Nitridergic Platelet Pathway Activation by Hementerin, a Metalloprotease from the Leech Haementeria depressa
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A. M. Chudzinski-Tavassi
Abstract
Hementerin (HT) is an 80 kDa fibrino(geno)lytic metalloprotease, purified from saliva of the leech Haementeria depressa. In the present report, the effect of HT on several functional parameters of human platelets was assessed. HT inhibited platelet aggregation and ATP release induced by different agonists such as ADP, adrenaline, collagen, thrombin, and arachidonic acid. HT did neither modify the expression of platelet glycoproteins (Ib, IIb-IIIa, Ia-IIa, IV) nor intraplatelet fibrinogen levels, whereas it markedly decreased CD62P and CD63 levels after the stimulation with thrombin. HT significantly increased thrombininduced platelet Ca[2+] intracellular levels, cGMP content and nitric oxide synthase (NOS) activity. The effect of HT on platelet aggregation was reversed by two NOS inhibitors, Nω-Nitro-L-arginine methyl ester and 2 NG-Nitro-L-arginine. In summary, these results indicate that HT is an effective inhibitor of human platelet aggregation, presumably through activation of the platelets nitridergic pathway.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Paper of the Year 2002
- Terminal Differentiation of Epithelia
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- Protein Structure Similarity as Guiding Principle for Combinatorial Library Design
- The Making of a Professional Secretory Cell: Architectural and Functional Changes in the ER during B Lymphocyte Plasma Cell Differentiation
- No Superoxide Dismutase Activity of Cellular Prion Protein in vivo
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- Phosphatidylinositol-3,5-Bisphosphate Is a Potent and Selective Inhibitor of Acid Sphingomyelinase
- Function and Structure of N-Terminal and C-Terminal Domains of Calcineurin B Subunit
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- Nitridergic Platelet Pathway Activation by Hementerin, a Metalloprotease from the Leech Haementeria depressa
