scholarly journals Colony-stimulating factor 1 regulates CTP: phosphocholine cytidylyltransferase mRNA levels.

1991 ◽  
Vol 266 (25) ◽  
pp. 16261-16264
Author(s):  
T.G. Tessner ◽  
C.O. Rock ◽  
G.B. Kalmar ◽  
R.B. Cornell ◽  
S. Jackowski
Keyword(s):  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Phosphocholine Cytidylyltransferase ◽  
Stimulating Factor

scholarly journals Eosinophil Deficiency Compromises Lung Defense against Aspergillus fumigatus

2013 ◽  
Vol 82 (3) ◽  
pp. 1315-1325 ◽  
Author(s):  
Lauren M. Lilly ◽  
Michaella Scopel ◽  
Michael P. Nelson ◽  
Ashley R. Burg ◽  
Chad W. Dunaway ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Allergic Bronchopulmonary Aspergillosis ◽  
Cell Contact ◽  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Content Type ◽  
Eosinophil Peroxidase ◽  
Stimulating Factor ◽  
Deficient Mice

ABSTRACTExposure to the moldAspergillus fumigatusmay result in allergic bronchopulmonary aspergillosis, chronic necrotizing pulmonary aspergillosis, or invasive aspergillosis (IA), depending on the host's immune status. Neutrophil deficiency is the predominant risk factor for the development of IA, the most life-threatening condition associated withA. fumigatusexposure. Here we demonstrate that in addition to neutrophils, eosinophils are an important contributor to the clearance ofA. fumigatusfrom the lung. AcuteA. fumigatuschallenge in normal mice induced the recruitment of CD11b+Siglec F+Ly-6GloLy-6CnegCCR3+eosinophils to the lungs, which was accompanied by an increase in lungEpx(eosinophil peroxidase) mRNA levels. Mice deficient in the transcription factor dblGATA1, which exhibit a selective deficiency in eosinophils, demonstrated impairedA. fumigatusclearance and evidence of germinating organisms in the lung. Higher burden correlated with lower mRNA expression ofEpx(eosinophil peroxidase) andPrg2(major basic protein) as well as lower interleukin 1β (IL-1β), IL-6, IL-17A, granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage colony-stimulating factor (GM-CSF), and CXCL1 levels. However, examination of lung inflammatory cell populations failed to demonstrate defects in monocyte/macrophage, dendritic cell, or neutrophil recruitment in dblGATA1-deficient mice, suggesting that the absence of eosinophils in dlbGATA1-deficient mice was the sole cause of impaired lung clearance. We show that eosinophils generated from bone marrow have potent killing activity againstA. fumigtausin vitro, which does not require cell contact and can be recapitulated by eosinophil whole-cell lysates. Collectively, our data support a role for eosinophils in the lung response afterA. fumigatusexposure.

Regulation of macrophage colony-stimulating factor in liver fat-storing cells by peptide growth factors

1992 ◽  
Vol 262 (4) ◽  
pp. C876-C881 ◽  
Author(s):  
M. Pinzani ◽  
H. E. Abboud ◽  
L. Gesualdo ◽  
S. L. Abboud
Keyword(s):  
Growth Factor ◽  
Constitutive Expression ◽  
Liver Fat ◽  
Northern Analysis ◽  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Term Survival ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

Macrophage colony-stimulating factor (M-CSF) selectively promotes mononuclear phagocyte survival, proliferation, and differentiation. The production of this factor within the liver may be necessary to support the relatively long-term survival of circulating monocytes as they migrate into tissues and differentiate into macrophages. We studied the constitutive expression and the effects of platelet-derived growth factor (PDGF), basic fibroblast growth factor (bFGF), and epidermal growth factor (EGF) on M-CSF mRNA levels and secretion of M-CSF in murine liver fat-storing cells (FSC), vascular pericytes likely involved in the development of liver fibrosis. By Northern analysis, using a murine M-CSF cDNA, FSC constitutively express two major transcripts of 4.4 and 2.2 kb, similar to those detected in mouse L cells, used as a control. Exposure to 10 ng/ml PDGF or bFGF increased M-CSF mRNA levels. Peak effects were observed at 3 and 6 h for PDGF and bFGF, respectively, returning to baseline levels by 12 h. Under basal conditions, detectable amounts of M-CSF, measured by radioimmunoassay, were found in cell supernatants conditioned for 8 and 24 h. PDGF and bFGF markedly stimulated the release of M-CSF as early as 8 h, an effect persisting for at least 24 h. These findings suggest that liver FSC release M-CSF upon stimulation by PDGF and bFGF and may contribute to the activation of resident or infiltrating cells in inflammatory liver diseases.

Inhibitor of nuclear factor-κB induction by cAMP antagonizes interleukin-1-induced human macrophage-colony-stimulating-factor expression

2001 ◽  
Vol 356 (2) ◽  
pp. 525-530 ◽  
Author(s):  
Pisate J. KAMTHONG ◽  
Ming-chi WU
Keyword(s):  
Nuclear Factor Κb ◽  
Human Macrophage ◽  
Mrna Levels ◽  
Nuclear Factor ◽  
Colony Stimulating Factor ◽  
Dibutyryl Camp ◽  
Iκb Kinase ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

We have recently reported that interleukin-1α (IL-1α) can induce human macrophage colony-stimulating factor (M-CSF) expression through nuclear factor κB (NF-κB) activation, and treatment of human pancreatic MIA PaCa-2 cancer cells with forskolin or cAMP attenuated the NF-κB activation as well as M-CSF expression. In this study, we have further investigated the mechanism of cAMP attenuation. MIA PaCa-2 cells were incubated with forskolin or dibutyryl-cAMP and then stimulated with IL-1 for 1h. Cell lysates were immunoprecipitated by anti-inhibitory κB (IκB) kinase-β (IKKβ) antibody and the immune complex assayed for kinase activity using recombinant inhibitor of NF-κB (IκBα) as substrate. The levels of IKKβ in the respective cellular proteins were measured by subsequent Western blot. The results show that the level of IKK protein remains constant in the presence of cAMP, forskolin and/or IL-1, whereas IKK activity was robustly stimulated by IL-1. Nonetheless, dibutyryl-cAMP or forskolin did not affect the IKK activation induced by IL-1. This experiment suggests that elevated cAMP has no effect on IKK activity. IκBα protein level decreased markedly in IL-1-treated cells compared with the untreated. By contrast, cells treated with cAMP or forskolin possessed discernibly higher IκBα levels. In addition, we observed that forskolin potentiated and prolonged the IL-1-induced IκBα mRNA levels, whereas it did not stabilize the IκBα mRNA message. Wholly, these studies indicate that elevated cAMP antagonizes IL-1-induced M-CSF transcription by up-regulating IκBα gene induction and its consequent attenuation of NF-κB activation.

scholarly journals Macrophage colony-stimulating factor and granulocyte-macrophage colony- stimulating factor stimulate the synthesis of plasminogen-activator inhibitors by human monocytes

Blood ◽  
1993 ◽  
Vol 82 (12) ◽  
pp. 3616-3621 ◽  
Author(s):  
JA Hamilton ◽  
GA Whitty ◽  
H Stanton ◽  
J Wojta ◽  
M Gallichio ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Human Monocyte ◽  
Mrna Levels ◽  
Human Monocytes ◽  
Colony Stimulating Factor ◽  
Gm Csf ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor ◽  
Pai 1

Macrophage colony-stimulating factor (M-CSF or CSF-1) and granulocyte- macrophage CSF (GM-CSF) have been shown to increase human monocyte urokinase-type plasminogen-activator (u-PA) activity with possible consequences for cell migration and tissue remodeling; because monocyte u-PA activity is likely to be controlled in part also by the PA inhibitors (PAIs) made by the cell, the effect of M-CSF and GM-CSF on human monocyte PAI-2 and PAI-1 synthesis was investigated. To this end, elutriation-purified human monocytes were treated in vitro with purified recombinant human M-CSF and GM-CSF, and PAI-2 and PAI-1 antigen and mRNA levels measured by specific enzyme-linked immunosorbent assays and Northern blot, respectively. Each CSF could enhance the protein and mRNA levels of PAI-2 and PAI-1 at similar concentrations for each product. This similar regulation of monocyte PAI expression in response to the CSFs contrasted with that found for the effects of lipopolysaccharide, transforming growth factor-beta and a glucocorticoid. Therefore, PAIs may be modulating the effects of the CSFs on monocyte u-PA activity at sites of inflammation and tissue remodeling.

scholarly journals Macrophage colony-stimulating factor-induced bone marrow macrophages do not synthesize or release prostaglandin E2

Blood ◽  
1994 ◽  
Vol 83 (11) ◽  
pp. 3316-3323 ◽  
Author(s):  
Y Shibata ◽  
DR Bjorkman ◽  
M Schmidt ◽  
Y Oghiso ◽  
A Volkman
Keyword(s):  
Bone Marrow ◽  
Enzyme Activity ◽  
Prostaglandin E2 ◽  
Bone Marrow Cells ◽  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Murine Bone Marrow ◽  
Gm Csf ◽  
Stimulating Factor

Abstract Previously, we found that murine bone marrow-derived macrophages (MO) induced in vitro by MO-specific colony-stimulating factor (M-CSF) have little capacity to release prostaglandin E2 (PGE2) and other eicosanoids. This work focused on the functional and transcriptional expression of the key enzymes for the PGE2 synthesis in the MO. Nonadherent bone marrow cells were cultured with RPMI1640 plus 10% fetal bovine serum (FBS) further supplemented with either M-CSF or granulocyte-macrophage (GM)-CSF and interleukin-3 (IL-3). Cellular PGG/H synthase (cyclooxygenase) levels were quantified by cytometric analysis with antibodies specific for the two isozymes of PGG/H synthase (PGG/H synthases 1 and 2). The enzyme activity was monitored by adding exogenous arachidonic acid (AA) substrate to the bone marrow MO cultures and to the cell-free particulate fractions. The levels of PGE2 converted were quantitated by radioimmunoassay (RIA). mRNA levels of the enzymes were detected by Northern blot analysis hybridized with mouse PGG/H synthase cDNA probes, 2.7 kb (PGG/H synthase 1) and 4.2 kb (PGG/H synthase 2). In addition, cellular phospholipase A2 (PLA2) activities were detected with sn-2–14C-arachidonyl phosphatidylcholine as a substrate. Cells proliferating in the presence of GM-CSF and IL-3 for more than 4 days showed significant release of PGE2 (> 7 ng/10(6) cells) when stimulated by AA. These cells also expressed significant amounts of PGG/H synthase 1 protein, its mRNA (2.7 kb) and cellular PLA2. M-CSF-induced MO, in sharp contrast, expressed little PGG/H synthase protein, mRNA, cellular enzyme activity, or PGE2 release, despite comparable levels of cellular PLA2 activity. These data suggest that the capacity of differentiating marrow-derived MO to form PGE2 is growth factor-dependent.

Bcl-3 Expression and Nuclear Translocation Are Induced by Granulocyte-Macrophage Colony-Stimulating Factor and Erythropoietin in Proliferating Human Erythroid Precursors

Blood ◽  
1998 ◽  
Vol 92 (4) ◽  
pp. 1225-1234 ◽  
Author(s):  
Min-Ying Zhang ◽  
Edward W. Harhaj ◽  
Laurie Bell ◽  
Shao-Cong Sun ◽  
Barbara A. Miller
Keyword(s):  
Nuclear Translocation ◽  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Reporter Plasmid ◽  
Gm Csf ◽  
Erythroid Precursors ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor ◽  
Stimulation Of

Bcl-3 is a proto-oncogene involved in the chromosomal translocation t(14;19) found in some patients with chronic lymphocytic leukemia. It shares structural similarities with and is a member of the IκB family of proteins. In this report, involvement of Bcl-3in hematopoietic growth factor-stimulated erythroid proliferation and differentiation was examined. In TF-1 cells, an erythroleukemia cell line, granulocyte-macrophage colony-stimulating factor (GM-CSF) and erythropoietin (Epo) greatly enhanced Bcl-3 expression at both the protein and mRNA levels in association with stimulation of proliferation. Bcl-3 protein was also highly expressed in early burst-forming unit-erythroid (BFU-E)–derived erythroid precursors (day 7) and decreased during maturation (days 10 and 14), suggesting that Bcl-3 is involved in normal erythroid proliferation. In these hematopoietic cells, Bcl-3 was hyperphosphorylated. GM-CSF and Epo modulated the subcellular localization of Bcl-3. Upon stimulation of TF-1 cells with GM-CSF or Epo, the nuclear translocation ofBcl-3 was dramatically enhanced. Overexpression of Bcl-3 in TF-1 cells by transient transfection along with the NF-κB factors p50 or p52 resulted in significant induction of an human immunodeficiency virus–type 1 (HIV-1) κB-TATA-luceriferase reporter plasmid, demonstrating that Bcl-3 has a positive role in transactivation of κB-containing genes in erythroid cells. Stimulation with GM-CSF enhanced c-myb mRNA expression in these cells. Bcl-3 in nuclear extracts of TF-1 cells bound to a κB enhancer in the c-mybpromoter together with NF-κB2/p52 and this binding activity was enhanced by GM-CSF stimulation. Furthermore, cotransfection of Bcl-3 with p52 or p50 in TF-1 cells resulted in significant activation of ac-myb κB-TATA-luceriferase reporter plasmid. These findings suggest that Bcl-3 may participate in the transcriptional regulation of certain κB-containing genes involved in hematopoiesis, includingc-myb. © 1998 by The American Society of Hematology.

Production of Interleukin-10 by Granulocyte Colony-Stimulating Factor–Mobilized Blood Products: A Mechanism for Monocyte-Mediated Suppression of T-Cell Proliferation

Blood ◽  
1998 ◽  
Vol 92 (1) ◽  
pp. 215-222 ◽  
Author(s):  
Marco Mielcarek ◽  
Lynn Graf ◽  
Gretchen Johnson ◽  
Beverly Torok-Storb
Keyword(s):  
Cell Proliferation ◽  
T Cell ◽  
Neutralizing Antibodies ◽  
Proliferative Response ◽  
Relative Proportion ◽  
Interleukin 10 ◽  
Mrna Levels ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Stimulating Factor

Previous reports showed that granulocyte colony-stimulating factor (G-CSF)-mobilized peripheral blood mononuclear cells (G-PBMC) are hyporesponsive to alloantigen compared with control PBMC. In the current study, neutralizing antibodies to interleukin-10 (IL-10) increased the proliferative response of G-PBMC to alloantigen by 50.14% (± 12.79%; n = 8), whereas the proliferative response of control PBMC was not affected. The inhibition of OKT3-stimulated CD4 cell proliferation by G-PBMC–derived CD14+ cells could also be abrogated by the addition of IL-10 neutralizing antibodies. Further, IL-10 levels correlated with the number of CD14 cells in these cultures. Constitutive IL-10 mRNA levels detected by quantitative reverse transcriptase-polymerase chain reaction (RT-PCR) were 10-fold higher in G-PBMC compared with control PBMC. This translated into significantly higher IL-10 levels after 24-hour lipopolysaccharide (LPS) stimulation of G-PBMC compared with control PBMC (P = .036). IL-10 mRNA levels were also fivefold higher in isolated G-PBMC-derived CD14 cells compared with control CD14 cells. This corresponded to increased constitutive production of IL-10 by isolated G-PBMC–derived CD14 cells compared with control CD14 cells (357.2 ± 104.5 v 51.7 ± 30.5, P = .051). In conclusion, these data suggest that monocytes contained within G-PBMC, which, in comparison to marrow, are increased in absolute number and relative proportion to T cells, may suppress T-cell responsiveness by secretion of IL-10.

scholarly journals Granulocyte-macrophage colony-stimulating factor (CSF) and multilineage CSF recruit human monocytes to express granulocyte CSF

Blood ◽  
1989 ◽  
Vol 73 (1) ◽  
pp. 64-67 ◽  
Author(s):  
W Oster ◽  
A Lindemann ◽  
R Mertelsmann ◽  
F Herrmann
Keyword(s):  
Peripheral Blood Monocyte ◽  
Biologically Active ◽  
Mrna Levels ◽  
Colony Stimulating Factor ◽  
Gm Csf ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Culture Supernatants ◽  
Stimulating Factor ◽  
Insight Into

Abstract We assessed the capacity of recombinant human granulocyte-macrophage colony-stimulating factor (GM-CSF) and multilineage (Multi)-CSF to induce release of granulocyte-CSF (G-CSF) by highly purified peripheral blood monocyte (Mo) preparations. Our results reveal that GM-CSF and Multi-CSF, either alone or in a synergistic concert, activate Mo to transcribe G-CSF messenger (m) RNA and release biologically active G- CSF protein into their culture supernatants. G-CSF had no regulatory effect on Mo expression of cytoplasmic G-CSF mRNA levels and G-CSF protein secretion by itself. These differential actions of CSFs provide further insight into self-regulatory mechanisms within the growth factor hierarchy system.

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