High‐density lipoprotein 3 and apolipoprotein A‐I alleviate platelet storage lesion and release of platelet extracellular vesicles. Issue 9 (10th June 2014)

• Record Type: Journal Article
• Authors: Pienimaeki‐Roemer, Annika; Fischer, Astrid; Tafelmeier, Maria; Orsó, Evelyn; Konovalova, Tatiana; Böttcher, Alfred; Liebisch, Gerhard; Reidel, Armin; Schmitz, Gerd
• Is Part Of: Transfusion. Volume 54:Issue 9(2014)
• Page Start: 2301
• Page End: 2314
• Publication Date: 2014-06-10
• Subjects: Hematology -- Periodicals; Blood -- Transfusion -- Periodicals; Blood Group Antigens -- Periodicals; Blood Preservation -- Periodicals; Blood Transfusion -- Periodicals; 615
• DOI: 10.1111/trf.12640
• Languages: English
• ISSNs: 0041-1132

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="trf12640-sec-0001" sec-type="section"> <title>Background</title> <p>Stored platelet (PLT) concentrates (PLCs) for transfusion develop a PLT storage lesion (PSL), decreasing PLT viability and function with profound lipidomic changes and PLT extracellular vesicle (PL‐EV) release. High‐density lipoprotein 3 (HDL<sub>3</sub>) improves PLT homeostasis through silencing effects on PLT activation in vivo. This prompted us to investigate HDL<sub>3</sub> and apolipoprotein A‐I (apoA‐I) as PSL‐antagonizing agents.</p> </sec> <sec id="trf12640-sec-0002" sec-type="section"> <title>Study Design and Methods</title> <p>Healthy donor PLCs were split into low‐volume standard PLC storage bags and incubated with native (n)HDL<sub>3</sub> or apoA‐I from plasma ethanol fractionation (precipitate IV) for 5 days under standard blood banking conditions. Flow cytometry, Born aggregometry, and lipid mass spectrometry were carried out to analyze PL‐EV release, PLT aggregation, agonist‐induced PLT surface marker expression, and PLT and plasma lipid compositions.</p> </sec> <sec id="trf12640-sec-0003" sec-type="section"> <title>Results</title> <p>Compared to control, added nHDL<sub>3</sub> and apoA‐I significantly reduced PL‐EV release by up to −62% during 5 days, correlating with the added apoA‐I concentration. At the lipid level, nHDL<sub>3</sub> and apoA‐I antagonized PLT lipid loss (+12%) and decreased cholesteryl ester (CE)/free cholesterol (FC) ratios (−69%), whereas in plasma polyunsaturated/saturated CE ratios increased (+3%) and CE 16:0/20:4 ratios decreased (−5%). Administration of nHDL<sub>3</sub> increased PLT bis(monoacylglycero)phosphate/phosphatidylglycerol (+102%) and phosphatidic acid/lysophosphatidic acid (+255%) ratios and improved thrombin receptor–activating peptide 6–induced PLT aggregation (+5%).</p> </sec> <sec id="trf12640-sec-0004" sec-type="section"> <title>Conclusion</title> <p>nHDL<sub>3</sub> and apoA‐I improve PLT membrane homeostasis and intracellular lipid processing and increase CE efflux, antagonizing PSL‐related reduction in PLT viability and function and PL‐EV release. We suggest uptake and catabolism of nHDL<sub>3</sub> into the PLT open canalicular system. As supplement in PLCs, nHDL<sub>3</sub> or apoA‐I from Fraction IV of plasma ethanol fractionation have the potential to improve PLC quality to prolong storage.</p> </sec> </abstract>