Abstract:
BACKGROUND AND OBJECTIVES:During platelet storage an array of deleterious changes occur, through mechanisms not fully understood, which impair platelet haemostasis. Transfused platelets should maintain the integrated networks of signalling pathways that regulate platelet activation and functionality. We hypothesized that protein phosphorylation and dephosphorylation, which play a fundamental role in these pathways, might be affected by platelet storage. We therefore investigated whether the activity of phosphotyrosine phosphatase (PTP), which belongs to an oxidant-susceptible group of enzymes involved in the platelet signal-transduction pathways that ensure platelet functionality, is affected by platelet storage. MATERIALS AND METHODS:Using sheep platelet species as a model system, we conducted serial studies on the membranes of platelets and microparticles shed during platelet storage, in their own plasma or in a synthetic medium called Seto, for up to 5 days at 4 degrees C. RESULTS:A progressive decrease in both total and specific membrane-associated PTP activities from whole platelets (but not from microparticles) located within each platelet storage bag was observed from day 1 onwards in both types of storage media. These decreases could be partly avoided by the addition of vitamin E. Additionally, the observed decrease in PTP activity was accompanied with increases in the tyrosine phosphorylation of proteins from whole platelets or crude platelet membranes, the tyrosine phosphorylation state of proteins from microparticles remaining basically unchanged. CONCLUSION:Our findings suggest that alterations of at least the tyrosine phosphorylation balance might be one of the reasons for the decrease in the haemostatic function of stored platelets.
journal_name
Vox Sangjournal_title
Vox sanguinisauthors
Hernández-Hernández A,Sánchez-Bernal C,Rodríguez MC,Gómez FP,Llanillo M,Sánchez-Yagüe Jdoi
10.1046/j.1423-0410.2001.00111.xsubject
Has Abstractpub_date
2001-11-01 00:00:00pages
241-7issue
4eissn
0042-9007issn
1423-0410pii
111journal_volume
81pub_type
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