Necrosis of the pars recta (S3 segment) of the rat kidney produced by hexachloro 1:3 butadiene

1982 ◽  
Vol 138 (2) ◽  
pp. 99-113 ◽  
Author(s):  
J. Ishmael ◽  
Iona Pratt ◽  
E. A. Lock
Keyword(s):  
1989 ◽  
Vol 12 (5-6) ◽  
pp. 302-312 ◽  
Author(s):  
Olivier Levillain ◽  
Annette Hus-Citharel ◽  
François Morel ◽  
Lise Bankir

1978 ◽  
Vol 234 (3) ◽  
pp. F207-F214 ◽  
Author(s):  
S. W. Weinstein ◽  
J. Szyjewicz

Silicone rubber injections of methyl salicylate-cleared rat kidneys were performed. In 50 of 56 injections of superficial nephrons with their accompanying blood supply, the efferent vessel and early proximal tubule were closely approximated. In 18 of 21 tubular injections filling through the pars recta, the proximal tubule folded upon itself with early and late proximal segments, in close contact, located over their parent glomerulus, and the midproximal segments separate and located over their parent interlobular artery. The distribution of blood was serially through the early-late proximal region above the glomerulus via a long unbranched efferent vessel, via branches over the capsular surface, via capillaries down through the midproximal region, then into the interlobular vein. The observed anatomical pattern of the superficial nephron appears to permit direct functional interactions between the juxtaposed early and late proximal tubule, and in turn may effect midproximal function via the distribution of blood (modified by early proximal) from the efferent vessel to midproximal convolutions. In addition, the relationship between specific segments of the proximal tubule and specific portions of the postglomerular peritubular blood supply may be important in determining the distribution of peritubular physical forces to these nephrons.


1976 ◽  
Vol 24 (12) ◽  
pp. 1239-1248 ◽  
Author(s):  
J K Reddy ◽  
M S Rao ◽  
D E Moody ◽  
S A Qureshi

The development of peroxisomes, lysosomes and endocytic vacuoles in regenerating cells of the pars recta (P3 segment) of proximal tubules, in rats given a single interperitoneal injection of d-serine (80 mg/100 g.b.wt), was studied by light and electron microscopy using cytochemical methods. Rapid proliferation of cells occurred between 2 and 5 days after d-serine induced tubular necrosis; by day 6 almost all injured tubules were re-epithelialized with flat or low cuboidal cells. Peroxisomes and lysosomes were not observed during the period of rapid cell multiplication i.e., between 2 and 6 days after d-serine injection. Restitution of mitochondrial population preceded the development of peroxisomes in the newly regenerated cells of P3 tubules. Maximum development of peroxisomes occurred between 9 and 14 days after d-serine injection. The formation of peroxisomes appeared to correlate closely with the differentiation of apical endocytic vacuoles and the brush border. Lysosomes in the regenerated cells of P3 tubules were the last to develop.


2001 ◽  
Vol 280 (5) ◽  
pp. F794-F802 ◽  
Author(s):  
Yan Huang ◽  
Randall Tracy ◽  
Glenn E. Walsberg ◽  
Anthony Makkinje ◽  
Pingke Fang ◽  
...  

Recently, we found that aquaporin-4 (AQP4) is expressed in the S3 segment of renal proximal tubules of mice but not in rat proximal tubules. Because mice have relatively larger papillae than rats, it was proposed that the renal distribution of AQP4 in various species could be related to their maximum urinary concentrating ability. Therefore, kidneys and other tissues of Merriam's desert kangaroo rat, Dipodomys merriami merriami, which produce extremely concentrated urine (up to 5,000 mosmol/kgH2O), were examined for AQP4 expression and localization. Contrary to our expectation, AQP4 immunostaining was undetectable in any region of the kidney, and the absence of AQP4 protein was confirmed by Western blotting. By freeze fracture electron microscopy, orthogonal arrays of intramembraneous particles (OAPs) were not detectable in plasma membranes of principal cells and proximal tubules. However, AQP4 protein was readily detectable in gastric parietal and brain astroglial cells. Northern blotting failed to detect AQP4 mRNA in kangaroo rat kidneys, whereas both in situ hybridization and RT-PCR experiments did reveal AQP4 mRNA in collecting ducts and proximal tubules of the S3 segment. These results suggest that renal expression of AQP4 in the kangaroo rat kidney is regulated at the transcriptional or translational level, and the absence of AQP4 may be critical for the extreme urinary concentration that occurs in this species.


2005 ◽  
Vol 68 (5) ◽  
pp. 1966
Author(s):  
Shinji Kitamura ◽  
Yasushi Yamasaki ◽  
Hirofumi Makino

1991 ◽  
Vol 261 (4) ◽  
pp. F679-F687 ◽  
Author(s):  
L. Q. Dong ◽  
J. L. Stevens ◽  
S. Jaken

Protein kinase C (PKC) plays an important role in regulation of renal transport and metabolic function. To understand the role of a specific PKC isozyme in renal homeostasis, alpha-PKC content, regulation, and localization have been characterized. Immunoadsorption assays were used to determine that 34% of the total rat kidney PKC (measured as phorbol ester receptors) was alpha-PKC. Immunohistochemical staining with alpha-PKC-specific monoclonal antibodies determined that alpha-PKC was present throughout the nephron and was especially concentrated in proximal tubules and papillary collecting ducts. In general, the S3 segment of the proximal tubule stained more intensely than the S1-S2 segments. Cortical collecting ducts stained poorly for alpha-PKC. Interstitial cells of the papilla also stained for alpha-PKC. Subcellular distribution of alpha-PKC could not be determined in tissue sections; however, in cultured proximal tubule epithelial cells, alpha-PKC was localized not only in cytoplasm but also in cell-cell borders and focal contacts. Chromatography of rat kidney soluble fraction revealed two endogenous kinase inhibitors, one which is PKC specific and one which is a more general kinase inhibitor. The presence of negative regulators of PKC activity suggests that both activation and inactivation of PKC are important for normal renal function.


2001 ◽  
Vol 12 (9) ◽  
pp. 1795-1804
Author(s):  
YOUNG-HEE KIM ◽  
JAE-HO EARM ◽  
TONGHUI MA ◽  
ALAN S. VERKMAN ◽  
MARK A. KNEPPER ◽  
...  

Abstract. Aquaporin-4 (AQP4) is a member of the aquaporin water-channel family. AQP4 is expressed primarily in the brain, but it is also present in the collecting duct of the kidney, where it is located in the basolateral plasma membrane of principal cells and inner medullary collecting duct (IMCD) cells. Recent studies in the mouse also have reported the presence of AQP4 in the basolateral membrane of the proximal tubule. The purpose of this study was to establish the pattern of AQP4 expression during kidney development and in the adult kidney of both the mouse and the rat. Kidneys of adult and 3-, 7-, and 15-d-old mice and rats were preserved for immunohistochemistry and processed using a peroxidase pre-embedding technique. In both the mouse and the rat, strong basolateral immunostaining was observed in IMCD cells and principal cells in the medullary collecting duct at all ages examined. Labeling was weaker in the cortical collecting duct and the connecting tubule, and there was no labeling of connecting tubule cells in the mouse. In adult mouse kidney, strong AQP4 immunoreactivity was observed in the S3 segment of the proximal tubule. However, there was little or no labeling in the cortex or around the corticomedullary junction in 3- and 7-d-old mice. Between 7 and 15 d of age, distinct AQP4 immunoreactivity appeared in the S3 segment of the mouse proximal tubule concomitant with the differentiation of this segment of the nephron. Labeling of proximal tubules was never observed in the rat kidney. These results suggest that there are differences in transepithelial water transport between mouse and rat or that additional, not yet identified water channels exist in the rat proximal tubule.


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