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Tumor Progression and Metastasis Program, Karmanos Cancer Institute [H. I., S. A., A. R.], Departments of Pathology and Radiation Oncology, Wayne State University School of Medicine [A. R.], Detroit, Michigan 48201; and Chiron Technologies, Chiron Corporation, Emeryville, California 94608 [K. K.]
Galectin-3 is a ß-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interaction between galectin-3 and Mac-2-binding protein in whole cells and measures their relative expression levels. Incubation of A375 cells with affinity-purified Mac-2-binding protein resulted in its binding to galectin-3 on the cell surface in a specific carbohydrate-dependent manner. Mac-2-binding protein also induced homotypic cell aggregation, which was inhibited by lactose or Fab' fragments of an anti-galectin-3 antibody. Northern blotting analysis revealed differences in the transcriptional regulation of galectin-3 and Mac-2-binding protein. These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3.
1 This work was supported by NIH Grant RO1-CA46120. A. R. is supported in part by the Paul Zuckerman Support Foundation for Cancer Research.
2 Present address: Department of Otolaryngology, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565, Japan.
3 To whom requests for reprints should be addressed, at Tumor Progression and Metastasis Program, Karmanos Cancer Institute, 110 East Warren Avenue, Detroit, MI 48201. Phone: (313) 833-0960; Fax: (313) 831-7518.
Received 5/16/96. Accepted 8/ 1/96.
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