Abstract
Galectin-3 is a member of a growing family of β-galactoside-binding animal lectins. It has been shown that the expression of galectin-3 is upregulated in proliferating cells, suggesting a possible role for this lectin in cell growth regulation. To definitely establish its function, we examined growth properties of human leukemia T cells transfected with galectin-3 cDNA. Transfectants expressing galectin-3 displayed higher growth rates than control transfectants which do not express this lectin. Furthermore, galectin-3 expression in these cells confers resistance to apoptosis induced by anti-Fas antibody and staurosporine. Galectin-3 was found to have significant sequence similarity to bcl-2, a well established inhibitor of apoptosis. In particular, the lectin contains the NWGR motif that is highly conserved in the BH1 domain among members of the bcl-2 family and shown to be critical for apoptosis-suppressing activity of bel 2. We further demonstrated that galectin-3 interacts through its lectin domain with bcl-2 in a lactose-inhibitable manner. Ga]ectin-3 also interacts with two other members of the bcl-2 family, bcl-Xs and bak, both being promoters of apoptosis. Sequence homology to bcl-2 and interactions with the bci-2 family members suggest that the lectin may participate in the control of cell growth and apoptosis by interacting with members of the bcl-2 family.
Original language | English (US) |
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Pages (from-to) | A1088 |
Journal | FASEB Journal |
Volume | 10 |
Issue number | 6 |
State | Published - 1996 |
Externally published | Yes |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Genetics