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Journal articles on the topic 'Macrophage inhibitory cytokine - 1'

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Published: 4 June 2021

Last updated: 10 February 2022

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1

Huh, Sung Jin, Chin-Ying Chung, Arati Sharma, and Gavin P. Robertson. "Macrophage Inhibitory Cytokine-1 Regulates Melanoma Vascular Development." American Journal of Pathology 176, no. 6 (June 2010): 2948–57. http://dx.doi.org/10.2353/ajpath.2010.090963.

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2

Lu, Chunxia, P. Anil Kumar, Yong Fan, Mark A. Sperling, and Ram K. Menon. "A Novel Effect of Growth Hormone on Macrophage Modulates Macrophage-Dependent Adipocyte Differentiation." Endocrinology 151, no. 5 (February 25, 2010): 2189–99. http://dx.doi.org/10.1210/en.2009-1194.

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The GH receptor (GHR) is expressed on macrophages. However, the precise role of GH in regulation of macrophage function is unclear. We hypothesized that soluble factors including cytokines produced by macrophages in a GH-dependent manner regulate adipogenesis. We confirmed expression and functional integrity of the GHR in the J774A.1 macrophage cells. Conditioned medium (CM) from macrophages inhibited adipogenesis in a 3T3-L1 adipogenesis assay. CM from GH-treated macrophages decreased the inhibitory effect of CM from macrophages on adipogenesis. This effect on preadipocyte differentiation was active only during the first (early) phase of adipocyte differentiation. CM from stromal vascular compartment macrophages of mice with macrophage-specific deletion of the GHR exhibited more inhibitory effect on 3T3-L1 preadipocyte differentiation compared with CM from stromal vascular compartment macrophages of control mice, indicating that intact GH action in primary macrophages also increases preadipocyte differentiation. GH did not increase IGF-1 expression in macrophages. PCR array analysis identified IL-1β as a candidate cytokine whose expression was altered by GH in macrophages. Levels of IL-1β mRNA and protein were significantly decreased in GH-treated J774A.1 macrophages. Nuclear factor-κB stimulates IL-1β gene expression, and GH induced a significant decrease in the levels of phosphorylated nuclear factor-κB in macrophages. IL-1β is a known inhibitor of adipogenesis, and these results support GH-dependent down-regulation of macrophage IL-1β expression as one mechanism for the observed increase in adipogenesis with CM from GH-treated macrophages. We conclude that GH decreases secretion of IL-1β by the macrophage and thus in a paracrine manner increases adipocyte differentiation. These results provide a novel mechanism for GH’s actions in the control of adipogenesis.

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3

Singla, Reetu D., Jing Wang, and Dinender K. Singla. "Regulation of Notch 1 signaling in THP-1 cells enhances M2 macrophage differentiation." American Journal of Physiology-Heart and Circulatory Physiology 307, no. 11 (December 1, 2014): H1634—H1642. http://dx.doi.org/10.1152/ajpheart.00896.2013.

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Macrophage polarization is emerging as an important area of research for the development of novel therapeutics to treat inflammatory diseases. Within the current study, the role of Notch1R in macrophage differentiation was investigated as well as downstream effects in THP-1 monocytes cultured in “inflammation mimicry” media. Interference of Notch signaling was achieved using either the pharmaceutical inhibitor DAPT or Notch1R small interfering RNA (siRNA), and Notch1R expression, macrophage phenotypes, and anti- and proinflammatory cytokine expression were evaluated. Data presented show that Notch1R expression on M1 macrophages as well as M1 macrophage differentiation is significantly elevated during cellular stress ( P < 0.05). However, under identical culture conditions, interference to Notch signaling via Notch1R inhibition mitigated these results as well as promoted M2 macrophage differentiation. Moreover, when subjected to cellular stress, macrophage secretion of proinflammatory cytokines was significantly heightened ( P < 0.05). Importantly, Notch1R inhibition not only diminished proinflammatory cytokine secretion but also enhanced anti-inflammatory protein release ( P < 0.05). Our data suggest that Notch1R plays a pivotal role in M1 macrophage differentiation and heightened inflammatory responses. Therefore, we conclude that inhibition of Notch1R and subsequent downstream signaling enhances monocyte to M2 polarized macrophage outcomes and promotes anti-inflammatory mediation during cellular stress.

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4

Huang, Mingguo, Shintaro Narita, Takamitsu Inoue, Norihiko Tsuchiya, Shigeru Satoh, Hiroshi Nanjo, Takehiko Sasaki, and Tomonori Habuchi. "Diet-induced macrophage inhibitory cytokine 1 promotes prostate cancer progression." Endocrine-Related Cancer 21, no. 1 (February 2014): 39–50. http://dx.doi.org/10.1530/erc-13-0227.

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Recent studies have indicated that a high-fat diet (HFD) plays an important role in prostate cancer (PCa) progression. Palmitic acid (PA) is one of the most abundant saturated free fatty acids (FAs) and is associated with carcinogenesis. In this study, we investigated the mechanism underlying the association of dietary fat, including PA, with PCa progression. In four PCa cell lines,in vitroPA administration stimulated the expression of macrophage inhibitory cytokine 1 (MIC1), which is a divergent member of the transforming growth factor-β family.In vivo, LNCaP xenograft tumor growth, serum MIC1 levels, and FA levels in xenograft tumors were significantly higher in mice receiving an HFD containing high amounts of PA than in those receiving a low-fat diet (LFD). In addition, tumor cells with high MIC1 expression invaded to venules and lymph vessels in the LNCaP xenograft.In vitrostudies showed that proliferation and invasive capacity were significantly higher in PCa cells cultured with serum from HFD-fed mice than in those cultured with the serum from LFD-fed mice. This effect was attenuated by the addition of neutralizing antibodies against MIC1, but not by isotype control antibodies. Clinically, serum MIC1 levels were significantly higher in PCa patients than in healthy controls, and higher levels were associated with higher pathological grade and obesity. In conclusion, our results indicate that an HFD containing PA may promote growth and invasiveness of PCa cells through the upregulation of MIC1 expression.

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5

Yamashita, Toshiharu, Akihiro Yoneta, and Tokimasa Hida. "Macrophage Inhibitory Cytokine-1: A New Player in Melanoma Development." Journal of Investigative Dermatology 129, no. 2 (February 2009): 262–64. http://dx.doi.org/10.1038/jid.2008.366.

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6

Borsini, Alessandra, Maria Grazia Di Benedetto, Juliette Giacobbe, and Carmine M. Pariante. "Pro- and Anti-Inflammatory Properties of Interleukin in Vitro: Relevance for Major Depression and Human Hippocampal Neurogenesis." International Journal of Neuropsychopharmacology 23, no. 11 (July 29, 2020): 738–50. http://dx.doi.org/10.1093/ijnp/pyaa055.

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Abstract Background Although the pro-inflammatory cytokine interleukin (IL)6 has been generally regarded as “depressogenic,” recent research has started to question this assumption in light of the fact that this cytokine can also have anti-inflammatory properties. This bimodal action seems to be dependent on its concentration levels and on the concomitant presence of other pro-inflammatory cytokines. Methods We exposed a human hippocampal progenitor cell line, HPC0A07/03C, to cytokine levels described in depressed patients (IL6 5 pg/mL with IL1β 10 pg/mL or Macrophage Migration Inhibitory Factor (300 pg/mL) in healthy individuals (IL6 with IL1β, 1 pg/mL or Macrophage Migration Inhibitory Factor 10 pg/mL), as well as to the potentially anti-inflammatory, much higher concentrations of IL6 (50 000 pg/mL). Results Treatment with high concentrations of IL6 with IL1β or Macrophage Migration Inhibitory Factor (resembling depressed patients) decreases neurogenesis compared with low concentrations of the same cytokines (healthy individuals) and that this is mediated via production of, respectively, IL8 and IL1β in cell supernatant. Instead, treatment with very high, anti-inflammatory concentration of IL6 (50 000 pg/mL) together with high IL1β or Macrophage Migration Inhibitory Factor prevents decrease in neurogenesis and reduces both IL8 and IL1β. When high concentrations of both IL1β and Macrophage Migration Inhibitory Factor were used in co-treatment, as a model of treatment-resistant depression, we also demonstrated a reduction in neurogenesis and that this is mediated via a decrease in IL4; moreover, co-treatment with high IL1β and Macrophage Migration Inhibitory Factor and the very high concentration of IL6 prevented the reduction in neurogenesis and increased IL4. Conclusions Our results demonstrate that IL6 can exert both pro- and anti-inflammatory (potentially antidepressant) properties, depending on its concentrations and combinations with other inflammatory cytokines.

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7

Andreone, Teresa, Gordon P. Meares, Katherine J. Hughes, Polly A. Hansen, and John A. Corbett. "Cytokine-mediated β-cell damage in PARP-1-deficient islets." American Journal of Physiology-Endocrinology and Metabolism 303, no. 2 (July 15, 2012): E172—E179. http://dx.doi.org/10.1152/ajpendo.00055.2012.

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Poly(ADP)-ribose polymerase (PARP) is an abundant nuclear protein that is activated by DNA damage; once active, it modifies nuclear proteins through attachment of poly(ADP)-ribose units derived from β-nicotinamide adenine dinucleotide (NAD+). In mice, the deletion of PARP-1 attenuates tissue injury in a number of animal models of human disease, including streptozotocin-induced diabetes. Also, inflammatory cell signaling and inflammatory gene expression are attenuated in macrophages isolated from endotoxin-treated PARP-1-deficient mice. In this study, the effects of PARP-1 deletion on cytokine-mediated β-cell damage and macrophage activation were evaluated. There are no defects in inflammatory mediator signaling or inflammatory gene expression in macrophages and islets isolated from PARP-1-deficient mice. While PARP-1 deficiency protects islets against cytokine-induced islet cell death as measured by biochemical assays of membrane polarization, the genetic absence of PARP-1 does not effect cytokine-induced inhibition of insulin secretion or cytokine-induced DNA damage in islets. While PARP-1 deficiency appears to provide protection from cell death, it fails to provide protection against the inhibitory actions of cytokines on insulin secretion or the damaging actions on islet DNA integrity.

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8

Calandra, T., J. Bernhagen, R. A. Mitchell, and R. Bucala. "The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor." Journal of Experimental Medicine 179, no. 6 (June 1, 1994): 1895–902. http://dx.doi.org/10.1084/jem.179.6.1895.

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For over 25 years, the cytokine known as macrophage migration inhibitory factor (MIF) has been considered to be a product of activated T lymphocytes. We recently identified the murine homolog of human MIF as a protein secreted by the pituitary in response to endotoxin administration. In the course of these studies, we also detected MIF in acute sera obtained from endotoxin-treated, T cell-deficient (nude), and hypophysectomized mice, suggesting that still more cell types produce MIF. Here, we report that cells of the monocyte/macrophage lineage are an important source of MIF in vitro and in vivo. We observed high levels of both preformed MIF protein and MIF mRNA in resting, nonstimulated cells. In the murine macrophage cell line RAW 264.7, MIF secretion was induced by as little as 10 pg/ml of lipopolysaccharide (LPS), peaked at 1 ng/ml, and was undetectable at LPS concentrations > 1 microgram/ml. A similar stimulation profile was observed in LPS-treated peritoneal macrophages; however, higher LPS concentrations were necessary to induce peak MIF production unless cells had been preincubated with interferon gamma (IFN-gamma). In RAW 264.7 macrophages, MIF secretion also was induced by tumor necrosis factor alpha (TNF-alpha) and IFN-gamma, but not by interleukins 1 beta or 6. Of note, MIF-stimulated macrophages were observed to secrete bioactive TNF-alpha. Although previously overlooked, the macrophage is both an important source and an important target of MIF in vivo. The activation of both central (pituitary) and peripheral (macrophage) sources of MIF production by inflammatory stimuli provides further evidence for the critical role of this cytokine in the systemic response to tissue invasion.

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9

Hayes, V. M. "Macrophage Inhibitory Cytokine-1 H6D Polymorphism, Prostate Cancer Risk, and Survival." Cancer Epidemiology Biomarkers & Prevention 15, no. 6 (June 1, 2006): 1223–25. http://dx.doi.org/10.1158/1055-9965.epi-06-0063.

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10

Brown, D. A., F. Lindmark, P. Stattin, K. Balter, H. O. Adami, S. L. Zheng, J. Xu, et al. "Macrophage Inhibitory Cytokine 1: A New Prognostic Marker in Prostate Cancer." Clinical Cancer Research 15, no. 21 (October 20, 2009): 6658–64. http://dx.doi.org/10.1158/1078-0432.ccr-08-3126.

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11

Baek, Kyoung Eun, Suk Ran Yoon, Jong-Tae Kim, Kwang Soo Kim, Seong Ho Kang, Young Yang, Jong-Seok Lim, et al. "Upregulation and secretion of macrophage inhibitory cytokine-1 (MIC-1) in gastric cancers." Clinica Chimica Acta 401, no. 1-2 (March 2009): 128–33. http://dx.doi.org/10.1016/j.cca.2008.12.008.

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12

Baer, Mark, Allan Dillner, Richard C. Schwartz, Constance Sedon, Sergei Nedospasov, and Peter F. Johnson. "Tumor Necrosis Factor Alpha Transcription in Macrophages Is Attenuated by an Autocrine Factor That Preferentially Induces NF-κB p50." Molecular and Cellular Biology 18, no. 10 (October 1, 1998): 5678–89. http://dx.doi.org/10.1128/mcb.18.10.5678.

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ABSTRACT Macrophages are a major source of proinflammatory cytokines such as tumor necrosis factor alpha (TNF-α), which are expressed during conditions of inflammation, infection, or injury. We identified an activity secreted by a macrophage tumor cell line that negatively regulates bacterial lipopolysaccharide (LPS)-induced expression of TNF-α. This activity, termed TNF-α-inhibiting factor (TIF), suppressed the induction of TNF-α expression in macrophages, whereas induction of three other proinflammatory cytokines (interleukin-1β [IL-1β], IL-6, and monocyte chemoattractant protein 1) was accelerated or enhanced. A similar or identical inhibitory activity was secreted by IC-21 macrophages following LPS stimulation. Inhibition of TNF-α expression by macrophage conditioned medium was associated with selective induction of the NF-κB p50 subunit. Hyperinduction of p50 occurred with delayed kinetics in LPS-stimulated macrophages but not in fibroblasts. Overexpression of p50 blocked LPS-induced transcription from a TNF-α promoter reporter construct, showing that this transcription factor is an inhibitor of the TNF-α gene. Repression of the TNF-α promoter by TIF required a distal region that includes three NF-κB binding sites with preferential affinity for p50 homodimers. Thus, the selective repression of the TNF-α promoter by TIF may be explained by the specific binding of inhibitory p50 homodimers. We propose that TIF serves as a negative autocrine signal to attenuate TNF-α expression in activated macrophages. TIF is distinct from the known TNF-α-inhibiting factors IL-4, IL-10, and transforming growth factor β and may represent a novel cytokine.

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13

Khaled, Yazan S., Eyad Elkord, and Basil J. Ammori. "Macrophage Inhibitory Cytokine-1: A review of its pleiotropic actions in cancer." Cancer Biomarkers 11, no. 5 (November 29, 2012): 183–90. http://dx.doi.org/10.3233/cbm-2012-00287.

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14

Lindmark, F., S. L. Zheng, F. Wiklund, J. Bensen, K. A. Balter, B. Chang, M. Hedelin, et al. "H6D Polymorphism in Macrophage-Inhibitory Cytokine-1 Gene Associated With Prostate Cancer." JNCI Journal of the National Cancer Institute 96, no. 16 (August 17, 2004): 1248–54. http://dx.doi.org/10.1093/jnci/djh227.

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15

Crabtree, Traves D., Long Jin, Daniel P. Raymond, Shawn J. Pelletier, C. Webster Houlgrave, Thomas G. Gleason, Timothy L. Pruett, and Robert G. Sawyer. "Preexposure of Murine Macrophages to CpG Oligonucleotide Results in a Biphasic Tumor Necrosis Factor Alpha Response to Subsequent Lipopolysaccharide Challenge." Infection and Immunity 69, no. 4 (April 1, 2001): 2123–29. http://dx.doi.org/10.1128/iai.69.4.2123-2129.2001.

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ABSTRACT Bacterial DNA and synthetic oligonucleotides containing CpG sequences (CpG-DNA and CpG-ODN) provoke a proinflammatory cytokine response (tumor necrosis factor alpha [TNF-α], interleukin-12 [IL-12], and IL-6) and increased mortality in lipopolysaccharide (LPS)-challenged mice via a TNF-α-mediated mechanism. It was hypothesized that preexposure of macrophages to CpG-ODN would result in an increased TNF-α response to subsequent LPS challenge in vitro. Using the murine macrophage cell line RAW 264.7, we demonstrated both a rapid proinflammatory cytokine response (TNF-α) and a delayed inhibitory cytokine response (IL-10) with CpG-ODN. Preexposure of macrophages to CpG-ODN for brief periods (1 to 3 h) augmented TNF-α secretion and mRNA accumulation following subsequent LPS challenge (1 μg/ml). However, prolonged preexposure to CpG-ODN (6 to 9 h) resulted in suppression of the TNF-α protein and mRNA response to LPS. The addition of anti-IL-10 antibody to CpG-ODN during preexposure resulted in an increase in the LPS-induced TNF-α response over that induced by CpG-ODN preexposure alone. Thus, while brief preexposure of macrophages to CpG-ODN augments the proinflammatory cytokine response to subsequent LPS challenge, prolonged preexposure elicits IL-10 production, which inhibits the TNF-α response. Although the initial proinflammatory effects of CpG-DNA are well established, the immune response to CpG-DNA may also include autocrine or paracrine feedback mechanisms, leading to a complex interaction of proinflammatory and inhibitory cytokines.

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Tong, Stephen, Budi Marjono, David A. Brown, Sheila Mulvey, Samuel N. Breit, Ursula Manuelpillai, and Euan M. Wallace. "Serum concentrations of macrophage inhibitory cytokine 1 (MIC 1) as a predictor of miscarriage." Lancet 363, no. 9403 (January 2004): 129–30. http://dx.doi.org/10.1016/s0140-6736(03)15265-8.

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Bauskin, Asne R., David A. Brown, Tamara Kuffner, Heiko Johnen, X. Wei Luo, Mark Hunter, and Samuel N. Breit. "Role of Macrophage Inhibitory Cytokine-1 in Tumorigenesis and Diagnosis of Cancer: Figure 1." Cancer Research 66, no. 10 (May 15, 2006): 4983–86. http://dx.doi.org/10.1158/0008-5472.can-05-4067.

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Breit, S. N., J. J. Carrero, V. W. W. Tsai, N. Yagoutifam, W. Luo, T. Kuffner, A. R. Bauskin, et al. "Macrophage inhibitory cytokine-1 (MIC-1/GDF15) and mortality in end-stage renal disease." Nephrology Dialysis Transplantation 27, no. 1 (September 22, 2011): 70–75. http://dx.doi.org/10.1093/ndt/gfr575.

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19

Wiklund, Fredrik E., Anna M. Bennet, Patrik K. E. Magnusson, Ulrika K. Eriksson, Fredrik Lindmark, Liyun Wu, Nasreen Yaghoutyfam, et al. "Macrophage inhibitory cytokine-1 (MIC-1/GDF15): a new marker of all-cause mortality." Aging Cell 9, no. 6 (October 21, 2010): 1057–64. http://dx.doi.org/10.1111/j.1474-9726.2010.00629.x.

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Karan, Dev, Jeffrey Holzbeierlein, and J. Brantley Thrasher. "Macrophage Inhibitory Cytokine-1: Possible Bridge Molecule of Inflammation and Prostate Cancer: Figure 1." Cancer Research 69, no. 1 (December 31, 2008): 2–5. http://dx.doi.org/10.1158/0008-5472.can-08-1230.

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21

Stejskal, David, Michal Karpíšek, Viera Humeňanská, Bořek Lačňák, and Marek Švesták. "Macrophage-inhibitory cytokine-1 (mic-1) in differential diagnosis of dyspnea—A pilot study." Clinical Biochemistry 42, no. 13-14 (September 2009): 1347–51. http://dx.doi.org/10.1016/j.clinbiochem.2009.03.022.

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22

Hoshino, Yoshihiko, Koh Nakata, Satomi Hoshino, Yoshihiro Honda, Doris B. Tse, Tatsuo Shioda, William N. Rom, and Michael Weiden. "Maximal HIV-1 Replication in Alveolar Macrophages during Tuberculosis Requires both Lymphocyte Contact and Cytokines." Journal of Experimental Medicine 195, no. 4 (February 18, 2002): 495–505. http://dx.doi.org/10.1084/jem.20011614.

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HIV-1 replication is markedly upregulated in alveolar macrophages (AM) during pulmonary tuberculosis (TB). This is associated with loss of an inhibitory CCAAT enhancer binding protein β (C/EBPβ) transcription factor and activation of nuclear factor (NF)-κB. Since the cellular immune response in pulmonary TB requires lymphocyte–macrophage interaction, a model system was developed in which lymphocytes were added to AM. Contact between lymphocytes and AM reduced inhibitory C/EBPβ, activated NF-κB, and enhanced HIV-1 replication. If contact between lymphocytes and macrophages was prevented, inhibitory C/EBPβ expression was maintained and the HIV-1 long terminal repeat (LTR) was not maximally stimulated although NF-κB was activated. Antibodies that cross-linked macrophage expressed B-7, and vascular cell adhesion molecule and CD40 were used to mimic lymphocyte contact. All three cross-linking antibodies were required to abolish inhibitory C/EBPβ expression. However, the HIV-1 LTR was not maximally stimulated and NF-κB was not activated. Maximal HIV-1–LTR stimulation required both lymphocyte-derived soluble factors, and cross-linking of macrophage expressed costimulatory molecules. High level HIV-1–LTR stimulation was also achieved when IL-1β, IL-6, and TNF-β were added to macrophages with cross-linked costimulatory molecules. Contact between activated lymphocytes and macrophages is necessary to down-regulate inhibitory C/EBPβ, thereby derepressing the HIV-1 LTR. Lymphocyte-derived cytokines activate NF-κB, further enhancing the HIV-1 LTR.

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Lemay, Serge, Tatiana V. Lebedeva, and Ajay K. Singh. "Inhibition of Cytokine Gene Expression by Sodium Salicylate in a Macrophage Cell Line through an NF-κB-Independent Mechanism." Clinical Diagnostic Laboratory Immunology 6, no. 4 (July 1, 1999): 567–72. http://dx.doi.org/10.1128/cdli.6.4.567-572.1999.

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ABSTRACT Macrophage-derived cytokines and chemokines are involved at multiple steps of immune and inflammatory responses, and the transcriptional factor NF-κB appears to play a pivotal role in their coordinated upregulation. The anti-inflammatory agents salicylates have been proposed to act in part by inhibiting NF-κB. We have therefore studied the effects of sodium salicylate on lipopolysaccharide (LPS)-induced κB-binding activity and on cytokine and chemokine gene expression in the RAW264.7 murine macrophage cell line and compared them to those of an established NF-κB inhibitor, pyrrolidine dithiocarbamate (PDTC). PDTC (100 μM) completely abrogated LPS-induced κB-binding activity and also profoundly inhibited the induction of interleukin 1α (IL-1α), IL-1β, IL-6, IL-10, granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, and MCP-1 and, to a lesser extent, leukemia inhibitory factor, RANTES, and IL-1Ra. In contrast, sodium salicylate (15 to 20 mM) had no effect on NF-κB activation but, nevertheless, suppressed several LPS-induced cytokine and chemokine genes to a degree similar to that obtained with PDTC. However, compared to PDTC, sodium salicylate caused significantly less inhibition of IL-1Ra and IL-10 gene expression after LPS stimulation. Neither LPS-induced MIP-1α, MIP-1β, nor MIP-2 was significantly affected by PDTC or sodium salicylate, demonstrating that NF-κB is dispensable for the transcriptional regulation of these genes by LPS. In summary, these results suggest that both NF-κB-dependent and NF-κB-independent pathways are necessary for the induction by LPS of a complex cytokine and chemokine response. In the RAW264.7 macrophage cell line, suprapharmacological concentrations of sodium salicylate exert a potent inhibitory effect on LPS-induced cytokine gene induction but appear to accomplish this by interfering with NF-κB-independent pathways of activation.

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Moore, A. G., D. A. Brown, W. D. Fairlie, A. R. Bauskin, P. K. Brown, M. L. C. Munier, P. K. Russell, L. A. Salamonsen, E. M. Wallace, and S. N. Breit. "The Transforming Growth Factor-β Superfamily Cytokine Macrophage Inhibitory Cytokine-1 Is Present in High Concentrations in the Serum of Pregnant Women1." Journal of Clinical Endocrinology & Metabolism 85, no. 12 (December 1, 2000): 4781–88. http://dx.doi.org/10.1210/jcem.85.12.7007.

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Macrophage inhibitory cytokine-1 (MIC-1) is a recently described divergent member of the transforming growth factor-β superfamily. MIC-1 transcription up-regulation is associated with macrophage activation, and this observation led to its cloning. Northern blots indicate that MIC-1 is also present in human placenta. A sensitive sandwich enzyme-linked immunosorbent assay for the quantification of MIC-1 was developed and used to examine the role of this cytokine in pregnancy. High levels of MIC-1 are present in the sera of pregnant women. The level rises substantially with progress of gestation. MIC-1 can also be detected, in large amounts, in amniotic fluid and placental extracts. In addition, the BeWo placental trophoblastic cell line was found to constitutively express the MIC-1 transcript and secrete large amounts of MIC-1. These findings suggest that the placental trophoblast is a major source of the MIC-1 present in maternal serum and amniotic fluid. We suggest that MIC-1 may promote fetal survival by suppressing the production of maternally derived proinflammatory cytokines within the uterus.

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Marjono, B., U. Manuelpillai, E. Dimitriadis, L. Salamonsen, S. Breit, and E. Wallace. "270.Macrophage inhibitory cytokine-1 at the maternal - fetal interface in early pregnancy." Reproduction, Fertility and Development 16, no. 9 (2004): 270. http://dx.doi.org/10.1071/srb04abs270.

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Macrophage inhibitory cytokine-1 (MIC-1) is a transforming growth factor-β (TGF-β) superfamily member, first isolated from activated macrophages and subsequently localised in the human placenta. We previously reported that decreased circulating levels in very early pregnancy are associated with subsequent miscarriage. We undertook these current in vitro studies to investigate possible roles for MIC-1 in early pregnancy: (1) regulation of placental matrix metalloproteinase-2 and -9 (MMP-2 and -9); (2) effect on placental apoptosis; and (3) regulation of endometrial stromal cell decidualisation. (1) First trimester placental explant cultures were treated with 100–200 ng/mL MIC-1 � 1/1000 (v/v) anti-MIC-1 antibody. MMP-2 and -9 were measured by gelatin zymography. MMP activation via the plasminogen activation pathway was examined by measuring mRNA expression for urokinase plasminogen activator and its receptor (uPA, uPAR) and type-1 plasminogen activation inhibitor (PAI-1). (2) In first trimester trophoblast explants, apoptosis was induced in vitro with tumor necrosis factor-α (TNF-α) and interferon-β (IFN-β) � 200 ng/mL MIC-1. The pro-apoptosis factor caspase-3 was localised by immunohistochemistry. (3) Using an established model of oestrogen and progesterone induced endometrial stromal cell decidualisation, MIC-1 production was measured and correlated with morphological changes. Cultures were also treated with 20 ng/mL MIC-1. MIC-1 treatment inhibited activation of both MMP-2 and MMP-9 while treatment with anti-MIC-1 antibody blocked the inhibition. uPA, uPAR and PAI-1 mRNA did not change with either treatment. MIC-1 treatment mitigated TNF-α/IFN-β induced trophoblast apoptosis. MIC-1 production increased during induced decidualisation and MIC-1 treatment facilitates further decidualisation in this model. MIC-1 appears to have a number of potentially important functions in the human placenta and decidua consistent with physiological roles in normal placentation. Whether these functions are key to successful pregnancy remains to be studied.

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Müller, Ruth, Jörg Klug, Miriam Rodewald, and Andreas Meinhardt. "Macrophage migration inhibitory factor suppresses transforming growth factor-β2 secretion in cultured rat testicular peritubular cells." Reproduction, Fertility and Development 17, no. 4 (2005): 435. http://dx.doi.org/10.1071/rd04061.

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Cytokines have direct effects on testicular cell functions and a number of cytokines are produced constitutively within the testis, even in the absence of immune-activation events. There is clear evidence that cytokines play a dual role as important regulatory factors in the normal function of the testis, as well as in testicular inflammation. The pro-inflammatory cytokine macrophage migration inhibitory factor (MIF) is expressed locally in the testis and has direct effects on peritubular cells, which, in turn, produce anti-inflammatory mediators, including transforming growth factor (TGF)-β2. In the present study, we investigated the function of MIF by examining its effect on the secretion of TGF-β2 in peritubular cells. Expression of TGF-β2 mRNA was shown by reverse transcription–polymerase chain reaction in peritubular cells isolated from 19-day-old rat testis. The addition of recombinant MIF to cultured peritubular cells resulted in a dose-dependent decrease in TGF-β2 secretion up to 52% of control levels after 48 h, which was significant for all doses investigated (10–100 ng mL−1 MIF). Inhibition of TGF-β2 secretion was sustained for 72 h for the highest dose of MIF used (100 ng mL−1). No effect of MIF was observed on TGF-β2 mRNA expression levels, as shown by real-time polymerase chain reaction. These results suggest that the pro-inflammatory cytokine MIF can shift the cytokine balance from the immunosuppressive state towards an inflammatory reaction, potentially through the inhibition of TGF-β2 secretion by peritubular cells.

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Mehta, Raaj S., Navya Bezawada, Mingyang Song, Kana Wu, Xabier Garcia-de-Albeniz, Charles Fuchs, Shuji Ogino, Edward Giovannucci, and Andrew T. Chan. "648 Circulating Macrophage Inhibitory Cytokine-1 (MIC-1) Is Associated With Risk of Colorectal Cancer." Gastroenterology 144, no. 5 (May 2013): S—115. http://dx.doi.org/10.1016/s0016-5085(13)60415-1.

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Nakamura, T., A. Scorilas, C. Stephan, G. M. Yousef, G. Kristiansen, K. Jung, and E. P. Diamandis. "Quantitative analysis of macrophage inhibitory cytokine-1 (MIC-1) gene expression in human prostatic tissues." British Journal of Cancer 88, no. 7 (April 2003): 1101–4. http://dx.doi.org/10.1038/sj.bjc.6600869.

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Unsicker, Klaus, Björn Spittau, and Kerstin Krieglstein. "The multiple facets of the TGF-β family cytokine growth/differentiation factor-15/macrophage inhibitory cytokine-1." Cytokine & Growth Factor Reviews 24, no. 4 (August 2013): 373–84. http://dx.doi.org/10.1016/j.cytogfr.2013.05.003.

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Chong, Mark M. W., Donald Metcalf, Emma Jamieson, Warren S. Alexander, and Thomas W. H. Kay. "Suppressor of cytokine signaling-1 in T cells and macrophages is critical for preventing lethal inflammation." Blood 106, no. 5 (September 1, 2005): 1668–75. http://dx.doi.org/10.1182/blood-2004-08-3049.

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Abstract The balance between pro- and anti-inflammatory cytokines modulates inflammation. Intracellular inhibitors of signaling, in turn, contribute to the negative regulation of cytokines. One of these inhibitors is suppressor of cytokine signaling-1 (SOCS-1). Socs1-/- mice die by 3 weeks of age with inflammation and fatty necrosis of the liver. Here, cre/loxP deletion of Socs1 was used to investigate the contribution of specific cells/tissues to inflammatory disease. Mice with SOCS-1 deficiency in myeloid and lymphoid cells, but not lymphoid alone, became ill at 50 to 250 days of age. These mice developed splenomegaly and T-cell/macrophage infiltration of many organs, including liver, lung, pancreas, and muscle. There were also abnormally high levels of the proinflammatory cytokines interferon γ (IFN-γ), tumor necrosis factor (TNF), and interleukin-12 (IL-12), and activated T cells circulating in these mice. Socs1null T cells were found to be hypersensitive to multiple cytokines, including IL-1, IL-2, and IL-12, resulting in IFN-γ production without requiring T-cell receptor (TCR) ligation. Additionally, Socs1null macrophages produced excessive amounts of IL-12 and TNF in response to other cytokines, including IFN-γ. A dysregulated cytokine network between T cells and macrophages is thus associated with this inflammatory disease. These findings indicate that SOCS-1 is critical in both T cells and macrophages for preventing uncontrolled inflammation. (Blood. 2005;106:1668-1675)

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Yadon, A., D. Ruelas, G. Min-Oo, J. Taylor, and M. R. Warr. "AB0108 IRAK4 INHIBITION SUPPRESSES PROINFLAMMATORY CYTOKINE PRODUCTION FROM HUMAN MACROPHAGES STIMULATED WITH SYNOVIAL FLUID FROM RHEUMATOID ARTHRITIS PATIENTS." Annals of the Rheumatic Diseases 79, Suppl 1 (June 2020): 1353.2–1353. http://dx.doi.org/10.1136/annrheumdis-2020-eular.3793.

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Background:Rheumatoid arthritis (RA) is characterized by chronic, uncontrolled joint inflammation and tissue destruction. Macrophages are thought to be key mediators in both the initiation and perpetuation of this pathology.1,2The RA synovium contains a complex inflammatory milieu that can stimulate macrophage-dependent production of proinflammatory cytokines through multiple signaling pathways.1,2Existing evidence indicates that toll-like receptors (TLRs) and interleukin-1 receptors (IL-1R) along with their agonists, damage-associated molecular patterns (DAMPs) and IL-1β, are highly expressed in RA joints and are important mediators of synovial macrophage activation and proinflammatory cytokine production.1-9IRAK4 (interleukin-1 receptor-associated kinase 4) is a serine/threonine kinase that facilitates TLR and IL-1R signaling in many cell types, including macrophages.10IRAK4 inhibition represents an opportunity to reduce proinflammatory cytokine production in the joints of patients with RA.Objectives:To investigate the effect of a highly selective IRAK4 inhibitor on proinflammatory cytokine production from human macrophages stimulated with synovial fluid from patients with RA.Methods:Primary human monocytes from 2 independent donors were differentiated for 6 days with granulocyte-macrophage colony-stimulating factor (GM-CSF) to generate human monocyte-derived macrophages (hMDMs). hMDMs were then pretreated with an IRAK4 inhibitor for 1 hour and subsequently stimulated for 24 hours with RA synovial fluid from 5 patients. Culture supernatants were then assessed for secretion of proinflammatory cytokines by MesoScale Discovery.Results:RA synovial fluid stimulation of hMDMs resulted in the production of several proinflammatory cytokines, including IL-6, IL-8, and TNFα. Pretreatment of hMDMs with an IRAK4 inhibitor resulted in the dose-dependent inhibition of IL-6, IL-8, and TNFα production, with an average EC50± SD of 27 ± 31, 26 ± 41, and 28 ± 22 nM, respectively. Maximal percent suppression ± SD of IL-6, IL-8, and TNFα were 76 ± 8.8, 73 ± 15, and 77 ± 13, respectively. To evaluate the specific IRAK4-dependent signaling pathways mediating this response, hMDMs were pretreated with inhibitors of TLR4 (TAK242) and IL-1R (IL-1RA) prior to stimulation with RA synovial fluid. Both TAK242 and IL-1RA inhibited proinflammatory cytokine production. For TAK242, maximal percent suppression ± SD of IL-6, IL-8, and TNFα were 39 ± 25, 48 ± 24, and 50 ± 21, respectively. For IL-1RA maximal percent suppression ± SD of IL-6, IL-8, and TNFα were 18 ± 18, 20 ± 23, and 16 ± 18, respectively. The broad range of inhibition across each stimulation highlights the complexity and variability in the signaling pathways mediating proinflammatory cytokine production from hMDMs stimulated with RA synovial fluid, but demonstrates that RA synovial fluid can stimulate proinflammatory cytokine production in hMDMs, at least partly, through IRAK4-dependent pathways.Conclusion:This work demonstrates that IRAK4 inhibition can suppress proinflammatory cytokine production from macrophages stimulated with synovial fluid from patients with RA and supports a potential pathophysiological role for IRAK4 in perpetuating chronic inflammation in RA.References:[1]Smolen JS, et al.Nat Rev Dis Primers.2018;4:18001.[2]Udalova IA, et al.Nat Rev Rheumatol.2016;12(8):472-485.[3]Joosten LAB, et al.Nat Rev Rheumatol.2016;12(6):344-357.[4]Huang QQ, Pope RM.Curr Rheumatol Rep.2009;11(5):357-364.[5]Roh JS, Sohn DH.Immune Netw.2018;18(4):e27.[6]Sacre SM, et al.Am J Pathol.2007;170(2):518-525.[7]Ultaigh SNA, et al.Arthritis Res Ther.2011;13(1):R33.[8]Bottini N, Firestein GS.Nat Rev Rheumatol.2013;9(1):24-33.[9]Firestein GS, McInnes IB.Immunity.2017;46(2):183-196.[10]Janssens S, Beyaert R.Mol Cell.2003;11(2):293-302.Disclosure of Interests:Adam Yadon Employee of: Gilead, Debbie Ruelas Employee of: Gilead, Gundula Min-Oo Employee of: Gilead, James Taylor Employee of: Gilead, Matthew R. Warr Employee of: Gilead

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Kim, Do-Hoon, Ji-Young Lee, Young-Jin Kim, Hyun-Ju Kim, and Wansu Park. "Rubi Fructus Water Extract Alleviates LPS-Stimulated Macrophage Activation via an ER Stress-Induced Calcium/CHOP Signaling Pathway." Nutrients 12, no. 11 (November 22, 2020): 3577. http://dx.doi.org/10.3390/nu12113577.

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Despite the availability of antibiotics and vaccines, many intractable infectious diseases still threaten human health across the globe. Uncontrolled infections can lead to systemic inflammatory response syndrome and the excessive production of inflammatory cytokines, known as a cytokine storm. As cytokines also play necessary and positive roles in fighting infections, it is important to identify nontoxic and anti-inflammatory natural products that can modulate cytokine production caused by infections. Rubi Fructus, the unripe fruits of Rubus coreanus Miquel, are known to possess antioxidative properties. In this study, the effect of the water extract of Rubi Fructus (RF) on the lipopolysaccharide (LPS)-induced inflammatory response in RAW 264.7 macrophages was investigated using biochemical and cell biology techniques. Our data indicated that RF inhibits p38 phosphorylation, intracellular calcium release, and the production of nitric oxide (NO), interleukin (IL)-6, monocyte chemotactic activating factor (MCP)-1, tumor necrosis factor (TNF)-α, leukemia inhibitory factor (LIF), lipopolysaccharide-induced CXC chemokine (LIX), granulocyte-colony stimulating factor (G-CSF), granulocyte macrophage colony-stimulating factor (GM-CSF), vascular endothelial growth factor (VEGF), macrophage colony-stimulating factor (M-CSF), macrophage inflammatory protein (MIP)-1α, MIP-1β, MIP-2, and regulated on activation, normal T cell expressed and secreted (RANTES) in LPS-treated macrophages. In addition, we observed decreasing mRNA expression of Chop, Camk2a, Stat1, Stat3, Jak2, Fas, c-Jun, c-Fos, Nos2, and Ptgs2 without cytotoxic effects. We concluded that RF demonstrated immunoregulatory activity on LPS-stimulated macrophages via an endoplasmic reticulum (ER) stress-induced calcium/CCAAT-enhancer-binding protein homologous protein (CHOP) pathway and the Janus kinase (JAK)/signal transducers and activators of transcription (STAT) pathway.

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Hines II, Murray E., Charles A. Baldwin, Eloise L. Styer, Gordon A. Hullinger, and John R. Cole. "Effects of macrophage inhibitory factor-A3 (MIF-A3) on cytokine secretion and phagolysosome fusion in murine macrophages." Veterinary Microbiology 65, no. 1 (February 1999): 47–60. http://dx.doi.org/10.1016/s0378-1135(98)00283-1.

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Renz, JF, and GF Kalf. "Role for interleukin-1 (IL-1) in benzene-induced hematotoxicity: inhibition of conversion of pre-IL-1 alpha to mature cytokine in murine macrophages by hydroquinone and prevention of benzene-induced hematotoxicity in mice by IL-1 alpha." Blood 78, no. 4 (August 15, 1991): 938–44. http://dx.doi.org/10.1182/blood.v78.4.938.938.

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Abstract Chronic exposure of humans to benzene (BZ), a myelotoxin, causes aplastic anemia and acute leukemia. The stromal macrophage that produces interleukin-1 (IL-1), a cytokine essential for hematopoiesis, is a target of BZ's toxicity. Monocyte dysfunction and decreased IL-1 production have been shown to be involved in aplastic anemia in humans. Hydroquinone (HQ), a toxic bone marrow (BM) metabolite of BZ, causes time- and concentration-dependent inhibition of processing of the 34-Kd pre-interleukin-1 alpha (IL-1 alpha) to the 17-Kd mature cytokine in murine P388D1 macrophages and BM stromal macrophages, as measured by Western immunoblots of cell lysate proteins using a polyclonal rabbit antimurine IL-1 alpha antibody. HQ over a 10-fold concentration range had no effect on the lipopolysaccharide (LPS)-induced production of pre- IL-1 alpha precursor or on cell viability or DNA and protein synthesis. Stromal macrophages obtained from the femoral BM of C57Bl/6 mice exposed to BZ (600 or 800 mg/kg body weight) for 2 days were incapable of processing the 34-Kd pre-IL-1 alpha to the mature 17-Kd cytokine when stimulated in culture with LPS. Stromal macrophages from mice coadministered BZ and indomethacin, a prostaglandin H synthase (PHS) inhibitor that has been shown to prevent BZ-induced myelotoxic and genotoxic effects in mice when coadministered with benzene were able to convert the pre-IL-1 alpha to mature cytokine. Administration of recombinant murine IL-1 alpha (rMuIL-1 alpha) to mice before a dose of BZ that causes severe depression of BM cellularity completely prevents BM depression, most probably by bypassing the inability of the stromal macrophage in BZ-treated animals to process pre-IL-1 alpha to the mature cytokine.

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Renz, JF, and GF Kalf. "Role for interleukin-1 (IL-1) in benzene-induced hematotoxicity: inhibition of conversion of pre-IL-1 alpha to mature cytokine in murine macrophages by hydroquinone and prevention of benzene-induced hematotoxicity in mice by IL-1 alpha." Blood 78, no. 4 (August 15, 1991): 938–44. http://dx.doi.org/10.1182/blood.v78.4.938.bloodjournal784938.

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Chronic exposure of humans to benzene (BZ), a myelotoxin, causes aplastic anemia and acute leukemia. The stromal macrophage that produces interleukin-1 (IL-1), a cytokine essential for hematopoiesis, is a target of BZ's toxicity. Monocyte dysfunction and decreased IL-1 production have been shown to be involved in aplastic anemia in humans. Hydroquinone (HQ), a toxic bone marrow (BM) metabolite of BZ, causes time- and concentration-dependent inhibition of processing of the 34-Kd pre-interleukin-1 alpha (IL-1 alpha) to the 17-Kd mature cytokine in murine P388D1 macrophages and BM stromal macrophages, as measured by Western immunoblots of cell lysate proteins using a polyclonal rabbit antimurine IL-1 alpha antibody. HQ over a 10-fold concentration range had no effect on the lipopolysaccharide (LPS)-induced production of pre- IL-1 alpha precursor or on cell viability or DNA and protein synthesis. Stromal macrophages obtained from the femoral BM of C57Bl/6 mice exposed to BZ (600 or 800 mg/kg body weight) for 2 days were incapable of processing the 34-Kd pre-IL-1 alpha to the mature 17-Kd cytokine when stimulated in culture with LPS. Stromal macrophages from mice coadministered BZ and indomethacin, a prostaglandin H synthase (PHS) inhibitor that has been shown to prevent BZ-induced myelotoxic and genotoxic effects in mice when coadministered with benzene were able to convert the pre-IL-1 alpha to mature cytokine. Administration of recombinant murine IL-1 alpha (rMuIL-1 alpha) to mice before a dose of BZ that causes severe depression of BM cellularity completely prevents BM depression, most probably by bypassing the inability of the stromal macrophage in BZ-treated animals to process pre-IL-1 alpha to the mature cytokine.

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Albertoni, Michele, Phillip H. Shaw, Michimasa Nozaki, Sophie Godard, Mirna Tenan, Marie-France Hamou, Douglas W. Fairlie, et al. "Anoxia induces macrophage inhibitory cytokine-1 (MIC-1) in glioblastoma cells independently of p53 and HIF-1." Oncogene 21, no. 27 (June 2002): 4212–19. http://dx.doi.org/10.1038/sj.onc.1205610.

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Crilly, Anne, Susan E. Robertson, James H. Reilly, J. Alastair Gracie, Wen-Qi Lai, Bernard P. Leung, Paul F. Life, and Iain B. McInnes. "Phosphodiesterase 4 (PDE4) regulation of proinflammatory cytokine and chemokine release from rheumatoid synovial membrane." Annals of the Rheumatic Diseases 70, no. 6 (February 21, 2011): 1130–37. http://dx.doi.org/10.1136/ard.2010.134825.

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BackgroundThe cAMP-metabolising enzyme, phosphodiesterase 4 (PDE4), has been implicated in a number of immune responses, including tumour necrosis factor α (TNFα) production. To date, few data have directly addressed whether synovial cytokine and chemokine production is modified by PDE4.ObjectiveUsing specific PDE4 inhibitors, roflumilast plus two novel inhibitors, INH 0061 and INH 0062, the authors studied the effect of PDE4 inhibition on proinflammatory cytokine and chemokine release from primary rheumatoid arthritis (RA) synovial digest suspensions and in a macrophage T cell co-culture assay system.ResultsAll PDE4 inhibitors dose-dependently reduced the release of TNFα from primary synovial membrane cultures (n=5), half maximal inhibitory concentration (IC50) 300–30 nM, p<0.05. Similarly, a significant suppression in the release the proinflammatory chemokines, monocyte chemoattractant protein-1 (MCP-1), macrophage inflammatory protein (MIP)-1α, MIP-1β (IC50 300–30 nM) and regulated upon activation normal T-cell expressed and secreted (RANTES) (IC50 3 nM) was also observed, p<0.05. While interleukin 1β was also reduced, it did not achieve an IC50. These observations were further confirmed in a macrophage T cell co-culture system, demonstrating the importance of PDE4 pathways in regulating cytokine/chemokine release in a cellular interaction implicated in inflammatory synovitis. Subsequent studies using the human monocytic cell line U937 also demonstrated cytokine regulation with PDE4 knockdown utilising a small interfering RNA approach.ConclusionThese data provide direct evidence of PDE4-dependent pathways in human RA synovial inflammatory cytokine and chemokine release and may provide a novel approach in treating chronic autoimmune conditions such as RA.

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Leyva-Illades, Dinorah, Rama P. Cherla, Moo-Seung Lee, and Vernon L. Tesh. "Regulation of Cytokine and Chemokine Expression by the Ribotoxic Stress Response Elicited by Shiga Toxin Type 1 in Human Macrophage-Like THP-1 Cells." Infection and Immunity 80, no. 6 (March 19, 2012): 2109–20. http://dx.doi.org/10.1128/iai.06025-11.

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ABSTRACTShiga toxins (Stxs) are cytotoxins produced by the enteric pathogensShigella dysenteriaeserotype 1 and Shiga toxin-producingEscherichia coli(STEC). Stxs bind to a membrane glycolipid receptor, enter cells, and undergo retrograde transport to ultimately reach the cytosol, where the toxins exert their protein synthesis-inhibitory activity by depurination of a single adenine residue from the 28S rRNA component of eukaryotic ribosomes. The depurination reaction activates the ribotoxic stress response, leading to signaling via the mitogen-activated protein kinase (MAPK) pathways (Jun N-terminal protein kinase [JNK], p38, and extracellular signal-regulated kinase [ERK]) in human epithelial, endothelial, and myeloid cells. We previously showed that treatment of human macrophage-like THP-1 cells with Stxs resulted in increased cytokine and chemokine expression. In the present study, we show that individual inactivation of ERK, JNK, and p38 MAPKs using pharmacological inhibitors in the presence of Stx1 resulted in differential regulation of the cytokines tumor necrosis factor alpha and interleukin-1β (IL-1β) and chemokines IL-8, growth-regulated protein-β, macrophage inflammatory protein-1α (MIP-1α), and MIP-1β. THP-1 cells exposed to Stx1 upregulate the expression of select dual-specificity phosphatases (DUSPs), enzymes that dephosphorylate and inactivate MAPKs in mammalian cells. In this study, we confirmed DUSP1 protein production by THP-1 cells treated with Stx1. DUSP1 inhibition by triptolide showed that ERK and p38 phosphorylation is regulated by DUSP1, while JNK phosphorylation is not. Inhibition of p38 MAPK signaling blocked the ability of Stx1 to induce DUSP1 mRNA expression, suggesting that an autoregulatory signaling loop may be activated by Stxs. Thus, Stxs appear to be capable of eliciting signals which both activate and deactivate signaling for increased cytokine/chemokine production in human macrophage-like cells.

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Golkar, L., X. Ding, M. B. Ujiki, R. M. Salabat, D. J. Bentrem, M. S. Talamonti, R. H. Bell, and T. E. Adrian. "Resveratrol inhibits pancreatic cancer cell proliferation through transcriptional induction of macrophage inhibitory cytokine-1 (MIC-1)." Journal of Surgical Research 130, no. 2 (February 2006): 195. http://dx.doi.org/10.1016/j.jss.2005.11.094.

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Sian, Lee Jian, Malina Jasamai, Nor Syafinaz Yaakob, and Norsyahida Mohd Fauzi. "Synthetic chalcone derivatives inhibit cytokine secretion via inhibition of ERK and JNK pathways in human U937 macrophage." Tropical Journal of Pharmaceutical Research 18, no. 4 (May 18, 2021): 753–59. http://dx.doi.org/10.4314/tjpr.v18i4.11.

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Purpose: To investigate the inhibitory effects of a chalcone derivative on lipopolysaccharide (LPS)- induced interleukin (IL)-6 and IL-8 secretions and on LPS-induced mitogen-activated protein kinases (MAPK) and nuclear factor kappa B (NF-κB) activation in human U937 macrophage-like cell line. Methods: The effects of chalcone derivative on LPS-induced secretion of IL-6 and IL-8 in endothelial cells were determined by enzyme-linked immunosorbent assay while the effects of chalcone on the activation of MAPK and NF-kB pathway were determined by Western blotting. Results: The results showed that 3-(5-methyl-furan-2-yl)-naphthalen-1-yl-propenone (compound 1) significantly inhibited the secretion of LPS-induced IL-6 and IL-8 in U937 macrophages. This compound also demonstrated significant suppression of c-Jun N-terminal kinases (JNK) and extracellular signalregulated kinases (ERK) phosphorylation. However, the compound did not reverse the degradation of inhibitor kappa B alpha (IκBα) and did not inhibit the phosphorylation of NF-κB subunit and P-38 MAPK. Conclusion: Compound 1 inhibits the secretion of cytokines via the inhibition of ERK and JNK pathways. These results suggest that chalcone derivative could act as an antiinflammatory agent by altering cytokine secretion and inflammatory pathways.

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Stojanovic, Ivana, Danijela Maksimovic-Ivanic, Y. Al-Abed, F. Nicoletti, and Stanislava Stosic-Grujicic. "Control of the of the final stage of immune-mediated diabetes by ISO-1, an antagonist of macrophage migration inhibitory factor." Archives of Biological Sciences 60, no. 3 (2008): 389–401. http://dx.doi.org/10.2298/abs0803389s.

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We recently showed that attenuation of inflammatory cytokine MIF with pharmacological inhibitor ISO-1 down-regulates the immune-mediated diabetes in mice. Here we explore the effects of MIF neutralization by ISO-1 on the local inflammatory pathway of the disease. In vivo treatment of mice with ISO-1 inhibited the expression of pro-inflammatory cytokines and iNOS in the pancreatic islets. Moreover, ISO-1 affected in vitro cytokine-induced NO pro?duction by fibroblasts, endothelial cells, insulinoma cells, and pancreatic islets, and rescued ? cells from NO-dependent damage. These results suggest regulatory potential of ISO-1 at the level of the pancreas which can preserve the target tissue from autoimmune attack.

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Lu, Hong, Yongyu Bai, Lianfeng Wu, Weilong Hong, Yong Liang, Bicheng Chen, and Yongheng Bai. "Inhibition of Macrophage Migration Inhibitory Factor Protects against Inflammation and Matrix Deposition in Kidney Tissues after Injury." Mediators of Inflammation 2016 (2016): 1–12. http://dx.doi.org/10.1155/2016/2174682.

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Background. Macrophage migration inhibitory factor (MIF) is an important immunoregulatory cytokine involved in inflammation, which may be one important reason resulting in matrix deposition in renal tissues after injury. However, the underlying mechanisms have not yet been elucidated.Methods and Results. We uncovered a crucial role of MIF in inflammation and collagen depositionin vivoandin vitro. In rats, ureteral obstruction induced tubular injury, matrix accumulation, and inflammatory cell infiltration. Additionally, enhanced MIF levels in the obstructed kidneys were closely related to the increasing numbers of CD68-positive macrophages. These obstruction-induced injuries can be relieved by recanalization, consequently resulting in downregulated expression of MIF and its receptor CD74. Similarly, ischemia reperfusion induced renal injury, and it was accompanied by elevated MIF levels and macrophages infiltration. In cultured tubular epithelial cells (TECs), aristolochic acid (AA) promoted matrix production and increased MIF expression, as well as the release of macrophage-related factors. Inhibition of MIF with an antagonist ISO-1 resulted in the abolishment of these genotypes in AA-treated TECs.Conclusion. MIF plays an important role in macrophage-related inflammation and matrix deposition in kidney tissues following injury. MIF as a specific inhibitor may have therapeutic potential for patients with inflammatory and fibrotic kidney diseases.

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DUBEY, SEEMA, PETER VANVELDHUIZEN, JEFFREY HOLZBEIERLEIN, OSSAMA TAWFIK, J. BRANTLEY THRASHER, and DEV KARAN. "Inflammation-associated regulation of the macrophage inhibitory cytokine (MIC-1) gene in prostate cancer." Oncology Letters 3, no. 5 (March 6, 2012): 1166–70. http://dx.doi.org/10.3892/ol.2012.635.

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Golkar, Laleh, Xian-Zhong Ding, Michael B. Ujiki, Mohammad R. Salabat, David L. Kelly, Denise Scholtens, Angela J. Fought, et al. "Resveratrol Inhibits Pancreatic Cancer Cell Proliferation Through Transcriptional Induction of Macrophage Inhibitory Cytokine-1." Journal of Surgical Research 138, no. 2 (April 2007): 163–69. http://dx.doi.org/10.1016/j.jss.2006.05.037.

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Karczewska-Kupczewska, Monika, Irina Kowalska, Agnieszka Nikolajuk, Agnieszka Adamska, Elzbieta Otziomek, Maria Gorska, and Marek Straczkowski. "Hyperinsulinemia acutely increases serum macrophage inhibitory cytokine-1 concentration in anorexia nervosa and obesity." Clinical Endocrinology 76, no. 1 (December 7, 2011): 46–50. http://dx.doi.org/10.1111/j.1365-2265.2011.04139.x.

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Du, Zhong-Hong, Xiao-Ping Wei, and Qi-Yuan Hui. "Role of macrophage inhibitory cytokine-1 in the development and progression of gastric cancer." World Chinese Journal of Digestology 17, no. 22 (2009): 2272. http://dx.doi.org/10.11569/wcjd.v17.i22.2272.

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Baumgart, Samuel, Deborah A. Barber, Hong Ping Zhang, Michelle Lee-Ng, Samuel Breit, David Brown, and Mark Danta. "Macrophage Inhibitory Cytokine 1 (MIC1/GDF15) as a Novel Serum Biomarker of Colonic Neoplasia." Gastroenterology 152, no. 5 (April 2017): S1030. http://dx.doi.org/10.1016/s0016-5085(17)33483-2.

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Danta, M., D. A. Barber, H. P. Zhang, M. Lee-Ng, S. W. L. Baumgart, V. W. W. Tsai, Y. Husaini, et al. "Macrophage inhibitory cytokine-1/growth differentiation factor-15 as a predictor of colonic neoplasia." Alimentary Pharmacology & Therapeutics 46, no. 3 (June 1, 2017): 347–54. http://dx.doi.org/10.1111/apt.14156.

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Koopmann, Jens, Phillip Buckhaults, David A. Brown, Marianna L. Zahurak, Norihiro Sato, Noriyoshi Fukushima, Lori J. Sokoll, et al. "Serum Macrophage Inhibitory Cytokine 1 as a Marker of Pancreatic and Other Periampullary Cancers." Clinical Cancer Research 10, no. 7 (April 1, 2004): 2386–92. http://dx.doi.org/10.1158/1078-0432.ccr-03-0165.

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Mimeault, Murielle, and Surinder K. Batra. "Divergent molecular mechanisms underlying the pleiotropic functions of macrophage inhibitory cytokine-1 in cancer." Journal of Cellular Physiology 224, no. 3 (May 12, 2010): 626–35. http://dx.doi.org/10.1002/jcp.22196.

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