Affiliations: University of Lisbon Medical School, Santa Maria Hospital, Lisbon, Portugal | Institute of Biochemistry, Institute of Molecular Medicine, University of Lisbon Medical School, Lisbon, Portugal
Note: [] Corresponding author: J. Pedro Lopes de Almeida, Instituto de Bioquímica, Instituto de Medicina Molecular, Faculdade de Medicina de Lisboa, Edifício Egas Moniz, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal. Tel.: +351 91 8985450; Fax: +351 21 7999477; E-mail: jpedro.gla@gmail.com
Abstract: Recent evidence has shown that plasma fibrinogen, a major cardiovascular risk factor, interacts with the erythrocyte membrane and acts to influence blood flow via erythrocyte nitric oxide (NO) modulation. In the present in-vitro study, whole blood samples were harvested from healthy subjects and aliquots were incubated in the absence (control aliquots) and presence of fibrinogen at different degrees of band 3 phosphorylation, and the erythrocyte deformability was determined. The present study shows that in the presence of higher fibrinogen concentrations, similar to those found in inflammatory conditions, erythrocyte deformability is increased only when band 3 is dephosphorylated by the presence of syk inhibitor and at low shear stress. On the contrary, no changes were verified in the presence of fibrinogen when band 3 is allowed to be phosphorylated by inhibiting the phosphotyrosine phosphatase enzyme activity with calpeptin. We also observed that the presence of fibrinogen at higher concentration does not induce changes in erythrocyte deformability in the absence of modulators of the band 3 phosphorylation degree. However, the mechanisms by which fibrinogen signalling modulates erythrocyte function remain to be clarified and are currently under study.
Keywords: Band 3 protein, erythrocyte, deformability, fibrinogen
