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Originally published In Press as doi:10.1074/jbc.M110635200 on December 3, 2001

J. Biol. Chem., Vol. 277, Issue 7, 5468-5475, February 15, 2002
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Ym1 Is a Neutrophil Granule Protein That Crystallizes in p47phox-deficient Mice*

Marcus HarbordDagger §, Marco Novelli, Benito CanasDagger , David PowerDagger , Christine Davis||, Jasminka Godovac-ZimmermannDagger , Jürgen RoesDagger **, and Anthony W. SegalDagger **

From the Departments of Dagger  Medicine, || Anatomy, and  Histopathology, University College London, London WC1E 6JJ, United Kingdom

Crystals were discovered within the aged lung and at sites of chronic inflammation in a mouse model of chronic granulomatous disease. Following re-crystallization at neutral pH, the crystals were identified as the chitinase-like protein Ym1, expressed in organs of the lymphoreticular system, the lung, and distal stomach. Ym1 was shown to be a neutrophil granule protein and to have weak beta -N-acetylglucosaminidase activity, indicating that it might contribute to the digestion of glycosaminoglycans. Crystal formation is likely to be a function of excess neutrophil turnover at sites of inflammation in the chronic granulomatous disease mouse. Failure to remove subcutaneous Ym1 crystals injected into knockout mice indicates that a failure of digestion may also contribute to crystallization.

* This work was supported by the Wellcome Trust and the Chronic Granulomatous Disease Trust.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: The Rayne Institute, 5 University St., London WC1E 6JJ, UK. Tel.: 44-207-209-6173; Fax: 44-207-209-6211; E-mail: doc@dircon.co.uk.

** Both authors contributed equally to the work.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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