Molecular cloning of a human macrophage lectin specific for galactose

Proc Natl Acad Sci U S A. 1990 Sep;87(18):7324-8. doi: 10.1073/pnas.87.18.7324.

Abstract

The murine Mac-2 protein is a galactose- and IgE-binding lectin secreted by inflammatory macrophages. We describe here the cloning and characterization of a cDNA representing the human homolog of Mac-2 (hMac-2). The amino acid sequence derived from the hMac-2 cDNA indicates that the protein is evolutionarily highly conserved, with 85% of its amino acid residues being similar to those in the murine homolog. This conservation is especially marked in the carboxyl-terminal lectin domain. The amino-terminal half of the protein is less conserved but still contains the repetitive proline-glycine-rich motif seen in the mouse protein. hMac-2 synthesized in vitro is recognized by the M3/38 monoclonal antibody to Mac-2 and binds to the desialylated glycoprotein asialofetuin and to laminin, a major component of basement membranes. These findings are discussed in the context of the potential functions of hMac-2.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Differentiation / genetics*
  • Base Sequence
  • Cloning, Molecular / methods
  • Galactose / metabolism*
  • Galectin 3
  • Gene Library
  • Humans
  • Lectins / genetics*
  • Lectins / metabolism
  • Macrophages / immunology*
  • Mice
  • Molecular Sequence Data
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid
  • Transcription, Genetic

Substances

  • Antigens, Differentiation
  • Galectin 3
  • Lectins
  • Galactose

Associated data

  • GENBANK/M35368