and peptides in eccrine sweat. Most of the proteins identified from sweat samples were found to be different than the most abundant proteins from serum, which indicates that eccrine sweat is not simply a plasma transudate and may thereby be a source of unique disease-associated biomolecules. A second independent set of patient and control sweat samples were analyzed by LC-MS/MS and spectral counting to determine qualitative protein differential abundances between the control and disease groups. Differential abundances of selected proteins, initially determined by spectral counting, were verified by MRM-MS analyses. Seventeen proteins showed a differential abundance of approximately 2-fold or greater between the SZ pooled sample and the control pooled sample. This study demonstrates the utility of LC-MS/MS and MRM-MS as a viable strategy for the discovery and verification of potential sweat protein disease biomarkers. © 2012 American Chemical Society.
UR - https://www.scopus.com/pages/publications/84859621668
UR - https://www.scopus.com/pages/publications/84859621668#tab=citedBy
UR - https://www.mendeley.com/catalogue/33fdfb53-af9c-368b-a22f-62339bd1f467/
U2 - 10.1021/pr2007957
DO - 10.1021/pr2007957
M3 - Article
C2 - 22256890
SN - 1535-3893
VL - 11
SP - 2127
EP - 2139
JO - Journal of Proteome Research
JF - Journal of Proteome Research
IS - 4
ER -