1. Biphasic modulation of cell growth by recombinant human galectin-1.
- Author
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Adams L, Scott GK, and Weinberg CS
- Subjects
- Amino Acid Sequence, Base Sequence, Cell Line, DNA, Complementary genetics, Electrophoresis, Polyacrylamide Gel, Erythrocytes drug effects, Escherichia coli genetics, Galectin 1, Gene Expression, Glutathione Transferase, Hemagglutination drug effects, Hemagglutinins genetics, Humans, Molecular Sequence Data, Polymerase Chain Reaction, Recombinant Fusion Proteins pharmacology, Recombinant Proteins pharmacology, Thrombin metabolism, Tumor Cells, Cultured, Cell Division drug effects, Hemagglutinins pharmacology, Lectins pharmacology
- Abstract
Human soluble galactose-binding lectin (galectin-1) has been expressed as an Escherichia coli fusion protein, following the amplification by polymerase chain reaction of cDNA prepared from a human osteosarcoma cell line. The fusion protein is a functional beta-galactoside-binding lectin, as is the recombinant galectin when purified from the cleaved fusion protein. The recombinant galectin has a biphasic effect on cell proliferation. Unlike the fusion protein, it functions as a human cell growth inhibitor, confirming earlier findings with natural human galectin-1, though it is less effective than the natural galectin. This reaction is not significantly inhibited by lactose, and is thus largely independent of the beta-galactoside-binding site. At lower concentrations, recombinant galectin-1 is mitogenic, this activity being susceptible to inhibition by lactose, and thus attributable to the beta-galactoside-binding ability of the protein. Some tumour cells are susceptible to the growth-inhibitory effect, and the galectin-1 gene is expressed in both normal and tumour cells.
- Published
- 1996
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