Label‐free proteomic analysis of red blood cell membrane fractions from abdominal aortic aneurysm patients. Issue 7 (August 2014)
- Record Type:
- Journal Article
- Title:
- Label‐free proteomic analysis of red blood cell membrane fractions from abdominal aortic aneurysm patients. Issue 7 (August 2014)
- Main Title:
- Label‐free proteomic analysis of red blood cell membrane fractions from abdominal aortic aneurysm patients
- Authors:
- Martinez‐Pinna, Roxana
Burillo, Elena
Madrigal‐Matute, Julio
Lopez, Juan Antonio
Camafeita, Emilio
Torres‐Fonseca, Monica Maria
Llamas‐Granda, Patricia
Egido, Jesus
Michel, Jean‐Baptiste
Blanco‐Colio, Luis Miguel
Martin‐Ventura, Jose Luis
Ge, Ying
Van Eyk, Jennifer - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="prca1565-sec-0010" sec-type="section"> <title>Purpose</title> <p>To test whether red blood cell (RBC) membrane composition is modified in abdominal aortic aneurysms (AAA) patients.</p> </sec> <sec id="prca1565-sec-0020" sec-type="section"> <title>Experimental design</title> <p>RBC membrane extracts from AAA patients (aortic diameter &gt;3 cm, <italic>n</italic> = 7) and control subjects (<italic>n</italic> = 4) were analyzed by a label‐free quantitative MS‐based strategy, using spectral count data. Additional validation was performed by western‐blot.</p> </sec> <sec id="prca1565-sec-0030" sec-type="section"> <title>Results</title> <p>Data analysis based on spectral count from MS/MS‐based experiments provided us a signature of 39 proteins differentially expressed in RBC membranes between AAA and controls (changes equal/over 1.515‐fold; <italic>p</italic>‐values equal/lower 0.05). MS data revealed altered levels of structural membrane proteins (e.g. spectrins and ankyrin), components of the degradation machinery (proteasome subunits), and oxidative stress related proteins (e.g. catalase and peroxiredoxin‐2) among others. Decreased catalase and peroxiredoxin‐2 expression in RBC membrane of AAA patients compared to controls were further validated by Western blot, confirming the proteomic results.</p> </sec> <sec id="prca1565-sec-0040" sec-type="section"> <title>Conclusions and clinical<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="prca1565-sec-0010" sec-type="section"> <title>Purpose</title> <p>To test whether red blood cell (RBC) membrane composition is modified in abdominal aortic aneurysms (AAA) patients.</p> </sec> <sec id="prca1565-sec-0020" sec-type="section"> <title>Experimental design</title> <p>RBC membrane extracts from AAA patients (aortic diameter &gt;3 cm, <italic>n</italic> = 7) and control subjects (<italic>n</italic> = 4) were analyzed by a label‐free quantitative MS‐based strategy, using spectral count data. Additional validation was performed by western‐blot.</p> </sec> <sec id="prca1565-sec-0030" sec-type="section"> <title>Results</title> <p>Data analysis based on spectral count from MS/MS‐based experiments provided us a signature of 39 proteins differentially expressed in RBC membranes between AAA and controls (changes equal/over 1.515‐fold; <italic>p</italic>‐values equal/lower 0.05). MS data revealed altered levels of structural membrane proteins (e.g. spectrins and ankyrin), components of the degradation machinery (proteasome subunits), and oxidative stress related proteins (e.g. catalase and peroxiredoxin‐2) among others. Decreased catalase and peroxiredoxin‐2 expression in RBC membrane of AAA patients compared to controls were further validated by Western blot, confirming the proteomic results.</p> </sec> <sec id="prca1565-sec-0040" sec-type="section"> <title>Conclusions and clinical relevance</title> <p>RBCs membrane protein composition is altered in AAA patients, which could be involved in the pathological role of RBCs in aortic tissue and become potential targets to prevent AAA progression.</p> </sec> </abstract> … (more)
- Is Part Of:
- Proteomics. Volume 8:Issue 7/8(2014)
- Journal:
- Proteomics
- Issue:
- Volume 8:Issue 7/8(2014)
- Issue Display:
- Volume 8, Issue 7/8 (2014)
- Year:
- 2014
- Volume:
- 8
- Issue:
- 7/8
- Issue Sort Value:
- 2014-0008-NaN-0000
- Page Start:
- 626
- Page End:
- 630
- Publication Date:
- 2014-08
- Subjects:
- Proteomics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1862-8354 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/prca.201400035 ↗
- Languages:
- English
- ISSNs:
- 1862-8346
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178500
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3108.xml