Granulocyte-Macrophage Colony-Stimulating Factor
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Colony-stimulating factor
Interleukin 3
Hematopoietic growth factor
Colony-stimulating factor
Monocyte
Macrophage-activating factor
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Hematopoietic growth factor
Colony-stimulating factor
Monocyte
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Colony-stimulating factor
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FOUR colony-stimulating factors influence the survival, proliferation, differentiation, and functional activation of myeloid hematopoietic cells: macrophage colony-stimulating factor (M-CSF), granulocyte colony-stimulating factor (G-CSF), granulocytemacrophage colony-stimulating factor (GM-CSF), and interleukin-3 (formerly known as multi-colony-stimulating factor).1 2 3 Various other cytokines and factors are also implicated in these processes, including interleukins 1, 5, 6, and 11 and the recently identified Steel factor (variously designated c-kit ligand, mast-cell growth factor, and stem-cell factor).4 , 5 Of these factors, only G-CSF and GM-CSF are commercially available for clinical use. G-CSF has been approved in the United States and major European countries for the reduction of infection after . . .
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Colony-stimulating factor
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Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a well-characterized hematopoietic growth factor. Recently, using purified recombinant-derived material, we have found that GM-CSF is also a potent activator of mature functional macrophages. Thus, we have found that exogenous GM-CSF augments the primary plaque-forming response to sheep red blood cells and that this effect is due to upregulation of la antigen expression and interleukin 1 production by the macrophages. We also show that GM-CSF inhibits the replication of <i>Trypanosoma cruzi </i>in cultured peritoneal macrophages and causes an accelarated clearance of <i>Salmonella typhimurium </i>from the peritoneal cavity of mice. These data indicate that GM-CSF is a multifunctional molecule stimulating both hematopoiesis and mature macrophage function.
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Macrophages are crucial in controlling infectious agents and tissue homeostasis. Macrophages require a wide range of functional capabilities in order to fulfill distinct roles in our body, one being rapid and robust immune responses. To gain insight into macrophage plasticity and the key regulatory protein networks governing their specific functions, we performed quantitative analyses of the proteome and phosphoproteome of murine primary GM-CSF and M-CSF grown bone marrow derived macrophages (GM-BMMs and M-BMMs, respectively) using the latest isobaric tag based tandem mass tag (TMT) labeling and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Strikingly, metabolic processes emerged as a major difference between these macrophages. Specifically, GM-BMMs show significant enrichment of proteins involving glycolysis, the mevalonate pathway, and nitrogen compound biosynthesis. This evidence of enhanced glycolytic capability in GM-BMMs is particularly significant regarding their pro-inflammatory responses, because increased production of cytokines upon LPS stimulation in GM-BMMs depends on their acute glycolytic capacity. In contrast, M-BMMs up-regulate proteins involved in endocytosis, which correlates with a tendency toward homeostatic functions such as scavenging cellular debris. Together, our data describes a proteomic network that underlies the pro-inflammatory actions of GM-BMMs as well as the homeostatic functions of M-BMMs.
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Human macrophage colony-stimulating factor (M-CSF or CSF-1), either in purified or in recombinant form, is able to generate macrophagic colonies in a murine bone marrow colony assay, but only stimulates small macrophagic colonies of 40-50 cells in a human bone marrow colony assay. We report here that recombinant human granulocytic/macrophage colony stimulating factor (rhGM-CSF) at concentrations in the range of picograms enhances the responsiveness of bone marrow progenitors to M-CSF activity, resulting in an increased number of macrophagic colonies of up to 300 cells. Polyclonal antiserum against M-CSF did not alter colony formation of bone marrow progenitors incubated with GM-CSF at optimal concentration (1-10 ng/ml) for these in vitro assays. Thus, GM-CSF at higher concentrations (nanogram range) can by itself, elicit macrophagic colonies, and at lower concentrations (picogram range) acts to enhance the responsiveness of these progenitors to M-CSF.
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Abstract The responsiveness of bone marrow progenitors (BMP) from C3H mice to highly purified or recombinant preparations of Macrophage Colony-Stimulating Factor-1 (CSF-1) and Granulocyte-Macrophage Colony-Stimulating Factor (GM-CSF) was compared by counting the number of colonies (≥ 50 cells) after 10 days in culture with CSF. Cells responsive to CSF-1 or GM-CSF exhibited maximum colony formation over a wide dose range, although GM-CSF supported colony formation at lower concentrations. The response of BMP to optimal concentrations of CSF-1 was ≥5 times greater than the response of BMP to GM-CSF. Analysis of the kinetics of colony formation revealed that, at day 5, the number of BMP responsive to GM-CSF or CSF-1 was approximately equal; the number of CSF-1 colonies increased significantly through day 10, while those cultured in GM-CSF did not. The response of BMP to CSF-1 and GM-CSF was also studied in liquid culture; the differences in yield of mature macrophages was consistent with the differences observed in agar culture. Although both cell populations were shown to be 100% mononuclear by day 7, Coulter Channelyzer analysis of these mature macrophages showed marked differences in cell size distribution. By day 7, cells grown in CSF-1 resulted in a homogeneous population of large cells, whereas GM-CSF cultures showed a heterogeneous distribution. Finally, CSF-1-derived cells possessed increased nonspecific and specific phagocytic capabilities when compared to GM-CSF-derived macrophages. These findings indicate that the actions of GM-CSF and CSF-1 upon the bone marrow compartment results in the generation of mature macrophages which differ morphologically and functionally and may account for the heterogeneity in macrophage populations.
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Colony-stimulating factor
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