Cristina Weinberg | Massey University (original) (raw)

Uploads

Papers by Cristina Weinberg

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.

International Dairy Journal, 2002

A synthetic gene for bovine b-lactoglobulin-variant-A (b-LgA), designed to incorporate a number o... more A synthetic gene for bovine b-lactoglobulin-variant-A (b-LgA), designed to incorporate a number of restriction sites to form suitable ''cassettes'' for future site-directed mutagenesis experiments, was constructed as three separate fragments, F1, F2 and F3. F1 was made using the shotgun approach while F2 and F3 were synthesised using PCR.

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.

International Dairy Journal, 2002

A synthetic gene for bovine b-lactoglobulin-variant-A (b-LgA), designed to incorporate a number o... more A synthetic gene for bovine b-lactoglobulin-variant-A (b-LgA), designed to incorporate a number of restriction sites to form suitable ''cassettes'' for future site-directed mutagenesis experiments, was constructed as three separate fragments, F1, F2 and F3. F1 was made using the shotgun approach while F2 and F3 were synthesised using PCR.

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.