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  • Title: Incorporation of an Asp-Ser sequence to form an RGDS-like motif in hirutonin: the effect on in vitro platelet function.
    Author: van Wyk V, Leblond L, Winocour PD, Devine DV, Gyongyossy-Issa MI.
    Journal: Thromb Res; 2000 Aug 15; 99(4):343-52. PubMed ID: 10963785.
    Abstract:
    We investigated the effect on in vitro platelet function of hirutonin, a modified hirutonin with an RGD-like motif, a pseudo-RGDS peptide and a linear RGDS peptide. Inhibition of expression of surface fibrinogen on ADP-activated platelets with 40 microM of the peptide was as follows: hirutonin 10+/-3%, modified chimeric peptide 26+/-5%, pseudo-RGDS 66+/-11% and linear RGDS 93+/-13%. Both hirutonin and the chimeric peptide significantly inhibited ADP-induced platelet activation as detected by CD62 expression. Unlike the RGDS and pseudo-RGDS controls, neither the chimeric peptide nor the parent hirutonin inhibited ADP-induced platelet aggregation even at 140 microM. The chimeric hirutonin peptide reduced ATP release from ADP-stimulated platelets by 40+/-4%. This inhibition was stronger than that caused by hirutonin (23+/-13%), but less than the RGDS (90+/-2%) and pseudo RGDS-peptides (59+/-11%). Primary platelet haemostasis was slightly but not significantly affected by the peptide at 40 and 80 microM. However, shear-induced platelet adhesion to vWF and especially subsequent aggregate formation was interrupted after the addition of the chimeric peptide. Similar results were obtained with hirutonin. This inhibition was not as marked as with the RGDS- and pseudo-RGDS peptides. Both the parent hirutonin and the chimeric peptide caused prolongation of the clinical coagulation assays aPTT and TT. In conclusion, the chimeric hirutonin peptide with introduction of the RGD motif retained its anticoagulant effect but had little formal disintegrin activity. Instead, it appeared to have novel anti-platelet effects that may be of therapeutic use.
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