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Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and prolif... more Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and proliferation. In different circumstances,
it acts as a mitogen, as an inhibitor of cell proliferation, and as a promoter of cellular apoptosis. Many of
these activities, particularly the mitogenic and apoptotic responses, follow from the interaction of galectin-1 with cellsurface
β-galactoside ligands, but there is increasing evidence for protein-protein interactions involving galectin-1, and
for a β-galactoside-independent cytostatic mechanism. The bifunctional nature of galectin-1, in conjunction with other
experimental variables, makes it difficult to assess the overall outcomes and significance of the growth-regulatory actions
in many previous investigations. There is thus a need for well-defined experimental cross-correlation of observations,
for which specific loss-of-function galectin-1 mutants will be invaluable. Unsurprisingly, in view of this background, the
interpretation of the actions of galectin-1 in developmental situations, both normal and neoplastic, is often very complex.
Published in 2004.
Keywords: galectin-1, cell regulation, growth inhibition, differentiation, cancer, metastasis
Abstract Human soluble galactose-binding lectin (galectin-1) has been expressed as an Escherich... more 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 β-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 β-galactoside-binding site. At lower concentrations, recombinant galectin-1 is mitogenic, this activity being susceptible to inhibition by lactose, and thus attributable to the β-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.
Keywords
Galectin-1;
Lectin;
Fusion protein;
Cell growth control;
Proteinase
Glycoconjugate Journal, 2002
Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and prolif... more Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and proliferation. In different circumstances, it acts as a mitogen, as an inhibitor of cell proliferation, and as a promoter of cellular apoptosis. Many of these activities, particularly the mitogenic and apoptotic responses, follow from the interaction of galectin-1 with cell-surface β-galactoside ligands, but there is increasing evidence for protein-protein interactions involving galectin-1, and for a β-galactoside-independent cytostatic mechanism. The bifunctional nature of galectin-1, in conjunction with other experimental variables, makes it difficult to assess the overall outcomes and significance of the growth-regulatory actions in many previous investigations. There is thus a need for well-defined experimental cross-correlation of observations, for which specific loss-of-function galectin-1 mutants will be invaluable. Unsurprisingly, in view of this background, the interpretation of the actions of galectin-1 in developmental situations, both normal and neoplastic, is often very complex. Published in 2004.
Biochimica Et Biophysica Acta-molecular Cell Research, 1996
Human soluble galactose-binding lectin (galectin-1) has been expressed as an Escherichia coli fus... more 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 /3-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 /3-galactoside-binding site. At lower concentrations, recombinant galectin-I is mitogenic, this activity being susceptible to inhibition by lactose, and thus attributable to the /3-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.
Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and prolif... more Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and proliferation. In different circumstances,
it acts as a mitogen, as an inhibitor of cell proliferation, and as a promoter of cellular apoptosis. Many of
these activities, particularly the mitogenic and apoptotic responses, follow from the interaction of galectin-1 with cellsurface
β-galactoside ligands, but there is increasing evidence for protein-protein interactions involving galectin-1, and
for a β-galactoside-independent cytostatic mechanism. The bifunctional nature of galectin-1, in conjunction with other
experimental variables, makes it difficult to assess the overall outcomes and significance of the growth-regulatory actions
in many previous investigations. There is thus a need for well-defined experimental cross-correlation of observations,
for which specific loss-of-function galectin-1 mutants will be invaluable. Unsurprisingly, in view of this background, the
interpretation of the actions of galectin-1 in developmental situations, both normal and neoplastic, is often very complex.
Published in 2004.
Keywords: galectin-1, cell regulation, growth inhibition, differentiation, cancer, metastasis
Abstract Human soluble galactose-binding lectin (galectin-1) has been expressed as an Escherich... more 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 β-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 β-galactoside-binding site. At lower concentrations, recombinant galectin-1 is mitogenic, this activity being susceptible to inhibition by lactose, and thus attributable to the β-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.
Keywords
Galectin-1;
Lectin;
Fusion protein;
Cell growth control;
Proteinase
Glycoconjugate Journal, 2002
Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and prolif... more Galectin-1 has demonstrated a diverse range of activities in relation to cell survival and proliferation. In different circumstances, it acts as a mitogen, as an inhibitor of cell proliferation, and as a promoter of cellular apoptosis. Many of these activities, particularly the mitogenic and apoptotic responses, follow from the interaction of galectin-1 with cell-surface β-galactoside ligands, but there is increasing evidence for protein-protein interactions involving galectin-1, and for a β-galactoside-independent cytostatic mechanism. The bifunctional nature of galectin-1, in conjunction with other experimental variables, makes it difficult to assess the overall outcomes and significance of the growth-regulatory actions in many previous investigations. There is thus a need for well-defined experimental cross-correlation of observations, for which specific loss-of-function galectin-1 mutants will be invaluable. Unsurprisingly, in view of this background, the interpretation of the actions of galectin-1 in developmental situations, both normal and neoplastic, is often very complex. Published in 2004.
Biochimica Et Biophysica Acta-molecular Cell Research, 1996
Human soluble galactose-binding lectin (galectin-1) has been expressed as an Escherichia coli fus... more 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 /3-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 /3-galactoside-binding site. At lower concentrations, recombinant galectin-I is mitogenic, this activity being susceptible to inhibition by lactose, and thus attributable to the /3-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.