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Chin Hee Mun,Won Taek Lee,Kyung Ah Park,Jong Eun Lee 대한해부학회 2010 Anatomy & Cell Biology Vol.43 No.3
Nitric oxide (NO) production by endothelial nitric oxide synthase (eNOS) plays a protective role in cerebral ischemia by maintaining vascular permeability, whereas NO derived from neuronal and inducible NOS is neurotoxic and can participate in neuronal damage occurring in ischemia. Matrix metalloproteinases (MMPs) are up-regulated by ischemic injury and degrade the basement membrane if brain vessels to promote cell death and tissue injury. We previously reported that agmatine, synthesized from L-arginine by arginine decarboxylase (ADC) which is expressed in endothelial cells, has shown a direct increased eNOS expression and decreased MMPs expression in bEnd3 cells. But, there are few reports about the regulation of eNOS by agmatine in ischemic animal model. In the present study, we examined the expression of eNOS and MMPs by agmatine treatment after transient global ischemia in vivo. Global ischemia was induced with four vessel occlusion (4-VO) and agmatine (100 mg/kg) was administered intraperitoneally at the onset of reperfusion. The animals were euthanized at 6 and 24 hours after global ischemia and prepared for other analysis. Global ischemia led severe neuronal damage in the rat hippocampus and cerebral cortex, but agmatine treatment protected neurons from ischemic injury. Moreover, the level and expression of eNOS was increased by agmatine treatment, whereas inducible NOS (iNOS) and MMP-9 protein expressions were decreased in the brain. These results suggest that agmatine protects microvessels in the brain by activation eNOS as well as reduces extracellular matrix degradation during the early phase of ischemic insult.
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Han Byeol Kim,Sang-WonLee,ChinHeeMun,JiYoungYoon,JaeyoungPai,InjaeShin,Yong-BeomPark,Soo-KonLee,JinWonCho 한국당과학회 2016 한국당과학회 학술대회 Vol.2016 No.01
O-linked N-acetylglucosamine (O-GlcNAc) modification is unique glycosylations and it can occur exclusively in nucleus and cytoplasm. O-GlcNAc is attached onto a serine or threonine residue of a protein by O-GlcNAc transferase (OGT) and detached by O-GlcNAcase (OGA) under dynamic regulations by a variety of conditions. O-GlcNAcylation is associated with several clinical situations including cancers and inflammatory diseases. The effect of O-GlcNAcylation of subunits of nuclear factor-ĸB on its transcriptional activity has been reported to date. Interestingly, O-GlcNAc modification of NF-ĸB exhibited reciprocal results on its activity depending on different cell types: increased O-GlcNAcylation elevated the activity of NF-ĸB in pancreatic cancer cells, while aortic smooth muscle cells showed negative correlation between O-GlcNAcylation and NF-ĸB activity In Rheumatoid Arthirtis (RA), NF-ĸB is the novel regulator of pro-inflammatory cytokines mediating synovitis, long-term cartilage degradation and bone erosion. We hypothesize that the alteration in the activity of NF-ĸB resulting from its O-GlcNAcylation might affect the severity of RA. There was no report on the effect of O-GlcNAcylation of NF-ĸB on its activity in RA. We used in vitro synoviocytes and in vivo in mice with collagen induced arthritis (CIA) and investigated the inflammatory potential of O-GlcNAcylation of P65, one of subunits of NF-ĸB, in the pathogenesis of RA.
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