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Inhibition of -thrombin-induced human platelet aggregation by histone H1subtypes and H1.3 fragments
Journal article

Inhibition of -thrombin-induced human platelet aggregation by histone H1subtypes and H1.3 fragments

Gerald Soslau, Phillip J. Prest, Reiner Class, Monika Jost and Lynn Mathews
Platelets (Edinburgh), v 20(5), pp 349-356
2009
PMID: 19637099

Abstract

Human platelets are differentially activated by varying concentrations of -thrombin or by - and -thrombin via three thrombin receptors, PAR-1, PAR-4 and GPIb \tilde \alpha . It is likely that the development of a normal or abnormal hemostatic event in humans is dictated, in part, by the selective activation of these receptors. The ability to differentially inhibit these thrombin receptors could, therefore, have clinical significance. We have previously demonstrated that histone H1 selectively inhibits the PAR-4 receptor. In the current study we investigated whether five subtypes of the H1 molecule or fragments of the H1.3 subtype differentially inhibited the PAR-4 receptor. PAR-4 inhibition by all H1 subtypes was saturated at 1 uM with no statistical difference observed with the five H1 subtypes tested. Of the five fragments generated from the H1.3 molecule only one had significant inhibitory activity against PAR-4. The C-terminal fragment, N.1, generated by the proteolysis of the parent molecule by Asp-N endoproteinase (Aeromonas proteolytica) at the single aspartate residue, showed the same level of PAR-4 inhibition as the intact H1.3 at 1 uM concentrations. Removal of two N-terminal amino acids (Asp-Val as determined by MALDI analysis) from the N.1 fragment further enhanced its inhibitory activity. These studies may help to develop specific drugs to differentially inhibit the platelet thrombin receptors.

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Collaboration types
International collaboration
Web of Science research areas
Cell Biology
Hematology
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