Ym1 is a neutrophil granule protein that crystallizes in p47phox-deficient mice

J Biol Chem. 2002 Feb 15;277(7):5468-75. doi: 10.1074/jbc.M110635200. Epub 2001 Dec 3.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Embryo, Mammalian / cytology*
  • Hydrogen-Ion Concentration
  • Immunohistochemistry
  • Inflammation / metabolism*
  • Kinetics
  • Lectins / metabolism*
  • Lung / metabolism
  • Mice
  • Mice, Knockout
  • Models, Genetic
  • Mutagenesis, Site-Directed
  • NADPH Oxidases
  • Neutrophils / metabolism
  • Phosphoproteins / genetics*
  • Phosphoproteins / metabolism*
  • Stem Cells / cytology*
  • Subcellular Fractions
  • Time Factors
  • Tissue Distribution
  • beta-N-Acetylhexosaminidases / metabolism

Substances

  • Lectins
  • Phosphoproteins
  • NADPH Oxidases
  • neutrophil cytosolic factor 1
  • Chil3 protein, mouse
  • beta-N-Acetylhexosaminidases