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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
1   Laboratório de Fisiopatologia, Instituto Butantan, São Paulo, Brasil
,
Eva Maria A. Kelen
2   Institut National de la Santé et de la Recherche Medicale, Unité 143, Hôpital de Bicêtre, France
,
Ana Paula de Paula Rosa
1   Laboratório de Fisiopatologia, Instituto Butantan, São Paulo, Brasil
,
Stephane Loyau
2   Institut National de la Santé et de la Recherche Medicale, Unité 143, Hôpital de Bicêtre, France
,
Claudio A. M. Sampaio
3   Departamento de Bioquímica e Biologia Molecular, Escola Paulista de Medicina, São Paulo, Brasil
,
Cassian Bon
4   Unité des Venins, Institut Pasteur, Paris, France
,
Eduardo Anglés-Cano
2   Institut National de la Santé et de la Recherche Medicale, Unité 143, Hôpital de Bicêtre, France
› Author Affiliations
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Publication History

Received 26 November 1997

Accepted after revision 19 March 1998

Publication Date:
27 December 2017 (online)

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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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