Effects of combination therapy with angiotensin II type I receptor blockers and calcium channel blockers on renal function in hypertensive patients/a retrospective, "real-world" comparative study.

Background: Combination therapies with angiotensin II type I receptor blockers (ARBs) and calcium channel blockers (CCBs) are frequently administered to hypertensive patients, because these regimens have renoprotective and antihypertensive effects. However, few studies have focused on the renoprotective effects of individual CCBs when combined with ARBs for hypertension.

Methods: Two hundred eighty-six outpatients prescribed three different CCBs (benidipine [CAS 91599-74-5], amlodipine [CAS 111470-99-6] and controlled release nifedipine (nifedipine CR) [CAS 21829-25-4]) for hypertension in combination with ARBs during a 4-year period were registered in a retrospective comparative study.

NO-1886 (ibrolipim), a lipoprotein lipase activator, increases the expression of uncoupling protein 3 in skeletal muscle and suppresses fat accumulation in high-fat diet-induced obesity in rats.

Although the lipoprotein lipase (LPL) activator NO-1886 shows antiobesity effects in high-fat-induced obese animals, the mechanism remains unclear. To clarify the mechanism, we studied the effects of NO-1886 on the expression of uncoupling protein (UCP) 1, UCP2, and UCP3 in rats. NO-1886 was mixed with a high-fat chow to supply a dose of 100 mg/kg to 8-month-old male Sprague-Dawley rats.

The increase of antiglomerular basement membrane antibody following pauci-immune-type crescentic glomerulonephritis.

A 50-year-old woman was admitted because of high fever and fatigue. Proteinuria, hematuria, and elevated BUN (47.8 mg/dl) and creatinine (3.

[Extracellular-superoxide dismutase production in mesangial cell growing in extracellular matrix].

To study the protective function against oxygen radicals in the mesangial area, we assessed extracellular superoxide dismutase (EC-SOD) production in mesangial cells (MCs) in vitro. These cells have a major protective function against oxygen radicals in the extracellular space. In two different kinds of culture conditions: "growth medium" with fetal cow serum, and "differentiation medium" with reduced growth factor, and four extracellular matrixes; type I collagen, type IV collagen, laminin and fibronectin, were added to the MC culture.

Establishment of anti-rat-Cu,Zn-superoxide dismutase monoclonal antibodies applied to a highly sensitive immunoassay and immunohistochemistry system.

The superoxide anion has been implicated in a wide range of diseases. The major protector against superoxide anion in the cell cytosol is Cu,Zn-superoxide dismutase (Cu,Zn-SOD). In this study, anti rat Cu,Zn-SOD was established in murine monoclonal antibodies for the first time.

Extracellular superoxide dismutase and glomerular mesangial cells: its production and regulation.

Extracellular superoxide dismutase (EC-SOD) is synthesized in mesenchymally derived cells and prevents the oxygen radical-induced injury. We studied whether kidney mesangial cells (MCs) produce EC-SOD and how its production is associated with chemokine secretion. Under unstimulated condition, MCs produced EC-SOD, and its production was correlated positively with cyclic adenosine monophosphate (cAMP), but negatively with interleukin (IL)-6 or IL-8 production.

Heparin-stimulated expression of extracellular-superoxide dismutase in human fibroblasts.

Extracellular-superoxide dismutase (EC-SOD) is the major SOD isozyme in the arterial wall and may be important for antioxidation capability of the vascular wall and normal vascular function. EC-SOD is expressed in various cell types in the vascular wall such as fibroblasts, smooth muscle cells and macrophages, and the synthesis of EC-SOD by human fibroblasts is known to be highly responsive to various inflammatory cytokines, although there is no response to oxidative stress. Heparin is a highly sulfated glycosaminoglycan with many functions such as antithrombotic, antilipemic and antiatherosclerotic effects.

Protective role of extracellular superoxide dismutase in hemodialysis patients.

Background: The superoxide anion and other oxygen radicals have been implicated in the progression of chronic renal failure, and are removed by extracellular superoxide dismutase (EC-SOD) in the extracellular space on the surface of the endothelium. A single-base substitution of the EC-SOD gene which reduces the binding capability to endothelial cells resulting in an increased serum concentration, has been identified in healthy persons and hemodialysis patients.

Results: The proportion of patients with this mutation among hemodialysis patients in each 20 months' duration after the initiation of hemodialysis was retrospectively studied.

Increase of urinary extracellular-superoxide dismutase level correlated with cyclic adenosine monophosphate.

Extracellular superoxide dismutase (EC-SOD) is a secretory protein that is the major SOD isozyme in extracellular fluids. Plasma EC-SOD levels are distributed in two discrete groups with the rare group having an enzyme with glycine instead of arginine-213, which causes a 10-fold higher serum level. Within the common phenotype group, the urinary EC-SOD level was significantly correlated with the urinary excretion of N-acetyl-beta-D-glucosaminidase (NAG), but not with serum EC-SOD.

Polymorphism of extracellular superoxide dismutase (EC-SOD) gene: relation to the mutation responsible for high EC-SOD level in serum.

Extracellular superoxide dismutase (EC-SOD) with amino acid substitution R213G generated by the nucleotide substitution 760C-->G in the heparin binding domain is responsible for the high EC-SOD level in serum. We identified the two DNA polymorphic sites in the coding region of EC-SOD gene related to the 760C-->G and determined the allele frequencies. The polymorphism were A and G at nucleotide position (nt.

An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases.

Molecular genetic studies of extracellular-superoxide dismutase (EC-SOD) have shown that individuals with high serum EC-SOD content have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of this enzyme [Sandström, J. et al. (1994) J.

Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface.

Extracellular-superoxide dismutase (EC-SOD) levels in sera divide into two discontinuous groups: a low-level group below 400 ng/ml and a high-level group above 400 ng/ml [Adachi, Nakamura, Yamada, Futenma, Kato and Hirano (1994) Clin. Chim. Acta 229, 123-131].

The protective effect of probucol on adriamycin nephrosis in the rat.

Recent research has indicated the role of reactive oxygen species (ROS) in experimental nephritis. We examined the role of ROS and the effect of probucol, an anti-hyperlipidemic drug with antioxidant activity, on adriamycin (ADR)-induced nephrosis in the rat. Fourteen days after single intravenous injection of ADR (7.

Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum.

Extracellular-superoxide dismutase (EC-SOD) is one of the SOD isozymes mainly distributed in the extracellular fluid. In the vascular system, it is located on the endothelial cell surface according to studies on the heparin binding capacity. By measurement of serum EC-SOD levels of Japanese in healthy persons (n = 103) and hemodialysis patients (n = 150), 7 healthy subjects and 24 hemodialysis patients were classified into group II associated with high EC-SOD levels.

Heparin-induced release of extracellular-superoxide dismutase form (V) to plasma.

Extracellular-superoxide dismutase [EC 1.15.1.

[Distribution of glutathione peroxidase in the glomeruli of IgA nephropathy].

To study the role of reactive oxygen species in chronic renal disease, we studied the location of Glutathione peroxidase (GSH-Px) in glomeruli of patients with IgA nephropathy. In normal kidney, GSH-Px was localized in tubular cells, and not in glomeruli. In the kidney with IgA nephropathy, GSH-Px was detected in glomerular cells in addition to the tubular cells.

Quantitative and qualitative changes of extracellular-superoxide dismutase in patients with various diseases.

Extracellular-superoxide dismutase (EC-SOD) is a secretory glycoprotein that is the major SOD isozyme in extracellular fluids. It has previously been shown that EC-SOD levels in sera from healthy persons are clearly divided into two discontinuous groups: a lower group (named Group I, below 120 ng/ml) and a higher group (Group II, above 400 ng/ml). The family studies have shown that the high EC-SOD level in healthy persons is genetically transmitted.

Expression of interleukin 6 and major histocompatibility complex molecules in tubular epithelial cells of diseased human kidneys.

Background: Interleukin-6 (IL-6) exerts multiple effects on infiltrated inflammatory cells and on structural cells in tissues. We previously reported that IL-6 expression is increased in the area of glomerular and tubular inflammation and tubular atrophy (Lab Invest 65:61, 1991). In the present study, we investigated the expression of IL-6 and HLA molecules in the tubules of patients with renal diseases, and correlate it with the morphological findings.

Plasma levels of superoxide dismutase and its isomers in patients with chronic renal disease.

To evaluate the significance of Cu,Zn-superoxide dismutase (SOD) in chronic renal disease, we evaluated the plasma SOD activity and analyzed the plasma Cu,Zn-SOD isomers employing gel column chromatography. The plasma SOD activity was determined as the biological activity using the nitrite method and the Cu,Zn-SOD concentration was assayed from the immunological activity using enzyme-linked immunosorbent assay (ELISA). The subjects comprised 185 patients with chronic glomerular disease and 20 hemodialysis patients.

Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody.

The superoxide anion has been implicated in a wide range of diseases. The major protector against superoxide anion in the extracellular space is extracellular-superoxide dismutase (EC-SOD). EC-SOD is the major SOD isozyme in plasma and forms an equilibrium between the plasma phase and heparan sulfate proteoglycan on the surface of the endothelium.