Proteomic analysis of the supernatant of red blood cell units: the effects of storage and leucoreduction. Issue 3 (11th May 2013)
- Record Type:
- Journal Article
- Title:
- Proteomic analysis of the supernatant of red blood cell units: the effects of storage and leucoreduction. Issue 3 (11th May 2013)
- Main Title:
- Proteomic analysis of the supernatant of red blood cell units: the effects of storage and leucoreduction
- Authors:
- Dzieciatkowska, M.
Silliman, C. C.
Moore, E. E.
Kelher, M. R.
Banerjee, A.
Land, K. J.
Ellison, M.
West, F. B.
Ambruso, D. R.
Hansen, K. C. - Abstract:
- <abstract abstract-type="main" id="vox12042-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="vox12042-sec-0001" sec-type="section"> <title>Background</title> <p>Red blood cell (RBC) transfusion is a life‐saving intervention for critically ill patients; however, it has been linked to increased morbidity and mortality. We hypothesize that a number of important proteins accumulate during routine storage of RBCs, which may explain some of the adverse effects seen in transfused patients.</p> </sec> <sec id="vox12042-sec-0002" sec-type="section"> <title>Study Design</title> <p>Five RBC units were drawn and divided (half prestorage leucoreduced (LR‐RBC) and half left as an unmodified control (RBC). The supernatant was separated on days 1 and 42 of storage and proteomic analyses completed with in‐gel tryptic digestion and nano‐liquid chromatography tandem mass spectrometry.</p> </sec> <sec id="vox12042-sec-0003" sec-type="section"> <title>Results</title> <p>In RBC supernatants, 401 proteins were identified: 203 increased with storage, 114 decreased, and 84 were unchanged. In LR‐RBC supernatant, 231 proteins were identified: 84 increased with storage, 30 decreased, and 117 were unchanged. Prestorage leucoreduction removed many platelet‐ and leucocyte‐derived structural proteins; however, a number of intracellular proteins accumulated including peroxiredoxins (Prdx) 6 and latexin. The increases were confirmed by immunoblotting, including the T‐phosphorylation<abstract abstract-type="main" id="vox12042-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="vox12042-sec-0001" sec-type="section"> <title>Background</title> <p>Red blood cell (RBC) transfusion is a life‐saving intervention for critically ill patients; however, it has been linked to increased morbidity and mortality. We hypothesize that a number of important proteins accumulate during routine storage of RBCs, which may explain some of the adverse effects seen in transfused patients.</p> </sec> <sec id="vox12042-sec-0002" sec-type="section"> <title>Study Design</title> <p>Five RBC units were drawn and divided (half prestorage leucoreduced (LR‐RBC) and half left as an unmodified control (RBC). The supernatant was separated on days 1 and 42 of storage and proteomic analyses completed with in‐gel tryptic digestion and nano‐liquid chromatography tandem mass spectrometry.</p> </sec> <sec id="vox12042-sec-0003" sec-type="section"> <title>Results</title> <p>In RBC supernatants, 401 proteins were identified: 203 increased with storage, 114 decreased, and 84 were unchanged. In LR‐RBC supernatant, 231 proteins were identified: 84 increased with storage, 30 decreased, and 117 were unchanged. Prestorage leucoreduction removed many platelet‐ and leucocyte‐derived structural proteins; however, a number of intracellular proteins accumulated including peroxiredoxins (Prdx) 6 and latexin. The increases were confirmed by immunoblotting, including the T‐phosphorylation of Prdx‐6, indicating that it may be functioning as an active phospholipase. Active matrix metalloproteinase‐9 also increased with a coinciding decrease in the metalloproteinase inhibitor 1 and cystatin C.</p> </sec> <sec id="vox12042-sec-0004" sec-type="section"> <title>Conclusion</title> <p>We conclude that a number of proteins increase with RBC storage, which is partially ameliorated with leucoreduction, and transfusion of stored RBCs may introduce mediators that result in adverse events in the transfused host.</p> </sec> </abstract> … (more)
- Is Part Of:
- Vox sanguinis. Volume 105:Issue 3(2013)
- Journal:
- Vox sanguinis
- Issue:
- Volume 105:Issue 3(2013)
- Issue Display:
- Volume 105, Issue 3 (2013)
- Year:
- 2013
- Volume:
- 105
- Issue:
- 3
- Issue Sort Value:
- 2013-0105-0003-0000
- Page Start:
- 210
- Page End:
- 218
- Publication Date:
- 2013-05-11
- Subjects:
- Blood -- Periodicals
Blood -- Transfusion -- Periodicals
Immunohematology -- Periodicals
Immunopathology -- Periodicals
615.39 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1423-0410 ↗
http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=vox ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/vox.12042 ↗
- Languages:
- English
- ISSNs:
- 0042-9007
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9258.700000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2986.xml