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nephrosis/tyrosine

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Decreased tyrosine phosphorylation of nephrin in rat and human nephrosis.

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Phosphorylation of tyrosine residue (Y1204) of rat nephrin by Fyn kinase allows Nck adaptor protein binding to nephrin motifs, which include the phosphorylated tyrosine. This phosphorylation-dependent switch induces actin polymerization in a cell culture system. Here, we generated an antibody

GLEPP1 receptor tyrosine phosphatase (Ptpro) in rat PAN nephrosis. A marker of acute podocyte injury.

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Glomerular epithelial protein 1 (GLEPP1) is a podocyte receptor membrane protein tyrosine phosphatase located on the apical cell membrane of visceral glomerular epithelial cell and foot processes. This receptor plays a role in regulating the structure and function of podocyte foot process. To better

Clustering-induced tyrosine phosphorylation of nephrin by Src family kinases.

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BACKGROUND Nephrin is a recently discovered protein of the immunoglobulin (Ig) superfamily. In the kidney, it is located at the slit diaphragm, which forms the decisive size-selective filter of glomerular ultrafiltration barrier and locates between the interdigitating foot processes of podocytes.
In most forms of glomerular diseases, loss of size selectivity by the kidney filtration barrier is associated with changes in the morphology of podocytes. The kidney filtration barrier is comprised of the endothelial lining, the glomerular basement membrane, and the podocyte intercellular junction,

Podocyte Protein, Nephrin, Is a Substrate of Protein Tyrosine Phosphatase 1B.

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Glomerular podocytes are critical for the barrier function of the glomerulus in the kidney and their dysfunction causes protein leakage into the urine (proteinuria). Nephrin is a key podocyte protein, which regulates the actin cytoskeleton via tyrosine phosphorylation of its cytoplasmic domain. Here

Arginine augments neither albuminuria nor albumin synthesis caused by high-protein diets in nephrosis.

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Dietary protein independently modulates albuminuria (U(Alb)V) and albumin synthesis (AlbSyn) in nephrotic rats. While some amino acids are without effect on renal hemodynamics, arginine (Arg) augments renal blood flow and glomerular filtration rate, increases AlbSyn in tissue culture and isolated
Glomerulosclerosis correlates with a reduction in podocyte number that occurs through mechanisms that include apoptosis. Whether glial cell line-derived neurotrophic factor (GDNF), a growth factor that is critical for neural and renal development, is a survival factor for injured podocytes was

[Molecular dynamics of proteins found exclusively in glomerular epithelial cells].

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The visceral glomerular epithelial cells or podocytes of the renal glomerulus are uniquely characterized by a large cell body and numerous foot processes. These foot processes are kept wide open to facilitate passage of glomerular filtrate and are held together tenuous slit diaphragms that bridge

Early changes in gene expression that influence the course of primary glomerular disease.

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Serial changes in glomerular capillary loop gene expression were used to uncover mechanisms contributing to primary glomerular disease in rat models of passive Heymann nephritis and puromycin nephrosis. Before the onset of proteinuria, podocyte protein-tyrosine phosphatase (GLEPP1) expression was

p21-activated kinases regulate actin remodeling in glomerular podocytes.

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The tyrosine phosphorylation of nephrin is reported to regulate podocyte morphology via the Nck adaptor proteins. The Pak family of kinases are regulators of the actin cytoskeleton and are recruited to the plasma membrane via Nck. Here, we investigated the role of Pak in podocyte morphology. Pak1/2

Cortactin interacts with podocalyxin and mediates morphological change of podocytes through its phosphorylation.

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OBJECTIVE Morphological change of podocytes is closely correlated with the development of proteinuria. Podocalyxin is a major sialoglycoprotein of the podocytes and is thought to be involved in the maintenance of the foot processes structure. Our aim was to examine the mechanism by which podocalyxin

Connecting the interpodocyte slit diaphragm and actin dynamics: Emerging role for the nephrin signaling complex.

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Uchida et al. show in this issue that in rat and human nephrosis, tyrosine phosphorylation of nephrin is reduced, and this is accompanied by a decrease in F-actin in glomeruli. This, together with previous studies, suggests that the nephrin protein complex is a signaling nexus that regulates actin

[Mutation of hepatitis B virus S gene in children with hepatitis B virus-associated glomerulonephritis].

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OBJECTIVE Hepatitis B virus-associated glomerulonephritis (HBV-GN) is an immune complex-mediated glomerulonephritis. The present study was conducted to identify HBV S gene mutation in children with HBV-GN. METHODS Serum HBV DNA was extracted in 53 children, including 30 with HBV-GN, 5 with

S gene mutations of HBV in children with HBV-associated glomerulonephritis.

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BACKGROUND Hepatitis B virus-associated glomerulonephritis (HBV-GN) is a kind of immune complex-induced glomerulonephritis. The present study was designed to determine whether mutation of Hepatitis B virus (HBV) S gene is associated with glomerulonephritis in Chinese children. METHODS Total 53

The adaptor protein Grb2 is not essential for the establishment of the glomerular filtration barrier.

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The kidney filtration barrier is formed by the combination of endothelial cells, basement membrane and epithelial cells called podocytes. These specialized actin-rich cells form long and dynamic protrusions, the foot processes, which surround glomerular capillaries and are connected by specialized
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