Fibrino(geno)lytic Properties of Purified Hementerin, a Metalloproteinase from the Leech Haementeria depressa

Ana Marisa Chudzinski-Tavassi; Eva Maria A. Kelen; Ana Paula de Paula Rosa; Stephane Loyau; Claudio A. M. Sampaio; Cassian Bon; Eduardo Anglés-Cano

doi:10.1055/s-0037-1615155

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1998; 80(01): 155-160
DOI: 10.1055/s-0037-1615155

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Schattauer GmbH

Fibrino(geno)lytic Properties of Purified Hementerin, a Metalloproteinase from the Leech Haementeria depressa

Ana Marisa Chudzinski-Tavassi

¹Laboratório de Fisiopatologia, Instituto Butantan, São Paulo, Brasil

,

Eva Maria A. Kelen

²Institut National de la Santé et de la Recherche Medicale, Unité 143, Hôpital de Bicêtre, France

,

Ana Paula de Paula Rosa

¹Laboratório de Fisiopatologia, Instituto Butantan, São Paulo, Brasil

,

Stephane Loyau

²Institut National de la Santé et de la Recherche Medicale, Unité 143, Hôpital de Bicêtre, France

,

Claudio A. M. Sampaio

³Departamento de Bioquímica e Biologia Molecular, Escola Paulista de Medicina, São Paulo, Brasil

,

Cassian Bon

⁴Unité des Venins, Institut Pasteur, Paris, France

,

Eduardo Anglés-Cano

²Institut National de la Santé et de la Recherche Medicale, Unité 143, Hôpital de Bicêtre, France

› Author Affiliations

Abstract

Summary

The fibrino(geno)lytic protein designated hementerin contained in crude extracts of the salivary complex of Haementeria depressa leeches was purified to apparent homogeneity by gel filtration, ion exchange chromatography and preparative SDS-PAGE. It is a single-chain 80 kDa, PhMeSO₂F-resistant, calcium-dependent, metalloproteinase, which specifically degrades fibrin(ogen) through a plasminogen-independent pathway. The amino terminal sequence of 8 residues shows 80% similarity with hementin, another fibrino(geno)lytic protein purified from Haementeria ghilianii leeches. However, their activities differ somewhat in terms of kinetics and with regard to the structure of the fibrin(ogen) fragments they may produce. Cleavage by hementerin of fibrinogen Aα, γ and Bβ chains, in that order, produces 270 kDa to 67 kDa fragments which differ from those produced by plasmin. Hementerin was also able to degrade cross-linked fibrin although at a lower rate as compared to fibrinogen. In conclusion, hementerin is a plasminogen-independent fibrino(geno)lytic metalloproteinase that degrades fibrinogen faster than fibrin, prevents blood coagulation and destroys fibrin clots in vitro.

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References

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