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Originally published In Press as doi:10.1074/jbc.M100223200 on February 23, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18551-18556, May 25, 2001
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Dipeptidyl Peptidase I Is Essential for Activation of Mast Cell Chymases, but Not Tryptases, in Mice*

Paul J. WoltersDagger §, Christine T. N. Pham||, Diego J. MuilenburgDagger , Timothy J. Ley**, and George H. CaugheyDagger

From the Dagger  Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, California 94143-0911 and the  Departments of Internal Medicine, || Pathology and Immunology, and ** Genetics, Washington University School of Medicine, St. Louis, Missouri 63110-1093

Dipeptidyl peptidase I (DPPI) is the sole activator in vivo of several granule-associated serine proteases of cytotoxic lymphocytes. In vitro, DPPI also activates mast cell chymases and tryptases. To determine whether DPPI is essential for their activation in vivo, we used enzyme histochemical and immunohistochemical approaches and solution-based activity assays to study these enzymes in tissues and bone marrow-derived mast cells (BMMCs) from DPPI +/+ and DPPI -/- mice. We find that DPPI -/- mast cells contain normal amounts of immunoreactive chymases but no chymase activity, indicating that DPPI is essential for chymase activation and suggesting that DPPI -/- mice are functional chymase knockouts. The absence of DPPI and chymase activity does not affect the growth, granularity, or staining characteristics of BMMCs and, despite prior predictions, does not alter IgE-mediated exocytosis of histamine. In contrast, the level of active tryptase (mMCP-6) in DPPI -/- BMMCs is 25% that of DPPI +/- BMMCs. These findings indicate that DPPI is not essential for mMCP-6 activation but does influence the total amount of active mMCP-6 in mast cells and therefore may be an important, but not exclusive mechanism for tryptase activation.

* This work was supported in part by the American Lung Association of California and National Institutes of Health Grants HL-04055 (to P. J. W.), HL-03774 (to C. T. N. P.), DK-49786 (to T. J. L.), and HL-24136 (to G. H. C.).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: University of California, San Francisco, Box 0911, San Francisco, CA 94143-0911. Tel.: 415-514-2601; Fax: 415-476-9749; E-mail: pjwolt@itsa.ucsf.edu.

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