TY - JOUR
T1 - Evening and morning alterations in Obstructive Sleep Apnea red blood cell proteome
AU - Feliciano, Amélia
AU - Vaz, Fátima
AU - Valentim-Coelho, Cristina
AU - Torres, Vukosava M.
AU - Silva, Rita
AU - Prosinecki, Vesna
AU - Alexandre, Bruno M.
AU - Almeida, Andreia
AU - Almeida-Marques, Catarina
AU - Carvalho, Ana S.
AU - Matthiesen, Rune
AU - Malhotra, Atul
AU - Pinto, Paula
AU - Bárbara, Cristina
AU - Penque, Deborah
N1 - info:eu-repo/grantAgreement/FCT/5876/147362/PT#
info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F43365%2F2008/PT#
Project partially supported by Harvard Medical School-Portugal Program (HMSP-ICJ/
0022/2011), ToxOmics - Centre for Toxicogenomics and Human Health (FCT-UID/BIM/00009/2013), FCT/Poly-Annual Funding Program and FEDER/Saúde XXI Program (Portugal) and postdoctoral fellowship SFRH/BPD/43365/2008 of Fundação para a Ciência e a Tecnologia (FCT), Portugal.
PY - 2017/4/1
Y1 - 2017/4/1
N2 - This article presents proteomics data referenced in [1] Using proteomics-based evaluation of red blood cells (RBCs), we have identified differentially abundant proteins associated with Obstructive Sleep Apnea Syndrome (OSA). RBCs were collected from peripheral blood of patients with moderate/severe OSA or snoring at pre- (evening) and post-night (morning) polysomnography, so that proteome variations between these time points could be assessed. RBC cytoplasmic fraction depleted of hemoglobin, using Hemovoid™ system, were analyzed by two-dimensional fluorescence difference gel electrophoresis (2D-DIGE), the 2D image software-based analyzed and relevant differentially abundant proteins identified by mass spectrometry (MS). MS identified 31 protein spots differentially abundant corresponding to 21 unique proteins possibly due to the existence of post-translational modification regulations. Functional analysis by bioinformatics tools indicated that most proteins are associated with catalytic, oxidoreductase, peroxidase, hydrolase, ATPase and anti-oxidant activity. At morning a larger numbers of differential proteins including response to chemical stimulus, oxidation reduction, regulation of catalytic activity and response to stress were observed in OSA. The data might support further research in OSA biomarker discovery and validation.
AB - This article presents proteomics data referenced in [1] Using proteomics-based evaluation of red blood cells (RBCs), we have identified differentially abundant proteins associated with Obstructive Sleep Apnea Syndrome (OSA). RBCs were collected from peripheral blood of patients with moderate/severe OSA or snoring at pre- (evening) and post-night (morning) polysomnography, so that proteome variations between these time points could be assessed. RBC cytoplasmic fraction depleted of hemoglobin, using Hemovoid™ system, were analyzed by two-dimensional fluorescence difference gel electrophoresis (2D-DIGE), the 2D image software-based analyzed and relevant differentially abundant proteins identified by mass spectrometry (MS). MS identified 31 protein spots differentially abundant corresponding to 21 unique proteins possibly due to the existence of post-translational modification regulations. Functional analysis by bioinformatics tools indicated that most proteins are associated with catalytic, oxidoreductase, peroxidase, hydrolase, ATPase and anti-oxidant activity. At morning a larger numbers of differential proteins including response to chemical stimulus, oxidation reduction, regulation of catalytic activity and response to stress were observed in OSA. The data might support further research in OSA biomarker discovery and validation.
KW - 2D-DIGE
KW - Biomarkers
KW - Obstructive Sleep Apnea
KW - Red blood cells
UR - http://www.scopus.com/inward/record.url?scp=85010211043&partnerID=8YFLogxK
U2 - 10.1016/j.dib.2017.01.005
DO - 10.1016/j.dib.2017.01.005
M3 - Article
C2 - 28149928
AN - SCOPUS:85010211043
SN - 2352-3409
VL - 11
SP - 103
EP - 110
JO - Data in brief
JF - Data in brief
ER -