The juxtaglomerular apparatus in the normal rat kidney

1978 ◽  
Vol 379 (2) ◽  
pp. 143-150 ◽  
Author(s):  
Jan A. Christensen ◽  
Adalbert Bohle
Keyword(s):  
Rat Kidney ◽  
Juxtaglomerular Apparatus ◽  
Normal Rat

Glucose-6-phosphate dehydrogenase and renin in kidneys of hypertensive or adrenalectomized rats

1959 ◽  
Vol 197 (4) ◽  
pp. 869-872 ◽  
Author(s):  
R. Hess ◽  
F. Gross
Keyword(s):  
Enzymatic Activity ◽  
Rat Kidney ◽  
Juxtaglomerular Apparatus ◽  
Macula Densa ◽  
Sodium Balance ◽  
Normal Rat ◽  
Distal Tubules ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Renin Content ◽  
Intact Rats

Using a histochemical method, moderately strong glucose-6-phosphate dehydrogenase activity can be demonstrated in the macula densa of the distal tubules in the normal rat kidney. In rats rendered hypertensive by overdosage with cortexone (DOC) and saline, this enzymatic activity was found to decrease almost to zero within 4 weeks. This change was more marked in unilaterally nephrectomized animals than in intact rats. Measured by bioassay, the renin content of kidney extracts from the same animals was found to decrease simultaneously with the loss of enzymatic activity in the macula cells. The reverse effect, a marked increase in activity of the macula densa, was obtained in adrenalectomized animals. It is suggested that both the macula densa cells and the juxtaglomerular apparatus are parts of a system which respond similarly to changes in sodium balance and which may be related to the formation of renin.

scholarly journals Effects of hypertonic stress on transforming growth factor-β activity in normal rat kidney cells

1998 ◽  
Vol 53 (6) ◽  
pp. 1654-1660 ◽  
Author(s):  
Toshihiro Sugiura ◽  
Atsushi Yamauchi ◽  
Hiroshi Kitamura ◽  
Yasuko Matusoka ◽  
Masaru Horio ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Rat Kidney ◽  
Transforming Growth Factor Β ◽  
Kidney Cells ◽  
Hypertonic Stress ◽  
Normal Rat

scholarly journals Adhesion-dependent and Contractile Ring-independent Equatorial Furrowing during Cytokinesis in Mammalian Cells

2005 ◽  
Vol 16 (8) ◽  
pp. 3865-3872 ◽  
Author(s):  
Masamitsu Kanada ◽  
Akira Nagasaki ◽  
Taro Q.P. Uyeda
Keyword(s):  
Mammalian Cells ◽  
Rat Kidney ◽  
Myosin Ii ◽  
Rho Kinase ◽  
Cellular Slime Mold ◽  
Animal Cells ◽  
Contractile Ring ◽  
Normal Rat ◽  
Cellular Slime ◽  
Coated Surfaces

Myosin II-dependent contraction of the contractile ring drives equatorial furrowing during cytokinesis in animal cells. Nonetheless, myosin II-null cells of the cellular slime mold Dictyostelium divide efficiently when adhering to substrates by making use of polar traction forces. Here, we show that in the presence of 30 μM blebbistatin, a potent myosin II inhibitor, normal rat kidney (NRK) cells adhering to fibronectin-coated surfaces formed equatorial furrows and divided in a manner strikingly similar to myosin II-null Dictyostelium cells. Such blebbistatin-resistant cytokinesis was absent in partially detached NRK cells and was disrupted in adherent cells if the advance of their polar lamellipodia was disturbed by neighboring cells. Y-27632 (40 μM), which inhibits Rho-kinase, was similar to 30 μM blebbistatin in that it inhibited cytokinesis of partially detached NRK cells but only prolonged furrow ingression in attached cells. In the presence of 100 μM blebbistatin, most NRK cells that initiated anaphase formed tight furrows, although scission never occurred. Adherent HT1080 fibrosarcoma cells also formed equatorial furrows efficiently in the presence of 100 μM blebbistatin. These results provide direct evidence for adhesion-dependent, contractile ring-independent equatorial furrowing in mammalian cells and demonstrate the importance of substrate adhesion for cytokinesis.

scholarly journals DNA microarray analysis of normal rat kidney epithelial cells treated with cadmium

2011 ◽  
Vol 36 (1) ◽  
pp. 127-129 ◽  
Author(s):  
Maki Tokumoto ◽  
Tomoaki Ohtsu ◽  
Akiko Honda ◽  
Yasuyuki Fujiwara ◽  
Hisamitsu Nagase ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Microarray Analysis ◽  
Dna Microarray ◽  
Rat Kidney ◽  
Dna Microarray Analysis ◽  
Normal Rat ◽  
Kidney Epithelial Cells

scholarly journals Tunneling nanotube (TNT)-like structures facilitate a constitutive, actomyosin-dependent exchange of endocytic organelles between normal rat kidney cells☆

2008 ◽  
Vol 314 (20) ◽  
pp. 3669-3683 ◽  
Author(s):  
Steffen Gurke ◽  
João F.V. Barroso ◽  
Erlend Hodneland ◽  
Nickolay V. Bukoreshtliev ◽  
Oliver Schlicker ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Kidney Cells ◽  
Tunneling Nanotube ◽  
Normal Rat

scholarly journals Protective effect of zinc-N-acetylcysteine on the rat kidney during cold storage

2013 ◽  
Vol 305 (7) ◽  
pp. F1022-F1030 ◽  
Author(s):  
Mandeep Singh ◽  
Dolapo T. Odeniyi ◽  
Eugene O. Apostolov ◽  
Alena Savenka ◽  
Todd Fite ◽  
...  
Keyword(s):  
Cell Death ◽  
Dna Fragmentation ◽  
Cold Storage ◽  
Ex Vivo ◽  
Rat Kidney ◽  
Maximum Effect ◽  
Kidney Preservation ◽  
Endonuclease G ◽  
Normal Rat ◽  
Rat Kidneys

Cold storage of kidneys before transplantation is problematic because of the limited survival time of the allografts. In this study, zinc- N-acetylcysteine (ZnNAC) was shown to be a potent endonuclease inhibitor and antioxidant, and it was tested as a potential additive to a cold storage solution for kidney preservation. Exposure of normal rat kidney NRK-52E cells to ZnNAC resulted in zinc delivery to the cells as determined by TFL-Zn fluorophore and partial protection of the cells against injury by cold storage in University of Wisconsin solution (UWS) as measured by propidium iodide assay. Ex vivo, rat kidneys demonstrated time- and temperature-dependent DNA fragmentation as assessed by TUNEL assay, indicating irreversible cell death. DNA fragmentation was faster in the medulla than in the cortex, and tubules were affected more than glomeruli. Perfusion of rat kidneys with cold ZnNAC solution in UWS significantly inhibited cell death both in the cortex and medulla at concentrations of 0.3–30 mM compared with UWS alone, with a maximum effect at 1–10 mM ZnNAC. Cold storage of the kidney significantly increased quantities of cleaved caspase-3 and endonuclease G (EndoG) in the tissue, which were abolished by 10 mM ZnNAC, indicating its ability to suppress both caspase-dependent and -independent cell death. Therefore, supplementation of UWS with ZnNAC can decrease DNA fragmentation and protect kidney allografts from cell death due to cold storage.

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