scholarly journals Briarenol B, a New Polyoxygenated Briarane from the Octocoral Briareum excavatum

2017 ◽  
Vol 12 (2) ◽  
pp. 1934578X1701200
Author(s):  
Mu-Jang Li ◽  
Yin-Di Su ◽  
Zuo-Jian Liao ◽  
Zhi-Hong Wen ◽  
Jui-Hsin Su ◽  
...  

A new polyoxygenated briarane diterpenoid, briarenol B (1), was isolated from the octocoral Briareum excavatum and its structure determined from spectroscopic data. In RAW264.7 cells, a macrophage-like murine cell line, briarane B (1) was found to enhance the protein expression of pro-inflammatory cyclooxygenase (COX-2) and inducible nitric oxide synthase (iNOS) in cells stimulated by lipopolysaccharide (LPS).

2018 ◽  
Vol 13 (10) ◽  
pp. 1934578X1801301 ◽  
Author(s):  
Tsung-Chang Tsai ◽  
Jing-Hao Xu ◽  
Mu-Jang Li ◽  
Jih-Jung Chen ◽  
Jui-Hsin Su ◽  
...  

A new briarane-type diterpenoid, briaviolide Q (1), along with a known analogue, excavatolide Z (2), were obtained from a cultured octocoral Briareum violaceum. Details of the isolation and structure determination of briarane 1 from spectroscopic data are presented in this paper. In RAW264.7 cells, a macrophage-like murine cell line, briarane 1 was found to inhibit the protein expression of pro-inflammatory inducible nitric oxide synthase (iNOS) in cells stimulated by lipopolysaccharide (LPS).


2010 ◽  
Vol 5 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Eun-Jin Yang ◽  
Jong-Gwan Kim ◽  
Ji-Young Kim ◽  
Seong Kim ◽  
Nam Lee ◽  
...  

AbstractWe examined the effects of chitosan oligosaccharides (COSs) with different molecular weights (COS-A, 10 kDa < MW < 20 kDa; COS-C, 1 kDa < MW < 3 kDa) on the lipopolysaccharide (LPS)-induced production of prostaglandin E2 and nitric oxide and on the expression of cyclooxygenase-2 and inducible nitric oxide synthase in RAW264.7 macrophages. COS-A (0.4%) and COS-C (0.2%) significantly inhibited PGE2 production in LPS-stimulated macrophages without cytotoxicity. The effect of COS-A and COS-C on COX-2 expression in activated macrophages was also investigated by immunoblotting. The inhibition of PGE2 by COS-A and COS-C can be attributed to the blocking of COX-2 protein expression. COS-A (0.4%) and COS-C (0.2%) also markedly inhibited the LPS-induced NO production of RAW 264.7 cells by 50.2% and 44.1%, respectively. The inhibition of NO by COSs was consistent with decreases in inducible nitric oxide synthase (iNOS) protein expression. To test the inhibitory effects of COS-A and COS-C on other cytokines, we also performed ELISA assays for IL-1β in LPS-stimulated RAW 264.7 macrophage cells, but only a dose-dependent decrease in the IL-1β production exerted by COS-A was observed. In order to test for irritation and the potential sensitization of COS-A and COS-C for use as cosmetic materials, human skin primary irritation tests were performed on 32 volunteers; no adverse reactions of COSs usage were observed. Based on these results, we suggest that COS-A and COS-C be considered possible anti-inflammatory candidates for topical application.


1999 ◽  
Vol 126 (5) ◽  
pp. 1253-1261 ◽  
Author(s):  
Peter J Syapin ◽  
Alexia Rendon ◽  
David R Huron ◽  
Julius D Militante

2006 ◽  
Vol 291 (3) ◽  
pp. F567-F577 ◽  
Author(s):  
Li-Mei Chen ◽  
Cindy Wang ◽  
Mengqian Chen ◽  
Matthew R. Marcello ◽  
Julie Chao ◽  
...  

Prostasin is a glycosylphosphatidylinositol-anchored serine protease, with epithelial sodium channel activation and tumor invasion suppression activities. We identified the bladder as an expression site of prostasin. In the mouse, prostasin mRNA expression was detected by reverse transcription and real-time polymerase chain reaction in the bladder, and the prostasin protein was localized by immunohistochemistry in the urothelial cells. In mice injected intraperitoneally with bacterial lipopolysaccharide (LPS), bladder prostasin mRNA expression was downregulated, whereas the expression of inducible nitric oxide synthase (iNOS), cyclooxygenase-2 (COX-2), interferon-γ (IFN-γ), TNF-α, IL-1β, and IL-6 was upregulated. Viral promoter-driven expression of the human prostasin homolog in the bladder of transgenic mice attenuated the LPS induction of iNOS but did not abolish the induction. LPS induction of COX-2, TNF-α, IL-1β, and IL-6 expression, however, was not reduced by prostasin transgene expression. Liposome-mediated delivery of prostasin-expressing plasmid into mouse bladder produced similar attenuation effects on LPS-induced iNOS expression, while not affecting COX-2 or cytokine induction. Mice receiving plasmid expressing a catalytic mutant prostasin did not manifest the iNOS induction attenuation phenotype. We propose a proteolytic mechanism for prostasin to intercept cytokine signaling during LPS-induced bladder inflammation.


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