Possible Biogenesis of the Membrane-Bound Bodies of the Thick Basal Laminae of the Proximal Convoluted Tubule Cells of the Gerbil Meriones crassus

1992 ◽  
Vol 144 (3) ◽  
pp. 225-230 ◽  
Author(s):  
A.M. Safer
Keyword(s):  
Proximal Convoluted Tubule ◽  
Membrane Bound ◽  
Tubule Cells

Abstract 215: Adam17 Regulates Renal Function

Circulation ◽  
2020 ◽  
Vol 142 (Suppl_4) ◽  
Author(s):  
Bo Zhang ◽  
Kai Chen ◽  
Zhongjie Sun
Keyword(s):  
Renal Function ◽  
Kidney Function ◽  
Renal Tubule ◽  
Renal Diseases ◽  
Normal Kidney ◽  
Normal Kidney Function ◽  
Membrane Bound ◽  
Tubule Cells ◽  
A Disintegrin And Metalloproteinase

A disintegrin and metalloproteinase 17 (ADAM17) is a ubiquitously expressed membrane-bound sheddase that cleaves a diverse variety of membrane-bound molecules, including cytokines, growth factors, and their receptors to activate or inactivate various cellular signaling pathways. Although it was reported that ADAM17 may mediate renal diseases, the role of ADAM17 in the regulation of normal kidney function has never been identified. The objective of this study is to investigate whether renal ADAM17 plays a role in maintaining normal kidney function and structure. Tamoxifen-inducible kidney-specific cre (Ksp) and ADAM17-floxed mice were cross-bred for generating Ksp/ADAM17-floxed mice. Injection of tamoxifen initiated deletion of the ADAM17 gene in renal tubule cells. We found that conditional kidney-specific knockout of ADAM1 7 gene (Ksp-ADAM17 -/-) decreased urinary creatinine and sodium excretion were decreased in Ksp-ADAM17 -/- mice, indicating that ADAM17 gene deficiency impairs kidney function. H&E staining showed glomerulus collapse and tubule dilation in Ksp-ADAM17 -/- mice. The epithelial cells fall off into the lumen in the renal tubule. Mesangial expansion and fibrosis were found in glomeruli in Ksp-ADAM17 -/- mice. Moreover, apoptosis was increased in tubule cells in both cortex and medulla areas in Ksp-ADAM17 -/- mice. In conclusion, ADAM17 is critical to the maintenance of normal renal function and structure.

Aminopeptidase N reduces basolateral Na+-K+-ATPase in proximal tubule cells

2007 ◽  
Vol 293 (4) ◽  
pp. F1047-F1053 ◽  
Author(s):  
Kumar Kotlo ◽  
Sagar Shukla ◽  
Urmila Tawar ◽  
Randal A. Skidgel ◽  
Robert S. Danziger
Keyword(s):  
Atpase Activity ◽  
Proximal Tubule ◽  
Aminopeptidase N ◽  
Angiotensin Iv ◽  
Proximal Tubule Cells ◽  
Renal Adaptation ◽  
Membrane Bound ◽  
Tubule Cells ◽  
Trait Locus ◽  
Ang Iv

Aminopeptidase N/CD13 (Anpep) is a membrane-bound protein that catalyzes the formation of natriuretic hexapeptide angiotensin IV (ANG IV) from ANG III. We previously reported that Anpep is more highly expressed in the kidneys of Dahl salt-resistant (SR/Jr) than salt-sensitive (SS/Jr) rats, Anpep maps to a quantitative trait locus for hypertension, and that the Dahl SR/Jr rat contains a functional polymorphism of the gene. This suggests that renal Anpep may be linked to salt sensitivity; however, its effect on renal Na handling has not been determined. Here, we examined regulation of basolateral Na+-K+-ATPase, a preeminent basolateral Na+ transporter in proximal tubule cells, by Anpep in LLC-PK1 cells. Treatment of the cells with Anpep siRNA increased total cellular Na+-K+-ATPase activity and basolateral Na+-K+-ATPase abundance by approximately twofold. Conversely, Anpep overexpression reduced Na+-K+-ATPase activity and basolateral abundance by ∼50%. Similar effects were observed after treatment with ANG IV (10 nM, ×30 min and 12 h). ANG IV receptor (AGTRIV) knockdown via specific siRNA relieved the decreases in basolateral Na+-K+-ATPase levels and activity induced by Anpep overexpression. In sum, these results demonstrate that Anpep reduces basolateral Na+-K+-ATPase levels via ANG IV/AGTRIV signaling. This novel pathway may be important in renal adaptation to high salt.

scholarly journals Protein kinase A induces recruitment of active Na+,K+-ATPase units to the plasma membrane of rat proximal convoluted tubule cells

1998 ◽  
Vol 511 (1) ◽  
pp. 235-243 ◽  
Author(s):  
Maria Luisa Carranza ◽  
Martine Rousselot ◽  
Alexander V. Chibalin ◽  
Alejandro M. Bertorello ◽  
Hervé Favre ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Proximal Convoluted Tubule ◽  
Tubule Cells ◽  
Kinase A

Experiments on Fixation for Electron Microscopy

1963 ◽  
Vol s3-104 (65) ◽  
pp. 123-127
Author(s):  
S. K. MALHOTRA
Keyword(s):  
Electron Microscopy ◽  
Acetic Acid ◽  
Osmium Tetroxide ◽  
Proximal Convoluted Tubule ◽  
Mitochondrial Matrix ◽  
Zymogen Granules ◽  
Exocrine Cells ◽  
Acid Ph ◽  
Pancreatic Exocrine ◽  
Tubule Cells

The effect of fixation with acidified solutions of osmium tetroxide (pH 1.5 to 3.5 has been studied on the first (proximal) convoluted tubule cells of the kidney and the pancreatic exocrine cells of the mouse, by electron microscopy. Partially prepolymerized methacrylate was used for embedding. The various membranous structures and the ribosomes retain their individuality even after prolonged fixation in solutions containing 5% acetic acid (pH 1.5). However, the mitochondrial matrix and the ground cytoplasm are not preserved; the zymogen granules are also partially washed out.

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