PubMed · 3423554
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J P Gmür. 1987-12-08. [Thrombocyte transfusion].. https://pubmed.ncbi.nlm.nih.gov/3423554/
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OBJECTIVES: Platelet storage lesion (PSL) severely impairs platelet function during storage, presenting a major hurdle in transfusion medicine; however, the dynamic interplay between global proteomic changes and post-translational modifications (PTMs) underlying these functional deteriorations remains insufficiently characterized. Here, we report the first comprehensive multi-omics analysis integrating global proteomics, acetylomics, and succinylomics to dissect the molecular dynamics during platelet storage. METHODS: We performed quantification of global proteomics, acetylome and succinylome based on TMT-labeled LC-MS/MS analysis, combined with antibody-affinity enrichment and purification. Dynamic molecular changes and functional transformation of platelet were also characterized under proper conditions stored for 1, 3, 5, 7 days, respectively. RESULTS: We systematically characterized 3,609 proteins, 1,308 acetylation sites, and 1,947 succinylation sites across multiple storage time points (D1, D3, D5, D7). We distinct temporal patterns of post-translational modifications, with succinylation showing more extensive coverage than acetylation in platelets. Pathway enrichment analysis revealed extensive metabolic reprogramming involving complement activation, energy metabolism, and cellular detoxification processes. The identification of specific motif patterns provided mechanistic insights into the functional specificity of these modifications. Random forest machine learning identified 20 core regulatory proteins representing critical nodes in PSL development. Furthermore, we employed real - time quantitative polymerase chain reaction (RT - QPCR) to measure the expression levels of key genes related to platelet function and PTM - associated pathways. CONCLUSION: By mapping the interplay between proteomic abundance shifts and PTM dynamics, this study provides a multidimensional understanding of PSL, establishing a foundational framework for optimizing storage protocols and enhancing transfusion safety.
The intracellular distribution of sphingosine (Sph) kinase activity was examined in human platelets. A large proportion (72%) of the total activity was found to be associated with the membrane fraction, and the membrane-associated fraction had higher specific activity compared with the cytosolic enzyme. Most of the membrane-associated activity could be extracted with 1 M NaCl. The cytosolic activity was unstable upon heat treatment, with 80% of the activity being lost during incubation at 45 degreesC for 1 h, whereas the NaCl-extractable fraction was stable under the same conditions. When subjected to Mono Q column chromatography, the cytosolic fraction produced two activity peaks and the NaCl-extractable fraction gave a single peak. These three Sph kinase activities showed different responses to stimulation by beta-octylglucoside and inhibition by N, N-dimethylsphingosine and l-threo-dihydrosphingosine, suggesting the presence of multiple enzyme forms in human platelets.
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