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Originally published In Press as doi:10.1074/jbc.M103220200 on July 2, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33345-33352, September 7, 2001
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Cathepsin B, L, and S Cleave and Inactivate Secretory Leucoprotease Inhibitor*

Clifford C. Taggart, Gregory J. Lowe, Catherine M. Greene, Alan T. Mulgrew, Shane J. O'Neill, Rodney L. LevineDagger , and Noel G. McElvaney§

From the Pulmonary Research Division, Department of Medicine, The Royal College of Surgeons in Ireland, Education and Research Centre, Beaumont Hospital, Dublin 9, Ireland and the Dagger  Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-8012

A number of serine proteases, matrix metalloproteases, and cysteine proteases were evaluated for their ability to cleave and inactivate the antiprotease, secretory leucoprotease inhibitor (SLPI). None of the serine proteases or the matrix metalloproteases examined cleaved the SLPI protein. However, incubation with cathepsins B, L, and S resulted in the cleavage and inactivation of SLPI. All three cathepsins initially cleaved SLPI between residues Thr67 and Tyr68. The proteolytic cleavage of SLPI by all three cathepsins resulted in the loss of the active site of SLPI and the inactivation of SLPI anti-neutrophil elastase capacity. Cleavage and inactivation were catalytic with respect to the cathepsins, so that the majority of a 400-fold excess of SLPI was inactivated within 15 min by cathepsins L and S. Analysis of epithelial lining fluid samples from individuals with emphysema indicated the presence of cleaved SLPI in these samples whereas only intact SLPI was observed in control epithelial lining fluid samples. Active cathepsin L was shown to be present in emphysema epithelial lining fluid and inhibition of this protease prevented the cleavage of recombinant SLPI added to emphysema epithelial lining fluid. Taken together with previous data that demonstrates that cathepsin L inactivates alpha 1-antitrypsin, these findings indicate the involvement of cathepsins in the diminution of the lung antiprotease screen possibly leading to lung destruction in emphysema.

* This work was supported by the Health Research Board of Ireland, the Higher Education Authority of Ireland, the Charitable Infirmary Charitable Trust, and the Royal College of Surgeons in Ireland.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.

§ To whom correspondence should be addressed: Royal College of Surgeons in Ireland, Education and Research Center, Beaumont Hospital, Dublin 9, Ireland. Tel.: 353-8093764; Fax: 353-8093765; E-mail: gmcelvaney@rcsi.ie.

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