Secretion of interleukin-6 and prostaglandin E2 during uveal melanoma-monocyte in vitro interactions

2004 ◽  
Vol 79 (4) ◽  
pp. 451-454 ◽  
Author(s):  
Jonathan Cools-Lartigue ◽  
Jean Claude Marshall ◽  
Amanda L. Caissie ◽  
Vinicius S. Saraiva ◽  
Miguel N. Burnier
Keyword(s):  
Prostaglandin E2 ◽  
Uveal Melanoma ◽  
Interleukin 6 ◽  
In Vitro Interactions

scholarly journals Stimulation of interleukin-6 and prostaglandin E2 secretion from peritoneal macrophages by polymers of albumin

Blood ◽  
1993 ◽  
Vol 82 (9) ◽  
pp. 2853-2864 ◽  
Author(s):  
E Shacter ◽  
GK Arzadon ◽  
JA Williams
Keyword(s):  
Prostaglandin E2 ◽  
Interleukin 6 ◽  
Acute Infection ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Polymyxin B ◽  
Peritoneal Macrophages ◽  
Stimulatory Activity

Abstract Interleukin-6 (IL-6) is a multifunctional cytokine that is elevated in vivo during acute infection, chronic inflammation, and some hematopoietic malignancies. To understand how IL-6 becomes elevated in vivo, it is important to identify factors that can stimulate its secretion from effector cells. We found that commercial preparations of bovine serum albumin (BSA) stimulated murine macrophages to secrete high levels of IL-6. In fact, BSA was at least as potent as bacterial lipopolysaccharide (LPS) in stimulating IL-6 production. Stimulation was clearly visible at concentrations as low as 20 micrograms/mL and reached saturation at 0.5 to 1 mg/mL albumin, at which concentration 1.1 x 10(6) oil-elicited macrophages produced 6,000 +/- 700 B9 units of IL-6 in an overnight incubation. Prostaglandin E2 production was induced by the same concentrations of BSA. Both resident and oil- elicited peritoneal cells were responsive to the albumin. The stimulatory activity did not derive from contamination of the protein with Escherichia coli LPS; when compared directly with LPS, the response to BSA was more rapid, had a higher amplitude, and was not inhibitable by polymyxin B. In addition, macrophages isolated from C3H/HeJ mice, which have an inherited defect in their ability to respond to LPS, secreted IL-6 in response to BSA but not to LPS. The stimulatory activity was stable to heat, mild acid, and reduction/alkylation and copurified with albumin on Cibachron Blue agarose (Sigma, St Louis, MO) and anti-albumin immunoaffinity chromatography. Comparison of different sources and preparations of albumin showed differences in the levels of IL-6-inducing activity; three different lots of commercial fatty acid-free BSA and one lot of polymer-enhanced BSA stimulated IL-6 secretion by more than 100-fold over basal levels whereas other preparations showed more limited activity. A sample of BSA that was active in vitro caused a marked elevation of IL-6 when injected into BALB/c mice, thus demonstrating inflammatory activity in vivo. When the albumin preparations were fractionated by ion exchange and gel filtration chromatography and then analyzed by sodium dodecyl sulfate-gel electrophoresis and Western blot immunoassay, it was found that the IL-6-inducing activity resided in high molecular weight polymers of albumin. The ability of albumin polymers to stimulate IL-6 production represents a novel mechanism for modulation of this cytokine.

Synthesis and In Vitro Anti-inflammatory Activity of C20 Epimeric Ocotillol-Type Triterpenes and Protopanaxadiol

Planta Medica ◽  
2018 ◽  
Vol 85 (04) ◽  
pp. 292-301 ◽  
Author(s):  
Jianqiang Zhang ◽  
Qian Zhang ◽  
Yangrong Xu ◽  
Huixiang Li ◽  
Fenglan Zhao ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Prostaglandin E2 ◽  
Interleukin 6 ◽  
Inflammatory Mediator ◽  
Interleukin 10 ◽  
Inflammatory Activity ◽  
Raw 264.7 Cells ◽  
Tnf Α ◽  
Anti Inflammatory

AbstractGinseng is a perennial herb that contains various medicinal substances. The major active constituents of ginseng are ginsenosides, which have multifarious biological activities. Some pharmacological activities are closely dependent on the stereoisomers derived from the configuration at C20. In this study, the in vitro anti-inflammatory activity of C20 epimeric ocotillol-type triterpenes (2, 3, 9, and 10) and protopanaxadiol [20(S/R)-protopanaxadiol] were investigated. Epimers 2 and 3 were prepared starting from 20(S)-protopanaxadiol. Epimers 9 and 10 were synthesized from 20(R)-3-acetylprotopanaxadiol (7). The anti-inflammatory activity of 2, 3, 9, 10, 20(S)-protopanaxadiol, and 20(R)-protopanaxadiol was evaluated in cultured mouse macrophage RAW 264.7 cells. The MTT assay was used to measure the cytotoxicity. RAW 264.7 cells were stimulated by lipopolysaccharide to release the inflammatory mediators nitric oxide, prostaglandin E2, TNF-α, and interleukin-6 and anti-inflammatory mediator interleukin-10. The effect of the compounds on the overproduction of nitric oxide, prostaglandin E2, TNF-α, interleukin-6, and interleukin-10 was determined using Griess and ELISA methods. The results demonstrated that the in vitro anti-inflammatory activities of C20 epimeric ocotillol-type triterpenes and protopanaxadiol were different. Both the 20S-epimers (2 and 3) and 20R-epimers (9 and 10) inhibited the release of inflammatory mediator nitric oxide, while mainly the 20S-epimers inhibited the release of inflammatory mediator prostaglandin E2, and the 20R-epimers inhibited the release of inflammatory cytokine TNF-α. Both the 20S-epimers [2, 3, and 20(S)-protopanaxadiol] and 20R-epimers [9, 10, and 20(R)-protopanaxadiol] inhibited the release of inflammatory cytokine interleukin-6, but mainly the 20S-epimers [2, 3, and 20(S)-protopanaxadiol] increased the release of anti-inflammatory mediator interleukin-10.

scholarly journals Stimulation of interleukin-6 and prostaglandin E2 secretion from peritoneal macrophages by polymers of albumin

Blood ◽  
1993 ◽  
Vol 82 (9) ◽  
pp. 2853-2864 ◽  
Author(s):  
E Shacter ◽  
GK Arzadon ◽  
JA Williams
Keyword(s):  
Prostaglandin E2 ◽  
Interleukin 6 ◽  
Acute Infection ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Polymyxin B ◽  
Peritoneal Macrophages ◽  
Stimulatory Activity

Interleukin-6 (IL-6) is a multifunctional cytokine that is elevated in vivo during acute infection, chronic inflammation, and some hematopoietic malignancies. To understand how IL-6 becomes elevated in vivo, it is important to identify factors that can stimulate its secretion from effector cells. We found that commercial preparations of bovine serum albumin (BSA) stimulated murine macrophages to secrete high levels of IL-6. In fact, BSA was at least as potent as bacterial lipopolysaccharide (LPS) in stimulating IL-6 production. Stimulation was clearly visible at concentrations as low as 20 micrograms/mL and reached saturation at 0.5 to 1 mg/mL albumin, at which concentration 1.1 x 10(6) oil-elicited macrophages produced 6,000 +/- 700 B9 units of IL-6 in an overnight incubation. Prostaglandin E2 production was induced by the same concentrations of BSA. Both resident and oil- elicited peritoneal cells were responsive to the albumin. The stimulatory activity did not derive from contamination of the protein with Escherichia coli LPS; when compared directly with LPS, the response to BSA was more rapid, had a higher amplitude, and was not inhibitable by polymyxin B. In addition, macrophages isolated from C3H/HeJ mice, which have an inherited defect in their ability to respond to LPS, secreted IL-6 in response to BSA but not to LPS. The stimulatory activity was stable to heat, mild acid, and reduction/alkylation and copurified with albumin on Cibachron Blue agarose (Sigma, St Louis, MO) and anti-albumin immunoaffinity chromatography. Comparison of different sources and preparations of albumin showed differences in the levels of IL-6-inducing activity; three different lots of commercial fatty acid-free BSA and one lot of polymer-enhanced BSA stimulated IL-6 secretion by more than 100-fold over basal levels whereas other preparations showed more limited activity. A sample of BSA that was active in vitro caused a marked elevation of IL-6 when injected into BALB/c mice, thus demonstrating inflammatory activity in vivo. When the albumin preparations were fractionated by ion exchange and gel filtration chromatography and then analyzed by sodium dodecyl sulfate-gel electrophoresis and Western blot immunoassay, it was found that the IL-6-inducing activity resided in high molecular weight polymers of albumin. The ability of albumin polymers to stimulate IL-6 production represents a novel mechanism for modulation of this cytokine.

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