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Updated: Sep 23, 2026

Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells
Published on: October 27, 2009
Slow internal dynamics of membrane proteins in mechanisms of protease-induced aggregation of platelets
V Mazhul1, T Chernovets, E Zaitseva
1Institute of Photobiology, National Academy of Sciences of Belarus, Akademicheskaya str. 27, 220072 Minsk, Belarus. mazhul@biobel.bas-net.by
Abstract:
Room temperature tryptophan phosphorescence (RTTP) of suspensions of human platelets was studied. RTTP spectra and decay kinetics of both intact platelets and those after short-term incubation with low concentrations of thrombin or trypsin (0.3-50 microg/ml) were investigated. Protease-induced changes in the RTTP lifetime of platelets were observed, and interpreted in terms of the slow internal dynamics of membrane protein modification. The functional role of membrane protein internal dynamics is discussed in the context of platelet aggregation and signal transduction processes.
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