Electron microscopic cytochemical localization of?-hydroxyacid oxidase in rat kidney cortex

1986 ◽  
Vol 85 (5) ◽  
pp. 411-418 ◽  
Author(s):  
S. Angerm�ller ◽  
C. Leupold ◽  
K. Zaar ◽  
H. D. Fahimi
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Electron Microscopic ◽  
Cytochemical Localization ◽  
Rat Kidney Cortex

scholarly journals ULTRASTRUCTURE OF ISOLATED KIDNEY MITOCHONDRIA TREATED WITH PHLORIZIN AND ATP

1964 ◽  
Vol 23 (2) ◽  
pp. 207-215 ◽  
Author(s):  
Mario H. Burgos ◽  
Agustin Aoki ◽  
Fabio L. Sacerdote
Keyword(s):  
Rat Kidney ◽  
Heterogeneous Population ◽  
Kidney Cortex ◽  
Mitochondrial Membranes ◽  
Electron Microscopic ◽  
Isolated Kidney ◽  
Rat Kidney Cortex ◽  
Kidney Mitochondria ◽  
Isolated Mitochondria ◽  
The Matrix

Direct electron microscopic evidence is reported of the ultrastructure of mitochondrial membranes and compartments in mitochondria isolated in 0.5 M sucrose from the rat kidney cortex and the experimental changes they undergo with phlorizin and ATP treatment. A heterogeneous population of mitochondria is recognized under control conditions. The mitochondria appear to be of 3 main types, normal, swollen, and contracted. Under phlorizin treatment, most of the mitochondria swell in less than 15 minutes, apparently at the expense of the matrix. Treatment with ATP, on the other hand, produces, during the same time, a marked contraction of the isolated mitochondria, with many refoldings of the inner membrane and marked increase in the electron opacity of the matrix. It is concluded from these observations that mitochondrial swelling and contraction should be related mainly to the matrix content.

Light and electron microscopic characterization of the proliferative response induced by tobramycin in rat kidney cortex

1988 ◽  
Vol 48 (3) ◽  
pp. 335-352 ◽  
Author(s):  
D. Nonclercq ◽  
G. Toubeau ◽  
G. Laurent ◽  
P. Maldague ◽  
P.M. Tulkens ◽  
...  
Keyword(s):  
Proliferative Response ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Electron Microscopic ◽  
Rat Kidney Cortex

Ultracytochemical Localization of Aryl Sulfatase, Esterase, and Acid and Alkaline Phosphatases with 4-Nitrocatechol Substrates and Tetrazolium Salts

1974 ◽  
Vol 32 ◽  
pp. 226-227
Author(s):  
W. Allen Shannon ◽  
Yoshinobu Hoshino ◽  
Hannah L. Wasserkrug ◽  
Arnold M. Seligman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Alkaline Phosphatases ◽  
Cytochemical Localization ◽  
Rat Kidney Cortex ◽  
Aryl Sulfatase ◽  
Tetrazolium Salts

The ultra cytochemical localization of various hydrolases, i. e, aryl sulfatase(ArS), esterase (Est), acid phosphatase(AcP) and alkaline phosphatase (A1P) is demonstrated in rat kidney cortex with newly developed 4-nitrocatechol substrates (2-hydroxy-5-nitrophenyl compounds) (Fig. 1) and tetrazolium salts, Nitro-BT, BSPT, and BPPT. ArS was also investigated in adrenal cortex.

scholarly journals Increase of Na/Pi-cotransport encoding mRNA in response to low Pi diet in rat kidney cortex.

1994 ◽  
Vol 269 (9) ◽  
pp. 6637-6639
Author(s):  
A. Werner ◽  
S.A. Kempson ◽  
J. Biber ◽  
H. Murer
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Cytochrome P-450K of rat kidney cortex microsomes: Further studies on its interaction with fatty acids

1973 ◽  
Vol 158 (2) ◽  
pp. 597-604 ◽  
Author(s):  
Åke Ellin ◽  
Sten Orrenius ◽  
Åke Pilotti ◽  
Carl-Gunnar Swahn
Keyword(s):  
Fatty Acids ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

scholarly journals Studies on the orientation of brush-border membrane vesicles

1978 ◽  
Vol 172 (1) ◽  
pp. 57-62 ◽  
Author(s):  
W Haase ◽  
A Schäfer ◽  
H Murer ◽  
R Kinne
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Freeze Fracture ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Immunological Methods ◽  
Kidney Cortex ◽  
Asymmetric Distribution ◽  
Rat Kidney Cortex

Orientation of rat renal and intestinal brush-border membrane vesicles was studied with two independent methods: electron-microscopic freeze-fracture technique and immunological methods. With the freeze-fracture technique a distinct asymmetric distribution of particles on the two membrane fracture faces was demonstrated; this was used as a criterion for orientation of the isolated membrane vesicles. For the immunological approach the accessibility or inaccessibility of aminopeptidase M localized on the outer surface of the cell membrane to antibodies was used. With both methods we showed that the brush-border membrane vesicles isolated from rat kidney cortex and from rat small intestine for transport studies are predominantly orientated right-side out.

Endogenous Kallikrein Inhibitor in Rat Kidney Cortex-Effect of Glucocorticoid Administration

1986 ◽  
pp. 361-365 ◽  
Author(s):  
Kodo Ito ◽  
Kenichi Yamada ◽  
Setsuko Yoshida ◽  
Keiji Hasunuma ◽  
Yasushi Tamura ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Kallikrein Inhibitor ◽  
Glucocorticoid Administration

Identification of an apical \batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(\mathrm{Cl}^{-}{/}\mathrm{HCO}_{3}^{-}\) \end{document} exchanger in rat kidney proximal tubule

2003 ◽  
Vol 285 (3) ◽  
pp. C608-C617 ◽  
Author(s):  
Snezana Petrovic ◽  
Liyun Ma ◽  
Zhaohui Wang ◽  
Manoocher Soleimani
Keyword(s):  
Proximal Tubule ◽  
Apical Membrane ◽  
Rat Kidney ◽  
Proximal Tubules ◽  
Immunocytochemical Staining ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Kidney Proximal Tubule ◽  
Anion Transporter

SLC26A6 (or putative anion transporter 1, PAT1) is located on the apical membrane of mouse kidney proximal tubule and mediates [Formula: see text] exchange in in vitro expression systems. We hypothesized that PAT1 along with a [Formula: see text] exchange is present in apical membranes of rat kidney proximal tubules. Northern hybridizations indicated the exclusive expression of SLC26A6 (PAT1 or CFEX) in rat kidney cortex, and immunocytochemical staining localized SLC26A6 on the apical membrane of proximal tubules, with complete prevention of the labeling with the preadsorbed serum. To examine the functional presence of apical [Formula: see text] exchanger, proximal tubules were isolated, microperfused, loaded with the pH-sensitive dye BCPCF-AM, and examined by digital ratiometric imaging. The pH of the perfusate and bath was kept at 7.4. Buffering capacity was measured, and transport rates were calculated as equivalent base flux. The results showed that in the presence of basolateral DIDS (to inhibit [Formula: see text] cotransporter 1) and apical EIPA (to inhibit Na+/H+ exchanger 3), the magnitude of cell acidification in response to addition of luminal Cl– was ∼5.0-fold higher in the presence than in the absence of [Formula: see text]. The Cl–-dependent base transport was inhibited by ∼61% in the presence of 0.5 mM luminal DIDS. The presence of physiological concentrations of oxalate in the lumen (200 μM) did not affect the [Formula: see text] exchange activity. These results are consistent with the presence of SLC26A6 (PAT1) and [Formula: see text] exchanger activity in the apical membrane of rat kidney proximal tubule. We propose that SLC26A6 is likely responsible for the apical [Formula: see text] (and Cl–/OH–) exchanger activities in kidney proximal tubule.

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