1. Molecular cloning of a human macrophage lectin specific for galactose.
- Author
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Cherayil BJ, Chaitovitz S, Wong C, and Pillai S
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular methods, Galectin 3, Gene Library, Humans, Lectins metabolism, Mice, Molecular Sequence Data, Restriction Mapping, Sequence Homology, Nucleic Acid, Transcription, Genetic, Antigens, Differentiation genetics, Galactose metabolism, Lectins genetics, Macrophages immunology
- 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.
- Published
- 1990
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