Regular ArticleGlycated Serum Albumin-Induced Nitric Oxide Production in Vascular Smooth Muscle Cells by Nuclear Factor κB-Dependent Transcriptional Activation of Inducible Nitric Oxide Synthase☆
References (42)
- et al.
J. Biol. Chem.
(1981) - et al.
Kidney Int.
(1994) - et al.
J. Immunol. Methods
(1989) - et al.
Kidney Int.
(1994) - et al.
Kidney Int.
(1997) - et al.
Anal. Biochem.
(1987) - et al.
J. Biol. Chem.
(1992) - et al.
Biochem. Biophys. Res. Commun.
(1993) - et al.
J. Biol. Chem.
(1994) - et al.
Am. J. Med.
(1988)
Adv. Prot. Chem.
Cell
FEBS Lett.
Arch. Biochem. Biophys.
Biochim. Biophys. Acta
Biochim. Biophys. Acta
Prog. Clin. Biol. Res.
Diabetologia.
Ann. Int. Med.
N. Engl. J. Med.
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Glycated human serum albumin induces NF-κB activation and endothelial nitric oxide synthase uncoupling in human umbilical vein endothelial cells
2015, Journal of Diabetes and its ComplicationsCitation Excerpt :This NF-κB activation could be the reason for the gHSA-induced increase in NOX4 at the mRNA level, as observed in this work, and at the protein level, as reported previously (Rodino-Janeiro et al., 2010). NF-κB activation by glycated proteins has been previously described in vascular smooth muscle cells (Hattori, Banba, Gross, & Kasai, 1999), macrophage RAW cells (Cohen, Shea, Chen, & Shearman, 2003) and human peritoneal mesothelial cells (Nevado et al., 2005). Manea et al. (2010) showed that NF-κB regulated NOX4 expression in human aortic vascular smooth muscle cells, but they did not observe an activation of NF-kB at 4 h as we did.
Impact of elevated serum glycated albumin levels on contrast-induced acute kidney injury in diabetic patients with moderate to severe renal insufficiency undergoing coronary angiography
2013, International Journal of CardiologyCitation Excerpt :The increased reactive oxygen species resulting from renal ischemia could in turn augment the vasoconstrictive effects of CM [35]. This self-reinforcing pathophysiological cycle is partly triggered by nonenzymatically GA via activation of nuclear factor-κB and decreased nitric oxide dependent vasodilation [36,37]. Further studies are needed to clarify the exact mechanism of higher GA levels predisposing to CI-AKI.
Clinical, pathophysiological and structure/function consequences of modification of albumin by Amadori-glucose adducts
2013, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :AGA also stimulates adhesion of monocytes to endothelial cells through enhanced transcription of the cell surface adhesion molecules E-selectin, vascular adhesion molecule (VCAM)-1 and intercellular adhesion molecule (ICAM)-1, implicating it in the initial endothelial cell activation occurring at atherosclerosis-prone vascular sites [59–61]. In vascular smooth muscle cells, AGA activates NF-κB, AP-1, p38 MAPK and ERK, increases expression and release of MCP-1, IL-6 and IL-8, stimulates growth and migration, and induces expression of the anti-apoptotic inhibitor of apoptosis protein (IAP)-1 [62–66]. The pathophysiologic and clinical relevance of the above studies is underscored by the positive association of AGA with atherosclerosis and coronary artery disease [21,22].
Serum Advanced Glycation End-Products and Receptors as Prognostic Biomarkers in Diabetics Undergoing Coronary Artery Stent Implantation
2012, Canadian Journal of CardiologyGlycated albumin activates NADPH oxidase in rat mesangial cells through up-regulation of p47phox
2010, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Furthermore, we demonstrated that p47phox-depdendent NADPH oxidase activity mediates glycated albumin-induced stimulation of TGF-β and resultant extracellular matrix protein production in mesangial cells. It is known that glycated albumin activated NF-κB in a variety of cell types [28–33]. NF-κB is an important redox-sensitive transcription factor and has been implicated in the development of renal diseases [34].
Cellular factors involved in CXCL8 expression induced by glycated serum albumin in vascular smooth muscle cells
2010, AtherosclerosisCitation Excerpt :Promoter activation of the IL-8 gene was significantly suppressed by an ERK1/2 inhibitor, and CXCL8 release was profoundly inhibited by both ERK and p38 MAPK inhibitors. These results, along with previous reports [8,9,27], reinforce the idea that MAPKs are important molecules mediating cellular and molecular responses to GSA in VSMCs. We observed differences in the manner in which p38 MAPK inhibitor affects IL-8 up-regulation.
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Moncada, S.Stamler, J.Gross, S.Higgs, E.A.
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Corresponding author. Fax: + 81 282 (86) 4632. E-mail:[email protected].