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Please use this identifier to cite or link to this item: http://hdl.handle.net/10400.18/869

Título: Profiling the erythrocyte membrane proteome isolated from patients diagnosed with chronic obstructive pulmonary disease
Autor: Alexandre, Bruno
Charro, Nuno
Blonder, Yosip
Lopes, Carlos
Almeida, Antonio Bugalho
Veenstra, Timothy
Penque, Deborah
Azevedo, Pilar
Chan, K.C.
Prieto, D.A.
Issaq, H.
Palavras-chave: Proteomics
DPOC
Red Blood Cells
Genómica Funcional
Issue Date: 2012
Editora: Elsevier
Citação: J Proteomics. 2012 Apr 17. [Epub ahead of print]
Resumo: Structural and metabolic alterations in erythrocytes play an important role in the pathophysiology of Chronic Obstructive Pulmonary Disease (COPD). Whether these dysfunctions are related to the modulation of erythrocyte membrane proteins in patients diagnosed with COPD remains to be determined. Herein, a comparative proteomic profiling of the erythrocyte membrane fraction isolated from peripheral blood of smokers diagnosed with COPD and smokers with no COPD was performed using differential 16O/18O stable isotope labeling. A total of 219 proteins were quantified as being significantly differentially expressed within the erythrocyte membrane proteomes of smokers with COPD and healthy smokers. Functional pathway analysis showed that the most enriched biofunctions were related to cell-to-cell signaling and interaction, hematological system development, immune response, oxidative stress and cytoskeleton. Chorein (VPS13A), a cytoskeleton related protein whose defects had been associated with the presence of cell membrane deformation of circulating erythrocytes was found to be down-regulated in the membrane fraction of erythrocytes obtained from COPD patients. Methemoglobin reductase (CYB5R3) was also found to be underexpressed in these cells, suggesting that COPD patients may be at higher risk for developing methemoglobinemia. This article is part of a Special Issue entitled: “Integrated omics— Functional applications to blood and blood therapeutics”.
Arbitragem científica: yes
URI: http://hdl.handle.net/10400.18/869
ISSN: 1874-3919
Versão do Editor: http://www.sciencedirect.com/science/article/pii/S187439191200214X
Appears in Collections:DGH - Artigos em revistas internacionais

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