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J. Biol. Chem., Vol. 276, Issue 36, 33345-33352, September 7, 2001
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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 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
Cathepsin B, L, and S Cleave and Inactivate Secretory
Leucoprotease Inhibitor*
, and Laboratory
of Biochemistry, NHLBI, National Institutes of Health,
Bethesda, Maryland 20892-8012
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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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