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Originally published In Press as doi:10.1074/jbc.M003820200 on October 2, 2000

J. Biol. Chem., Vol. 276, Issue 2, 944-951, January 12, 2001
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Cathepsin B Activity Regulation
HEPARIN-LIKE GLYCOSAMINOGLYCANS PROTECT HUMAN CATHEPSIN B FROM ALKALINE pH-INDUCED INACTIVATION*

Paulo C. AlmeidaDagger , Iseli L. NantesDagger , Jair R. ChagasDagger , Cláudia C. A. RizziDagger , Adelaide Faljoni-Alario§, Euridice Carmona, Luiz Juliano||, Helena B. Nader**, and Ivarne L. S. TersariolDagger Dagger Dagger

From the Dagger  Centro Interdisciplinar de Investigação Bioquímica, Universidade de Mogi das Cruzes, Prédio I, Centro de Ciências Tecnológicas, sala 1S-15, Av. Dr. Candido X. de Almeida Souza 200, CEP 08780-911, Mogi das Cruzes, SP, Brazil, § Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil,  Laboratório de Farmacologia, Instituto Butantã, São Paulo, SP, Brazil, and || Departamento de Biofísica and the ** Disciplina de Biologia Molecular, Universidade Federal de São Paulo/Escola Paulista de Medicina, Instituto Nacional de Farmacologia, São Paulo, SP, Brazil

It has been shown that lysosomal cysteine proteinases, specially cathepsin B, has been implicated in a variety of diseases involving tissue remodeling states, such as inflammation, parasite infection, and tumor metastasis, by degradation of extracellular matrix components. Recently, we have shown that heparin and heparan sulfate bind to papain specifically; this interaction induces an increase of its alpha -helix content and stabilizes the enzyme structure even at alkaline pH (Almeida, P. C., Nantes, I. L., Rizzi, C. C. A., Júdice, W. A. S., Chagas, J. R., Juliano, L., Nader, H. B., and Tersariol, I. L. S. (1999) J. Biol. Chem. 274, 30433-30438). In the present work, a combination of circular dichroism analysis, affinity chromatography, cathepsin B mutants, and fluorogenic substrate assays were used to characterize the interaction of human cathepsin B with glycosaminoglycans. The nature of the cathepsin B-glycosaminoglycans interaction was sensitive to the charge and type of polysaccharide. Like papain, heparin and heparan sulfate bind cathepsin B specifically, and this interaction reduces the loss of cathepsin B alpha -helix content at alkaline pH. Our data show that the coupling of cathepsin B with heparin or heparan sulfate can potentiate the endopeptidase activity of the cathepsin B, increasing 5-fold the half-life (t1/2) of the enzyme at alkaline pH. Most of these effects are related to the interaction of heparin and heparan sulfate with His111 residue of the cathepsin B occluding loop. These results strongly suggest that heparan sulfate may be an important binding site for cathepsin B at cell surface, reporting a novel physiological role for heparan sulfate proteoglycans.

* This work was supported by Fundação de Amparo à Pesquisa do Estado de São Paulo Grants 97/13133-4 and Fundação de Amparo ao Ensino e Pesquisa Universidade de Mogi das Cruzes, SP, Brazil.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Dagger To whom correspondence should be addressed. Tel.: 55-11-4798-7102; E-mail: ivarne@ccb.umc.br.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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