The cellular distribution of aldolase isozymes in rat kidney and brain determined in tissue sections by the immuno-histochemical method

1975 ◽  
Vol 45 (2) ◽  
pp. 143-161 ◽  
Author(s):  
Ernst Dieter Wachsmuth ◽  
Monika Th�ner ◽  
Gerhard Pfleiderer
Keyword(s):  
Rat Kidney ◽  
Histochemical Method ◽  
Cellular Distribution ◽  
Tissue Sections

Cellular Distribution of Exogenous Aprotinin in the Rat Kidney

1998 ◽  
Vol 379 (10) ◽  
Author(s):  
Carlos P. Vio ◽  
Eveline Oestreicher ◽  
Veronica Olavarria ◽  
Victoria Velarde ◽  
Ronald K. Mayfield ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Cellular Distribution

scholarly journals Apoptosis Contributes to Amphotericin B- Induced Nephrotoxicity

2001 ◽  
Vol 45 (3) ◽  
pp. 679-685 ◽  
Author(s):  
Despina E. Varlam ◽  
Mustafa M. Siddiq ◽  
Lance A. Parton ◽  
Holger Rüssmann
Keyword(s):  
Side Effects ◽  
Amphotericin B ◽  
Rat Kidney ◽  
Renal Tissue ◽  
Concomitant Treatment ◽  
Sprague Dawley ◽  
Recombinant Human Insulin ◽  
Tissue Sections ◽  
Dose Dependent Fashion ◽  
Dose Dependent

ABSTRACT The aim of this study was to investigate whether apoptosis contributes to nephrotoxicity caused by amphotericin B (AmB). By detecting apoptosis-specific DNA fragmentation, it is demonstrated that proximal tubular cells (LLC-PK1) and medullary interstitial cells (RMIC) respond with programmed cell death when treated with therapeutic doses of AmB. Concomitant application of AmB and recombinant human insulin-like growth factor-1 (rhIGF-1), a known antiapoptotic agent, abrogated apoptosis in vitro. To validate that the observed apoptotic effects on renal tissue culture cells are applicable to an in vivo setting, an animal model was used for verification. Therefore, Sprague-Dawley rats were treated with AmB. The drug caused hypokalemia, decreased weight gain, loss of renal concentrating ability, and dehydration in a dose-dependent fashion. Microscopic examination of renal tissue sections revealed apoptotic alterations predominantly in proximal and distal tubular epithelial cells. To verify that the observed clinical side effects were linked to apoptosis, rhIGF-1 was applied concomitantly with AmB. In all animals, rhIGF-1 prevented the above-mentioned clinical side effects. Moreover, significantly reduced apoptosis was observed in renal tissue sections of these animals, indicating the relevance of apoptosis in nephrotoxicity. This is the first report to demonstrate that AmB induces apoptosis in the rat kidney in a dose-dependent fashion. The incidence of apoptosis correlates with renal toxicity and can be abrogated by concomitant treatment with rhIGF-1.

Cellular distribution of H(+)-ATPase following acute unilateral ureteral obstruction in rats

1991 ◽  
Vol 261 (3) ◽  
pp. F365-F376 ◽  
Author(s):  
H. Purcell ◽  
B. Bastani ◽  
K. P. Harris ◽  
P. Hemken ◽  
S. Klahr ◽  
...  
Keyword(s):  
Ureteral Obstruction ◽  
Morphological Changes ◽  
Rat Kidney ◽  
Cell Number ◽  
Unilateral Ureteral Obstruction ◽  
Cellular Distribution ◽  
Physiological Abnormalities ◽  
Human Disorder ◽  
Atpase Staining

Unilateral ureteral obstruction for 24 h produces an acidification defect in the rat kidney that closely resembles the human disorder. We examined the role of renal vacuolar H(+)-ATPase distribution and content in the generation of the postobstructive abnormality in distal hydrogen ion secretion. Rats were subjected to unilateral ureteral obstruction for 24 h, and the obstructed and contralateral kidneys were removed at 3 h, 5 days, and 10 days after release of the obstruction. The postobstructed and contralateral kidneys and kidneys from sham-operated rats were analyzed for intercalated cell number and subtype and for the cellular distribution of ATPase staining by means of a monoclonal antibody specific for the 31-kDa subunit of the vacuolar H(+)-ATPase. No change in the number or distribution of subtypes was detected in the cortex nor in the outer or inner stripe of the outer medulla. Immunoreactive H(+)-ATPase increased in both the cortex and medulla at 3 h after obstruction, and thereafter it declined to control values. The major morphological changes in H(+)-ATPase staining detected were an alteration in the intracellular distribution of the enzyme, which we refer to as discontinuity of (or “gaps” in) apical staining, and a decrease in the percent of intercalated cells showing a rim (or plasma membrane) staining pattern in the inner medulla. The changes observed may be a morphological representation of the physiological abnormalities underlying the postobstructive acidification defect.

Simultaneous Comparison of Two Techniques For X-Ray Microanalysis of Tissue Sections

1985 ◽  
Vol 43 ◽  
pp. 466-467
Author(s):  
A.J. Saubermann ◽  
V.L. Scheid ◽  
D.C. Dobyan ◽  
R.E. Bulger
Keyword(s):  
Renal Cortex ◽  
Rat Kidney ◽  
Proximal Tubule Cell ◽  
Tubule Cell ◽  
X Ray ◽  
Tissue Sections ◽  
Ringer’S Solution ◽  
External Standard ◽  
Analytical Algorithm ◽  
Biological Differences

Major differences in elemental and water content in cells of rat renal papillae in antidiuresis have been reported using x-ray microanalysis by us and by Beck et al. Various reasons for these reported differences have been suggested, including the analytical algorithm used, cryosectioning at “warmer” temperatures leading to elemental displacement, and biological differences. The purpose of these studies is to determine the reasons for these reported differences by comparing both our methods for x-ray analysis of frozen hydrated tissue sections and the method of Beck et al. simultaneously on the same tissue. Our methodology uses fully hydrated tissue sections without external standards, while Beck et al. uses frozen dried cryosections with an albumin external standard (Ringer's solution in 20% albumin). In these studies two anatomical areas of the rat kidney were subjected to analysis using both our methods and theirs simultaneously: 1) the proximal tubule cell (PTC) from rat renal cortex, and 2) the antidiuretic papilla prepared according to Beck et al.

Expression of synaptotagmin VIII in rat kidney

1998 ◽  
Vol 275 (1) ◽  
pp. F131-F142 ◽  
Author(s):  
Bellamkonda K. Kishore ◽  
James B. Wade ◽  
Kristel Schorr ◽  
Takeaki Inoue ◽  
Béatrice Mandon ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Rat Kidney ◽  
Rt Pcr ◽  
Tissue Sections ◽  
Pcr Product ◽  
Collecting Ducts ◽  
Cell Remodeling ◽  
Regulation Of Transport ◽  
Carboxy Terminal ◽  
Renal Expression

The synaptotagmins are a family of integral membrane proteins proposed to function as regulators of both exocytosis and endocytosis. Here, we have used immunochemical techniques and RT-PCR to assess sites of renal expression of synaptotagmin VIII. A polyclonal antibody was raised to a synthetic peptide corresponding to the carboxy-terminal 21 amino acids of mouse synaptotagmin VIII. On immunoblots of membrane fractions from renal cortex and medulla (and in several other tissues), the antibody labeled a 52-kDa band (absent with preimmune IgG). Immunofluorescence localization was carried out in tissue sections from rat kidney. The synaptotagmin VIII antibody labeled early proximal tubules, thin ascending limbs, thick ascending limbs, connecting tubules, and collecting ducts. In collecting ducts, both type A and B intercalated cells exhibited basolateral labeling, whereas principal cells were labeled chiefly in the apical and subapical portion of the cells. Thick ascending limbs were labeled in both the basolateral and apical regions. RT-PCR experiments using total RNA extracted from cortex and medulla or microdissected inner medullary collecting ducts gave a single band of appropriate size. Sequencing of the PCR product confirmed that the amplified target is synaptotagmin VIII. We conclude that synaptotagmin VIII is broadly expressed among renal tubule epithelia, raising the possibility that it is involved in regulation of transport and/or cell remodeling at several sites in the nephron and collecting duct.

A PLCδ1-binding protein, p122RhoGAP, is localized in focal adhesions

2004 ◽  
Vol 32 (6) ◽  
pp. 1107-1109 ◽  
Author(s):  
K. Kawai ◽  
M. Yamaga ◽  
Y. Iwamae ◽  
M. Kiyota ◽  
H. Kamata ◽  
...  
Keyword(s):  
Cell Migration ◽  
Focal Adhesion ◽  
Rat Kidney ◽  
Focal Adhesions ◽  
Small Gtpase ◽  
Cellular Distribution ◽  
Kidney Cells ◽  
Gtpase Activating Protein ◽  
Immunofluorescence Studies ◽  
Normal Rat

We have investigated the cellular distribution of p122RhoGAP, a GTPase-activating protein of Rho small GTPase and an activator of phospholipase C-δ1. Immunofluorescence studies demonstrated that endogenous p122 is localized at the tips of actin stress fibres and co-localizes with vinculin in normal rat kidney cells. In immunoprecipitation studies, p122 co-precipitated with vinculin, indicating that p122 is localized at the sites of focal adhesion. We have also shown that the N-terminal half of p122 is responsible for this localization. It is conceivable, therefore, that p122 is involved in the reorganization of the actin cytoskeleton and focal adhesions that regulate cell–substratum adhesion and cell migration.

scholarly journals The Histochemical Localization of Triphosphopyridine Nucleotide Diaphorase

1958 ◽  
Vol 4 (4) ◽  
pp. 467-474 ◽  
Author(s):  
Marvin M. Nachlas ◽  
Donald G. Walker ◽  
Arnold M. Seligman
Keyword(s):  
Macula Densa ◽  
Histochemical Method ◽  
Histochemical Localization ◽  
Kidney Cortex ◽  
Tetrazolium Salt ◽  
Tissue Sections ◽  
Isocitric Dehydrogenase ◽  
Diaphorase Activity

A histochemical method is described for the localization of triphosphopyridine nucleotide diaphorase using a recently synthesized tetrazolium salt (Nitro-BT). By virtue of the favorable histochemical properties of this reagent, it has been possible to demonstrate that whereas DPN diaphorase is usually restricted to the mitochondria, the TPN diaphorase activity of corresponding cells was distributed throughout the cytoplasm in granules too fine to be considered mitochondria. Furthermore, although the diaphorase alone is responsible for the passage of electrons from TPNH to the tetrazole, it has been found that sites of activity of different TPN-linked dehydrogenases can be visualized in tissue sections, and characteristic loci for each enzyme may be observed. For example, whereas TPN diaphorase and isocitric dehydrogenase have an extensive distribution in the kidney cortex, 6-phosphogluconic dehydrogenase is limited to the cells of the macula densa.

scholarly journals Evaluation of cellular substrates for antinuclear antibody determinations

1975 ◽  
Vol 2 (1) ◽  
pp. 42-45
Author(s):  
N Hahon ◽  
H L Eckert ◽  
J Stewart
Keyword(s):  
Antinuclear Antibody ◽  
Human Lung ◽  
Animal Cell ◽  
Rat Kidney ◽  
Fibroblast Cell ◽  
Serum Samples ◽  
Cell Monolayers ◽  
Tissue Sections ◽  
Immunofluorescent Technique ◽  
Fibroblast Cell Lines

The immunofluorescent technique was employed to evaluate the sensitivity of 10 human and animal cell monolayers and tissue sections as substrates for titering the antinuclear antibody content of serum samples. The highest mean ranks of sensitivity, the relative ability of each substrate to maintain its sensitivity rank when 21 selected positive sera were tested, were achieved by two fibroblast cell lines, baby hamster kidney (BHK 21/C13) and human lung (WI-38), respectively. The least sensitive substrates were commercial rat kidney and liver tissue sections.

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