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glomerulonephritis/phosphatase

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The mesangial cell provides structural support to the kidney glomerulus. A polymerase chain reaction-based cDNA display approach identified a novel protein-tyrosine phosphatase, rPTP-GMC1, whose transcript expression is transiently and dramatically up-regulated during the period of mesangial cell

Oxidative stress-inducible protein tyrosine phosphatase in glomerulonephritis.

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Previously we found that rat mesangial cells express 3CH134/CL100 protein-tyrosine phosphatase (PTPase) in response to reactive oxygen intermediates (ROIs), and we now extend these studies to glomerulonephritis (GN), where ROI have been demonstrated to play a role. The rat homologue of 3CH134/CL100

Induction of glomerulonephritis in rats with staphylococcal phosphatase: new aspects in post-infectious ICGN.

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Staphylococcal neutral phosphatase (NPtase) is a highly cationic bacterial surface bound protein. It has significant affinity for human and rat immunoglobulins in vitro and an electrostatic interaction may be involved. Radioisotopic studies showed that NPtase had a high affinity for the polyanionic

[Serum and urinary alkaline phosphatase isoenzymes in children, aged 3-14, suffering from acute streptococcal glomerulonephritis].

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[Serum and urinary alkaline phosphatase and its isoenzyme activity in children with submicroscopical glomerulonephritis].

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BACKGROUND There is increasing evidence that some organ-specific and generalized autoimmune diseases in humans might be related to a breakdown of oral tolerance. We explored this hypothesis in human primary glomerulonephritides. We prospectively counted intraepithelial T lymphocytes in the duodenal
Chronic glomerulonephritis (CGN) is the most common form of primary glomerular disease. Qi Teng Xiao Zhuo granules have been proposed as a prescription of traditional Chinese medicine (TCM) for treatment of CGN, however,the comprehensive molecular mechanism underlying this therapeutic

Changes in lysosome populations in the rat kidney cortex induced by passive Heymann glomerulonephritis.

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Acute passive Heymann glomerulonephritis in rats induced heavy proteinuria and highly increased urinary activity of N-acetyl-beta-D-glucosaminidase, acid beta-galactosidase and acid phosphatase. The cortical activity of these acid hydrolases was increased essentially in the large lysosomes as

Urinary trehalase activity in chronic glomerulonephritis.

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To determine the diagnostic role of urinary trehalase in chronic glomerular disease, urinary trehalase activity and other urinary markers such as N-acetyl-beta-D-glucosaminidase (NAG), alanine aminopeptidase (AAP), alkaline phosphatase (ALP), gamma-glutamyltranspeptidase (gamma-GTP), lactate

The role of mammalian target of rapamycin pathway in the pathogenesis of pauci-immune glomerulonephritis.

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Background: The characteristic lesion of pauci-immune glomerulonephritis is focal necrotizing and crescentic glomerulonephritis. The underlying mechanisms in the formation or progression of crescent formation need further investigations. Therefore, we aimed to evaluate the role of mammalian
Kidney biopsy specimens obtained from a group of individuals with chronic glomerulonephritis (CGN) have been processed for light and electron microscopic immunolocalization of total immunoglobulins (Igs). In a few cases, acid phosphatase (ACPase), a lysosomal enzyme marker, was ultrastructurally

Urinary lactic dehydrogenase, alkaline phosphatase and lysozyme studies in renal disease.

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Urinary lactic dehydrogenase, alkaline phosphatase and lysozyme determinations were performed on 70 patients with various kidney diseases such as acute and chronic pyelonephritis, acute and chronic glomerulonephritis, idiopathic nephrotic syndrome, diabetic nephropathy, nephrosclerosis, lupus
PTPRQ (rPTP-GMC1) is a member of the type III receptor-like protein tyrosine phosphatase family. PTPRQ has very low activity against phosphotyrosine but is active against phosphatidylinositol phosphates that are involved in regulation of survival, proliferation, and subcellular architecture. Here,
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