Glycated albumin increases oxidative stress, activates NF-κB and extracellular signal-regulated kinase (ERK), and stimulates ERK-dependent transforming growth factor-β1 production in macrophage RAW cells

Cohen, Morrel H.; Shea, Elizabeth; Chen, Sheldon; Shearman, Clyde W.

doi:10.1067/mlc.2003.27

Cited by 101 publications

(59 citation statements)

References 56 publications

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“…This is consistent with a previous report showing that the binding of glycated albumin to MonoMac 6 cells leads to the activation of p44/42 and p38 MAPKs with the subsequent translocation of NF-B to the nucleus (1). In addition, the p44/42 MAPKs-dependent activation of NF-B occurs in macrophage RAW cells after NADPH oxidase stimulation (10). Hence, these results suggest that BSA-induced DNA synthesis is mediated by Ca 2ϩ , PKC, p44/42 MAPK, and NF-B signal pathways.…”

Section: Discussionmentioning

confidence: 66%

Albumin-stimulated DNA synthesis is mediated by Ca²⁺/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

Lee¹,

Han²

2008

American Journal of Physiology-Renal Physiology

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Section: Discussionmentioning

confidence: 66%

Albumin-stimulated DNA synthesis is mediated by Ca²⁺/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

Lee¹,

Han²

2008

American Journal of Physiology-Renal Physiology

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“…-LA has been reported to suppress NF-B activation in cells of the monocyte lineage cells, such as the RAW 246·7 (Cohen et al 2003) and MonoMac6 (Lee & Hughes 2002) cell lines and peripheral blood mononuclear cells from diabetic patients (Hofmann et al 1998(Hofmann et al , 1999. We therefore hypothesized that -LA inhibits osteoclast formation by suppressing NF-B activation.…”

Section: Discussionmentioning

confidence: 98%

α-Lipoic acid suppresses osteoclastogenesis despite increasing the receptor activator of nuclear factor κB ligand/osteoprotegerin ratio in human bone marrow stromal cells

Koh

Lee²,

Byun³

et al. 2005

Journal of Endocrinology

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Growing evidence has shown a biochemical link between increased oxidative stress and reduced bone density. Although -lipoic acid ( -LA) has been shown to act as a thiol antioxidant, its effect on bone cells has not been determined. Using proteomic analysis, we identified six differentially expressed proteins in the conditioned media of -LA-treated human bone marrow stromal cell line (HS-5). One of these proteins, receptor activator of nuclear factor B ligand (RANKL), was significantly up-regulated, as confirmed by immunoblotting with anti-RANKL antibody. ELISA showed that -LA stimulated RANKL production in cellular extracts (membranous RANKL) about 5-fold and in conditioned medium (soluble RANKL) about 23-fold, but had no effect on osteoprotegerin (OPG) secretion. Despite increasing the RANKL/OPG ratio, -LA showed a dose-dependent suppression of osteoclastogenesis, both in a coculture system of mouse bone marrow cells and osteoblasts and in a mouse bone marrow cell culture system, and reduced bone resorption in a dose-dependent manner. In addition, -LA-induced soluble RANKL was not inhibited by matrix metalloprotease inhibitors, indicating that soluble RANKL is produced by -LA without any posttranslational processing. In contrast, -LA had no significant effect on the proliferation and differentiation of HS-5 cells. These results suggest that -LA suppresses osteoclastogenesis by directly inhibiting RANKL-RANK mediated signals, not by mediating cellular RANKL production. In addition, our findings indicate that -LA-induced soluble RANKL is not produced by shedding of membranous RANKL.

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“…Glycosylation also causes proteins to acquire functions that they normally do not possess by binding to receptors for AGEs on cell surfaces. For example, glycosylation of collagen and albumin confers signalling properties to these molecules so that they then possess pro-inflammatory and pro-apoptotic activity (50,(59)(60)(61)(62) AGEs also have the capacity to stimulate migration of mononuclear phagocytes (63,64). Blockage of RAGE in diabetic mice reduces TNF-alpha and IL-6 production and decreases activity of matrix metalloproteinases which degrade extracellular matrix proteins (22,65).…”

Section: Advanced Glycation Endproductsmentioning

confidence: 99%

Diabetic complications and dysregulated innate immunity

Graves

Kayal²

2008

Front Biosci

225

188

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Diabetes mellitus is a metabolic disorder that leads to the development of a number of complications. The etiology of each diabetic complication is undoubtedly multifactorial. We will focus on one potential component that may be common in many diabetic complications, dysregulation of innate immunity associated with an increased inflammatory response. High glucose levels lead to shunting through the polyol pathway, an increase in diacylglycerol which activates protein kinase C, an increase in the release of electrons that react with oxygen molecules to form superoxides, and the non-enzymatic glycosylation of proteins that result in greater formation of advanced glycation end products. Each of these can lead to aberrant cell signalling that affects innate immunity for example, by activating the MAP kinase pathway or inducing activation of transcription factors such as NF-kappaB. This may be a common feature of several complications including periodontal disease, atherosclerosis, nephropathy, impaired healing and retinopathy. These complications are frequently associated with increased expression of inflammatory cytokines such as TNF-alpha, IL-1beta and IL-6 and enhanced generation of reactive oxygen species. Cause and effect relationship between dysregulation of key components of innate immunity and diabetic complications in many instances have been demonstrated with the use of cytokine blockers and antioxidants.

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Glycated albumin increases oxidative stress, activates NF-κB and extracellular signal-regulated kinase (ERK), and stimulates ERK-dependent transforming growth factor-β1 production in macrophage RAW cells

Cited by 101 publications

References 56 publications

Albumin-stimulated DNA synthesis is mediated by Ca²⁺/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

Albumin-stimulated DNA synthesis is mediated by Ca²⁺/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

α-Lipoic acid suppresses osteoclastogenesis despite increasing the receptor activator of nuclear factor κB ligand/osteoprotegerin ratio in human bone marrow stromal cells

Diabetic complications and dysregulated innate immunity

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Glycated albumin increases oxidative stress, activates NF-κB and extracellular signal-regulated kinase (ERK), and stimulates ERK-dependent transforming growth factor-β1 production in macrophage RAW cells

Cited by 101 publications

References 56 publications

Albumin-stimulated DNA synthesis is mediated by Ca2+/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

Albumin-stimulated DNA synthesis is mediated by Ca2+/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

α-Lipoic acid suppresses osteoclastogenesis despite increasing the receptor activator of nuclear factor κB ligand/osteoprotegerin ratio in human bone marrow stromal cells

Diabetic complications and dysregulated innate immunity

Contact Info

Product

Resources

About

Albumin-stimulated DNA synthesis is mediated by Ca²⁺/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells

Albumin-stimulated DNA synthesis is mediated by Ca²⁺/PKC as well as EGF receptor-dependent p44/42 MAPK and NF-κB signal pathways in renal proximal tubule cells