Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04141 (granulocyte-macrophage colony-stimulating factor)
 6,790 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The expression of galectin-3 (formerly known as IgE-binding protein or Mac-2) in rat bone marrow (BM) was investigated by FACS, immunocytochemical and immunoblot analysis. The functional significance of rat recombinant galectin-3 on mouse recombinant granulocyte-macrophage colony-stimulating factor (GM-CSF)-driven proliferation of macrophage progenitors and gene transcription was further examined. Immunocytochemical analysis of in situ BM sections demonstrated galectin-3 in myelopoietic cells and surrounding stroma, whereas erythropoietic and lymphopoietic environments essentially lacked galectin-3 expression. FACS analysis demonstrated that incubation of freshly isolated BMC with lactose, a competing ligand for galectin-3 binding to glycoconjugates, decreased binding of antigalectin antibodies to cells primarily expressing the myeloid antigen recognized by mAb His-54. Similarly, lectin-mediated binding of exogenous galectin-3 to myeloid lineage cells was also demonstrated. Immunoblot analysis of BM eluates demonstrated galectin-3 both in the extracellular matrix and in a lactose elutable form, bound to the surface of BMC. [3H]Thymidine incorporation studies on BMC cultured in the presence of galectin-3 demonstrated suppression of GM-CSF-induced proliferation by galectin-3. In addition, differential display analysis of immediate early gene expression in BMC cultured in the presence of galectin-3 revealed a 76.2% inhibition of GM-CSF-induced gene transcription by galectin-3 assessed by the number of PCR-fragments generated. Our data suggest a role for galectin-3 in the organization of myelopoietic compartments in rat BM and regulation of the action of growth factors on myelopoietic precursor cells.
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PMID:Galectin-3 inhibits granulocyte-macrophage colony-stimulating factor (GM-CSF)-driven rat bone marrow cell proliferation and GM-CSF-induced gene transcription. 924 34

In the present study we have analyzed the expression of galectin-3, a beta-galactoside-specific soluble animal lectin, by microglial cells in vitro. In enriched microglial cell cultures derived from neonatal mouse brain after 2 to 3 weeks in vitro, almost all microglial cells expressed galectin-3 intracellularly and about 90% expressed the molecule on the cell surface. Western blot analyses of lysates from microglial cells using galectin-3-specific antibodies revealed a single band with an apparent molecular weight of 29 kD. The carbohydrate recognition domain of microglia-derived galectin-3 was functional as the molecule could be affinity purified on lactose-agarose. Upon an incubation with lactose-, but not with sucrose-containing buffers the amount of cell surface expressed galectin-3 was strongly reduced, suggesting that the molecule appears to be associated with the plasma membrane via its carbohydrate recognition domain. The total amount as well as the portion of cell surface expressed galectin-3 increased upon treatment with granulocyte-macrophage colony-stimulating factor. Our findings suggest that galectin-3 expression is subject to regulation by growth factors supposed to be involved in the cascade of microglial activation under pathological conditions.
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PMID:Murine microglial cells express functionally active galectin-3 in vitro. 945 8