Glucose-induced oxidative stress in mesangial cells

Catherwood, Mark; Powell, Lesley; Anderson, Paul; McMaster, Dorothy; Sharpe, Peter; Trimble, Elisabeth R.

doi:10.1046/j.1523-1755.2002.00168.x

Cited by 161 publications

(128 citation statements)

References 59 publications

(3 reference statements)

Supporting

Mentioning

114

Contrasting

Unclassified

Order By: Relevance

“…Our previous findings (19) suggest that this downregulation of Mn-SOD with salt loading may be a consequence of a reduction in Ang II, but this was not tested in the present study. ROS activate mitogen-activated protein kinase in renal tubule cells (38), contribute to hypertrophic responses to Ang II (38) and to cellular injury (39), and increase fibrogenic matrix protein synthesis in mesangial cells (40). A high salt intake enhances oxidative stress in rat skeletal muscle arterioles and vessels (23) and increases BP, protein excretion, and renal fibrosis and worsens renal function in several models of chronic renal failure (7,38,(41)(42)(43) and accelerates the decline of renal function in patients with chronic renal failure (44).…”

Section: Discussionmentioning

confidence: 99%

Salt Intake, Oxidative Stress, and Renal Expression of NADPH Oxidase and Superoxide Dismutase

Kitiyakara

Chabrashvili²,

Chen³

et al. 2003

Journal of the American Society of Nephrology

280

236

View full text Add to dashboard Cite

Abstract. The hypothesis that a high salt (HS) intake increases oxidative stress was investigated and was related to renal cortical expression of NAD(P)H oxidase and superoxide dismutase (SOD). 8-Isoprostane PGF 2␣ and malonyldialdehyde were measured in groups (n ϭ 6 to 8) of conscious rats during low-salt, normal-salt, or HS diets. NADPH-and NADH-stimulated superoxide anion (O 2 ·Ϫ ) generation was assessed by chemiluminescence, and expression of NAD(P)H oxidase and SOD were assessed with real-time PCR. Excretion of 8-isoprostane and malonyldialdehyde increased incrementally twoto threefold with salt intake (P Ͻ 0.001), whereas prostaglandin E 2 was unchanged. Renal cortical NADH-and NADPHstimulable O 2 ·Ϫ generation increased (P Ͻ 0.05) 30 to 40% with salt intake. Compared with low-salt diet, HS significantly (P Ͻ 0.005) increased renal cortical mRNA expression of gp91 phox and p47 phox and decreased expression of intracellular CuZn (IC)-SOD and mitochondrial (Mn)-SOD. Despite suppression of the renin-angiotensin system, salt loading enhances oxidative stress. This is accompanied by increased renal cortical NADH and NADPH oxidase activity and increased expression of gp91 phox and p47 phox and decreased IC-and Mn-SOD. Thus, salt intake enhances generation of O 2 ·Ϫ accompanied by enhanced renal expression and activity of NAD(P)H oxidase with diminished renal expression of IC-and Mn-SOD.

show abstract

Section: Discussionmentioning

confidence: 99%

Salt Intake, Oxidative Stress, and Renal Expression of NADPH Oxidase and Superoxide Dismutase

Kitiyakara

Chabrashvili²,

Chen³

et al. 2003

Journal of the American Society of Nephrology

280

236

View full text Add to dashboard Cite

show abstract

“…The latter finding is similar to the effect of IL-1␤ up-regulation of GCLC expression that we observed. Long term exposure to high glucose conditions decreases GCLC expression in mesangial as well as retinal Muller cells resulting in a decrease in GSH levels (4,5). Decreased GSH levels in erythrocytes from hyperglycemic type 2 diabetics are also accompanied by a decrease in GCLC activity (13).…”

Section: Discussionmentioning

confidence: 99%

“…The regulation of GCL expression and activity has been studied in many other cell types, including mesangial and endothelial cells, but not the pancreatic islet. Long term exposure to high glucose levels decreases GCL expression in mesangial, retinal Muller, and endothelial cells, which results in a decrease in GSH levels (3)(4)(5). Long term exposure to high glucose conditions inhibits endothelial cells from responding to cytokine exposure with an increase in GCL expression and activity (3).…”

mentioning

confidence: 99%

Adenoviral Overexpression of the Glutamylcysteine Ligase Catalytic Subunit Protects Pancreatic Islets against Oxidative Stress

Tran

Parker

Leroy

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

The catalytic subunit of glutamylcysteine ligase (GCLC) primarily regulates de novo synthesis of glutathione (GSH) in mammalian cells and is central to the antioxidant capacity of the cell. However, GCLC expression in pancreatic islets has not been previously examined. We designed experiments to ascertain whether GCLC is normally expressed in islets and whether it is up-regulated by interleukin-1␤ (IL-1␤). GCLC expression levels were intermediate compared with other metabolic tissues (kidney, liver, muscle, fat, and lung). IL-1␤ up-regulated GCLC expression (10 ng/ml IL-1␤, 3.76 ؎ 0.86; 100 ng/ml IL-1␤, 4.22 ؎ 0.68-fold control) via the p38 form of mitogen-activated protein kinase and NF B and also increased reactive oxygen species levels (10 ng/ml IL-1␤, 5.41 ؎ 1.8-fold control). This was accompanied by an increase in intraislet GSH/GSSG ratio (control, 7.1 ؎ 0.1; 10 ng/ml IL-1␤, 8.0 ؎ 0.5; 100 ng/ml IL-1␤, 8.2 ؎ 0.5-fold control; p < 0.05). To determine whether overexpression of GCLC increases the antioxidant capacity of the islet and prevents the adverse effects of IL-1␤ on glucose-induced insulin secretion, islets were infected with an adenovirus encoding GCLC. IL-1␤ significantly decreased glucose-stimulated insulin secretion (control, 123.8 ؎ 17.7; IL-1␤, 40.2 ؎ 3.9 microunits/ml insulin/islet). GCLC overexpression increased intraislet GSH levels and partially prevented the decrease in glucose-stimulated insulin secretion caused by IL-1␤. These data provide the first report of GCLC expression in the islet and demonstrate that adenoviral overexpression of GCLC increases intracellular GSH levels and protects the beta cell from the adverse effects of IL-1␤.Glutamylcysteine ligase (GCL) 1 is the primary and ratelimiting enzyme responsible for de novo synthesis of intracellular glutathione (GSH). This enzyme catalyzes ATP-dependent ligation of L-glutamate and L-cysteine to form ␥-glutamyl-L-cysteine, which undergoes another ATP-dependent ligation with glycine catalyzed by glutathione synthetase to form the final GSH product (1, 2). GCL is a heterodimer, composed of a light regulatory subunit as well as a heavy catalytic subunit. Although both are required for optimal enzyme activity, overexpression of the catalytic subunit GCLC alone is sufficient to increase enzyme activity significantly over control levels (1). The regulation of GCL expression and activity has been studied in many other cell types, including mesangial and endothelial cells, but not the pancreatic islet. Long term exposure to high glucose levels decreases GCL expression in mesangial, retinal Muller, and endothelial cells, which results in a decrease in GSH levels (3-5). Long term exposure to high glucose conditions inhibits endothelial cells from responding to cytokine exposure with an increase in GCL expression and activity (3). That the pathogenesis of diabetes mellitus involves interactions with IL-1␤ and oxidative stress secondary to chronic hyperglycemia (6, 7) raises the questions of whether GCL is normally expressed in the islet and whe...

show abstract

“…Reactive oxygen species have been implicated in the response of mesangial cells to hyperglycemia (38) and increased levels of prostaglandins are characteristic of diabetic and other glomerulopathies (39,40). The role of PLA 2 s in the generation of eicosanoids and propagation of inflammation has been extensively studied by several groups using mesangial cells derived from rats.…”

mentioning

confidence: 99%

Cross-talk between Cytosolic Phospholipase A2α (cPLA2α) and Secretory Phospholipase A2 (sPLA2) in Hydrogen Peroxide-induced Arachidonic Acid Release in Murine Mesangial Cells

Han¹,

Sapirstein

Hung³

et al. 2003

Journal of Biological Chemistry

144

111

View full text Add to dashboard Cite

Glucose-induced oxidative stress in mesangial cells

Cited by 161 publications

References 59 publications

Salt Intake, Oxidative Stress, and Renal Expression of NADPH Oxidase and Superoxide Dismutase

Salt Intake, Oxidative Stress, and Renal Expression of NADPH Oxidase and Superoxide Dismutase

Adenoviral Overexpression of the Glutamylcysteine Ligase Catalytic Subunit Protects Pancreatic Islets against Oxidative Stress

Cross-talk between Cytosolic Phospholipase A2α (cPLA2α) and Secretory Phospholipase A2 (sPLA2) in Hydrogen Peroxide-induced Arachidonic Acid Release in Murine Mesangial Cells

Contact Info

Product

Resources

About