Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages

Eur J Biochem. 1998 Jan 15;251(1-2):504-9. doi: 10.1046/j.1432-1327.1998.2510504.x.


In various mammals, enzymatically active and inactive members of family 18 glycosyl hydrolases, containing chitinases, have been identified. In man, chitotriosidase is the functional chitinolytic enzyme, whilst the homologous human cartilage 39-kDa glycoprotein (HC gp-39) does not exhibit chitinase activity and its function is unknown. This study establishes that HC gp-39 is a chitin-specific lectin. It is experimentally demonstrated that a single amino acid substitution in the catalytic centre of the 39-kDa isoform of chitotriosidase, which generates a similar sequence to that in HC gp-39, results in a loss of hydrolytic activity and creates the capacity to bind to chitin. The possible implication of the finding for chitinolytic and chitin-binding proteins that are produced in high quantities by activated macrophages are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipokines
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • COS Cells
  • Cells, Cultured
  • Chitin / metabolism*
  • Chitinase-3-Like Protein 1
  • Glycoproteins / metabolism*
  • Hexosaminidases / genetics
  • Hexosaminidases / metabolism*
  • Humans
  • Lectins
  • Macrophages / enzymology
  • Macrophages / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Sequence Homology, Amino Acid


  • Adipokines
  • CHI3L1 protein, human
  • Chitinase-3-Like Protein 1
  • Glycoproteins
  • Lectins
  • Chitin
  • Hexosaminidases
  • chitotriosidase

Associated data

  • GENBANK/M94584