Protein changes occurring during storage of platelet concentrates. A two-dimensional gel electrophoretic analysis

• Published in: Transfusion (Philadelphia, Pa.) Vol. 27; no. 4; p. 335
• Main Authors: Snyder, E L, Dunn, B E, Giometti, C S, Napychank, P A, Tandon, N N, Ferri, P M, Hofmann, J P
• Format: Journal Article
• Language: English
• Published: United States 01-07-1987
• Subjects: Blood Platelets - cytology; Blood Preservation; Blood Proteins - analysis; Computers; Electrophoresis, Polyacrylamide Gel - methods; Humans; Peptide Mapping - methods
• ISSN: 0041-1132
• DOI: 10.1046/j.1537-2995.1987.27487264743.x

The changes in thrombocyte proteins during 22 degrees C storage of platelet concentrates (PC) were studied. To prepare a reference protein "map" of stored PC, platelet samples were taken on days 1, 7, and 21. The platelet proteins were separated by isoelectric focusing (first-dimension) followed by second-dimension polyacrylamide gradient gel electrophoresis with sodium dodecylsulfate (2D). The silver-stained gels were analyzed by computer to obtain a composite map of stored PC proteins. The pattern seen on day 1 changed during 7 days of storage, with 30 proteins increasing or decreasing in spot density. In general, the spot density for lower-molecular-weight proteins increased, whereas that for higher-molecular-weight proteins decreased. Membrane proteins of intact fresh and stored platelets were labeled with 3H using sodium metaperiodate-[3H]NaBH4 and with 125I using lactoperoxidase-H2O2. A comparison on the fluorographs of 2D gels of [3H]NaBH4-labeled platelet proteins showed several protein spots in the stored Day 7 sample that had not been seen in the Day 1 sample. Similarly, for the autoradiographs, several 125I-labeled proteins detected in Day 7 PC were not seen in the Day 1 samples. The results provide evidence that platelet proteins are altered during PC storage and that these changes involve platelet membrane proteins.