Journal articles: 'Kidneys – Histochemistry'

1

Gomez, R. A., K. R. Lynch, B. C. Sturgill, J. P. Elwood, R. L. Chevalier, R. M. Carey, and M. J. Peach. "Distribution of renin mRNA and its protein in the developing kidney." American Journal of Physiology-Renal Physiology 257, no. 5 (November 1, 1989): F850—F858. http://dx.doi.org/10.1152/ajprenal.1989.257.5.f850.

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The intrarenal distribution of renin changes markedly during maturation. To determine whether renin gene expression changes along the developing renal vasculature, renin mRNA distribution was assessed using in situ hybridization histochemistry. Fetal, newborn, and adult kidney tissue sections from Wistar-Kyoto rats were hybridized with an oligonucleotide complementary to rat renin mRNA. In fetal kidneys, renin mRNA was found in the vascular pole of juxtamedullary glomeruli and along afferent, interlobular, and arcuate arteries. In kidneys from newborn rats, renin mRNA localized throughout the whole length of afferent arterioles, but was not detected in interlobular or arcuate arteries. In adult kidneys, hybridization signals were less intense and confined to the juxtaglomerular apparatus. Immunolocalization of renin with a polyclonal anti-rat renin antibody paralleled closely the mRNA distribution. Northern blot analyses demonstrated that renin mRNA levels were higher in fetal and newborn (20- and 10-fold, respectively) than in adult kidneys. We conclude the following. 1) The fetal kidney expresses the renin gene. 2) Expression of the renin gene is subjected to developmental changes. 3) As maturation progresses, localization of renin synthesis and storage shifts from large intrarenal arteries to a restricted, classical juxtaglomerular site in the afferent arteriole.

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Castagnaro, M., M. Marin, C. Ghittino, and RP Hedrick. "Lectin histochemistry and ultrastructure of rainbow trout Oncorhynchus mykiss kidneys affected by proliferative kidney." Diseases of Aquatic Organisms 10 (1991): 173–83. http://dx.doi.org/10.3354/dao010173.

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Alpers, Charles E., and Jay H. Beckstead. "Enzyme Histochemistry in Plastic-Embedded Sections of Normal and Diseased Kidneys." American Journal of Clinical Pathology 83, no. 5 (May 1, 1985): 605–12. http://dx.doi.org/10.1093/ajcp/83.5.605.

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Cullen-McEwen, Luise A., James A. Armitage, Jens R. Nyengaard, Karen M. Moritz, and John F. Bertram. "A design-based method for estimating glomerular number in the developing kidney." American Journal of Physiology-Renal Physiology 300, no. 6 (June 2011): F1448—F1453. http://dx.doi.org/10.1152/ajprenal.00055.2011.

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Low glomerular (nephron) endowment has been associated with an increased risk of cardiovascular and renal disease in adulthood. Nephron endowment in humans is determined by 36 wk of gestation, while in rats and mice nephrogenesis ends several days after birth. Specific genes and environmental perturbations have been shown to regulate nephron endowment. Until now, design-based method for estimating nephron number in developing kidneys was unavailable. This was due in part to the difficulty associated with unambiguously identifying developing glomeruli in histological sections. Here, we describe a method that uses lectin histochemistry to identify developing glomeruli and the physical disector/fractionator principle to provide unbiased estimates of total glomerular number ( Nglom). We have characterized Nglom throughout development in kidneys from 76 rats and model this development with a 5-parameter logistic equation to predict Nglom from embryonic day 17.25 to adulthood ( r2 = 0.98). This approach represents the first design-based method with which to estimate Nglom in the developing kidney.

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Wintour, EM, A. Butkus, L. Earnest, and S. Pompolo. "The erythropoietin gene is expressed strongly in the mammalian mesonephric kidney." Blood 88, no. 9 (November 1, 1996): 3349–53. http://dx.doi.org/10.1182/blood.v88.9.3349.bloodjournal8893349.

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In the ovine fetus at 41 days of gestation (term is 150 days), there are two sets of kidneys, mesonephrol and metanephrol. We have examined the expression of the erythropoietin (Epo) gene in both types of kidneys by competitive reverse transcriptase-polymerase chain reaction and hybridization histochemistry and compared the expression to that of the 60-day fetal metanephros. At 41 days, the Epo gene was expressed in both mesonephros and metanephros, as well as in the fetal liver. The cells expressing the Epo gene in the mesonephros were interstitial cells in the vicinity of the proximal tubules.

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Castagnaro, Massimo, Joseph Alroy, Angelo A. Ucci, and Robert H. Glew. "Lectin histochemistry and ultrastructure of feline kidneys from six different storage diseases." Virchows Archiv B Cell Pathology Including Molecular Pathology 54, no. 1 (December 1987): 16–26. http://dx.doi.org/10.1007/bf02899193.

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Firth, J. A. "Quantitative assessment of Na+,K+-ATPase localization by direct and indirect p-nitrophenyl phosphatase methods." Journal of Histochemistry & Cytochemistry 35, no. 4 (April 1987): 507–13. http://dx.doi.org/10.1177/35.4.3029215.

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Na+,K+-ATPase histochemistry, using direct (Pb) and indirect (Mg/Sr-Co) p-nitrophenyl phosphatase methods, was assessed by scanning integrative microdensitometry of three classes of tubules in mouse and guinea pig kidneys. The methods yielded similar and appropriate patterns of activity distribution and inhibitor response. The indirect method gave preferable results, in that non-enzymic background was lower and rate of reaction product accumulation was considerably higher.

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Robert, Barry, Patricia L. St. John, and Dale R. Abrahamson. "Direct visualization of renal vascular morphogenesis inFlk1 heterozygous mutant mice." American Journal of Physiology-Renal Physiology 275, no. 1 (July 1, 1998): F164—F172. http://dx.doi.org/10.1152/ajprenal.1998.275.1.f164.

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Flk1, a receptor tyrosine kinase for vascular endothelial growth factor (VEGF), is the earliest known marker for endothelial precursors (angioblasts). We examined heterozygous mice in which the Flk1gene was partially replaced by a promoter-less LacZ insert and used β-galactosidase histochemistry to view cells transcribing Flk1. In day 10 ( E10) embryos, a Flk1-positive network surrounded the metanephric blastema, and, at E11, a vessel entered the metanephros from its ventral aspect alongside the ingrowing ureteric bud. However, aortic branches did not engage embryonic kidneys at these time points. In newborns, β-galactosidase was localized exclusively and intensely to endothelial cells of all vessels and glomeruli. In contrast, when E12 kidneys grown in organ culture for 6 days were examined, only scattered Flk1-positive cells were seen, glomeruli were unlabeled, and vessels were absent. When organ-cultured kidneys were then grafted into wild-type anterior eye chambers, numerous Flk1-positive endothelial cells in vessels and glomeruli were found, all stemming from the graft. Image analysis showed that grafts with the most abundant glomerulo- and tubulogenesis were also those with the richest expression of Flk1. We conclude that 1) kidney microvessels precede renal artery development, 2) angioblast differentiation is arrested in organ culture but released on grafting when vasculogenesis resumes, and 3) nephrogenesis and microvessel assembly are tightly coupled in vivo.

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el-Dahr, S. S., R. A. Gomez, M. S. Gray, M. J. Peach, R. M. Carey, and R. L. Chevalier. "In situ localization of renin and its mRNA in neonatal ureteral obstruction." American Journal of Physiology-Renal Physiology 258, no. 4 (April 1, 1990): F854—F862. http://dx.doi.org/10.1152/ajprenal.1990.258.4.f854.

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Angiotensin II is an important mediator of renal vasoconstriction resulting from chronic unilateral ureteral obstruction (UUO). Distribution of renin mRNA and immunoreactive renin (IR) was examined in kidneys of 1-mo-old Sprague-Dawley rats subjected to either sham operation (n = 21), left complete UUO (n = 21), or right uninephrectomy (UNX, n = 16) at 2 days of age. There were no differences among the three groups in mean arterial pressure or plasma renin activity. Unlike sham kidneys, in which IR was detected in less than 55% of juxtaglomerular apparatuses (JGA) and was confined to a juxtaglomerular location, IR in both kidneys of animals with UUO appeared in greater than 75% of JGA and extended along most of the length of the afferent arteriole (P less than 0.01). In contrast, IR in kidneys of UNX rats was localized to the JGA as in sham-operated animals. Compared with sham-operated kidneys, renal renin content was increased in the obstructed kidneys (P less than 0.01) but decreased in the intact opposite kidneys of UUO rats and in the remaining kidneys of UNX rats (P less than 0.05). Renin mRNA, detected by in situ hybridization histochemistry, was localized to the JGA in kidneys of all groups. However, the fraction of JGA containing detectable renin mRNA was higher in obstructed kidneys than in intact opposite, UNX, or sham kidneys (P less than 0.05). In conclusion, UUO alters intrarenal renin independent of the systemic renin-angiotensin system. The greater distribution of IR, increased renin content, and renin gene expression of kidneys with ipsilateral UUO are consistent with a role for renin-angiotensin in mediating the vasoconstriction resulting from UUO.

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Okabe, M., K. Nakayama, M. Kurasaki, F. Yamasaki, K. Aoyagi, O. Yamanoshita, S. Sato, T. Okui, T. Ohyama, and N. Kasai. "Direct visualization of copper-metallothionein in LEC rat kidneys: application of autofluorescence signal of copper-thiolate cluster." Journal of Histochemistry & Cytochemistry 44, no. 8 (August 1996): 865–73. http://dx.doi.org/10.1177/44.8.8756759.

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We report on the histochemistry of copper-metallothionein (Cu-MT) in the kidneys of Long Evans Cinnamon (LEC) rats. We used the visualization principle of histochemistry based on the autofluorescence emission from the fluorophore of Cu(+)-thiolate clusters in proteins. Intense autofluorescence signals were observed with a ring at the outer stripe of the outer medulla. Orange fluorescence signals were observed in the nuclei and cytoplasm of proximal straight tubular (PST) cells of segment 3 (S3) at the outer stripe of the outer medulla, and yellow-orange signals were detected in lysosome-like organelles in the proximal convoluted tubule (PCT) cells of segments 1 and 2 (S1 and S2) adjacent to the glomeruli in the cortex. These fluorescent materials were identified as Cu-MT because both signals were quenched by withdrawing Cu+ or by blocking cysteine residues, the distributions of cysteine residues and immunoreactive MT showed identical patterns to the localization of the fluorescence signals, and the fluorescent proteins containing Cu were eluted at the same Kd value of purified Cu-MT by gel filtration chromatography. However, a high level of MT mRNA was detected only in the outer stripe of the outer medulla where the orange fluorescence signals were detected, but not in the cortex. This difference in localization between the protein and the mRNA suggested that synthesis of renal MT occurs do novo in the outer stripe of the outer medulla. The yellow-orange fluorescent Cu-MT located in the lysosomal organelles at S1 and S2 of the PCT cells in the cortex could be Cu-MT of nonrenal origin, i.e., Cu-MT transported from other organs.

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Almatroodi, Saleh A., Abdullah M. Alnuqaydan, Ali Yousif Babiker, Mashael Abdullah Almogbel, Amjad Ali Khan, and Arshad Husain Rahmani. "6-Gingerol, a Bioactive Compound of Ginger Attenuates Renal Damage in Streptozotocin-Induced Diabetic Rats by Regulating the Oxidative Stress and Inflammation." Pharmaceutics 13, no. 3 (February 28, 2021): 317. http://dx.doi.org/10.3390/pharmaceutics13030317.

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The aim of present study is to investigate the role of 6-gingerol in ameliorating the renal injury in streptozotocin (STZ)-induced diabetic rats. The diabetes was induced by using a single dose of freshly prepared STZ (55 mg/kg body weight) intraperitoneally which causes the degeneration of pancreatic Langerhans islet β-cells. The diabetic rats were treated with oral gavage of 6-gingerol (10 mg/kg b.w.). The treatment plan was continued for 8 weeks successively and the body weight and fasting blood glucose levels were weekly checked. The biochemical parameters like lipid profile, kidney profile, antioxidant enzyme levels, lipid peroxidation and anti-inflammatory marker levels were investigated after the treatment plant. The pathological condition of kidneys was examined by haematoxylin-eosin (H&E) staining besides this analysis of NF-κB protein expression by immuno-histochemistry was performed. Some of the major parameters in diabetes control vs. normal control were reported as fasting blood glucose (234 ± 10 vs. 102 ± 8 mg/dL), serum creatinine (109.7 ± 7.2 vs. 78.9 ± 4.5 μmol/L) and urea (39.9 ± 1.8 vs. 18.6 mg/dL), lipid profile levels were significantly enhanced in diabetic rats. Moreover, diabetic rats were marked with decreased antioxidant enzyme levels and increased inflammatory markers. Treatment with 6-gingerol significantly restored the fasting blood glucose level, hyperlipidaemia, Malondialdehyde (MDA) and inflammatory marker levels, NF-κB protein expression and augmented the antioxidant enzyme levels in the kidneys of diabetic rats. The kidney damage was significantly normalized by the treatment of 6-gingerol and it provides an evidence that this novel compound plays a significant role in the protection of kidney damage. These findings demonstrate that 6-gingerol reduces lipid parameters, inflammation and oxidative stress in diabetic rats, thereby inhibiting the renal damage. Our results demonstrate that use of 6-gingerol could be a novel therapeutic approach to prevent the kidney damage associated with the diabetes mellitus.

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12

Fischer, E., J. Schnermann, J. P. Briggs, W. Kriz, P. M. Ronco, and S. Bachmann. "Ontogeny of NO synthase and renin in juxtaglomerular apparatus of rat kidneys." American Journal of Physiology-Renal Physiology 268, no. 6 (June 1, 1995): F1164—F1176. http://dx.doi.org/10.1152/ajprenal.1995.268.6.f1164.

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The presence of NO synthase (NOS) in cells of the macula densa (MD) suggests a role for arginine-derived NO in tubulovascular information transfer. To investigate the postnatal development of the neuronal isoform of NOS and of renin in the kidney, the cellular distribution of these enzymes was examined in perfusion-fixed kidneys of 2-, 6-, and 15-day-old rats at both the protein and mRNA level (n = 4 rats/group). NOS and renin and their mRNAs were localized by immunohistochemical and in situ hybridization methods. In addition, NOS levels were assessed by using NADPH diaphorase (NADPH-d) histochemistry. For quantification, the fraction of NOS- and renin-positive glomeruli as well as the number of NOS-positive MD cells was evaluated at all stages. Presence of NOS in single cells of the developing distal tubule was encountered already in the S-shaped body. Full expression of a NOS signal in MD cells was seen as soon as a glomerular urinary space was developed. Double labeling with NADPH-d and antibody to Tamm-Horsfall protein (THP) indicated mutual exclusiveness of NADPH-d-positive MD cells and neighboring THP-positive distal tubule cells at all levels of development. The relative intensity of renin status was 2 day > 6 day > 15 day, whereas NOS expression was maximal on postnatal day 6. Our data are consistent with an involvement of MD NO synthesis in the early organization of the juxtaglomerular apparatus during nephrogenesis and suggest an interdependent relation with renin-producing cells.

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Ridderstråle, Y., P. J. Wistrand, and R. E. Tashian. "Membrane-associated carbonic anhydrase activity in the kidney of CA II-deficient mice." Journal of Histochemistry & Cytochemistry 40, no. 11 (November 1992): 1665–73. http://dx.doi.org/10.1177/40.11.1431055.

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Carbonic anhydrase II-deficient mice offer a possibility to study the localization along the nephron of membrane-associated carbonic anhydrase (CA) activity without interference from the cytoplasmic enzyme. We studied the localization of CA in kidneys from CA II-deficient and control mice by immunocytochemistry (CA II) and histochemistry. Cytoplasmic staining was found in convoluted proximal tubule, thick limb of Henle, and principal and intercalated cells of collecting duct in the control animals but was absent in the CA II-deficient mice. In cells with cytoplasmic staining the cell nuclei were stained. Intense histochemical activity was associated with apical and basolateral membranes of convoluted proximal tubule, first part of thin limb, thick limb, and basolateral membranes of late distal tubule. In collecting ducts of control animals, the basolateral cell membranes of intercalated cells were the only clearly stained membranes. In CA II-deficient animals one type of intercalated cell was stained most intensely at the apical membranes and another only at the basolateral. We suggest that the former corresponds to Type A intercalated cells secreting H+ ions to the luminal side and the latter to Type B cells secreting H+ ions to the basolateral side.

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14

Bachmann, Sebastian, Kerim Mutig, James Bates, Pia Welker, Beate Geist, Volkmar Gross, Friedrich C. Luft, et al. "Renal effects of Tamm-Horsfall protein (uromodulin) deficiency in mice." American Journal of Physiology-Renal Physiology 288, no. 3 (March 2005): F559—F567. http://dx.doi.org/10.1152/ajprenal.00143.2004.

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The Tamm-Horsfall protein (THP; uromodulin), the dominant protein in normal urine, is produced exclusively in the thick ascending limb of Henle's loop. THP mutations are associated with disease; however, the physiological role of THP remains obscure. We generated THP gene-deficient mice (THP −/−) and compared them with wild-type (WT) mice. THP −/− mice displayed anatomically normal kidneys. Steady-state electrolyte handling was not different between strains. Creatinine clearance was 63% lower in THP −/− than in WT mice ( P < 0.05). Sucrose loading induced no changes between strains. However, water deprivation for 24 h decreased urine volume from 58 ± 9 to 28 ± 4 μl·g body wt−1·24 h−1 in WT mice ( P < 0.05), whereas in THP −/− mice this decrease was less pronounced (57 ± 4 to 41 ± 5 μl·g body wt−1·24 h−1; P < 0.05), revealing significant interstrain difference ( P < 0.05). We further used RT-PCR, Northern and Western blotting, and histochemistry to study renal transporters, channels, and regulatory systems under steady-state conditions. We found that major distal transporters were upregulated in THP −/− mice, whereas juxtaglomerular immunoreactive cyclooxygenase-2 (COX-2) and renin mRNA expression were both decreased in THP −/− compared with WT mice. These observations suggest that THP influences transporters in Henle's loop. The decreased COX-2 and renin levels may be related to an altered tubular salt load at the macula densa, whereas the increased expression of distal transporters may reflect compensatory mechanisms. Our data raise the hypothesis that THP plays an important regulatory role in the kidney.

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Marsigliante, S., A. Muscella, S. Barker, and C. Storelli. "Angiotensin II modulates the activity of the Na+/K+ATPase in eel kidney." Journal of Endocrinology 165, no. 1 (April 1, 2000): 147–56. http://dx.doi.org/10.1677/joe.0.1650147.

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We have previously shown that angiotensin II (Ang II) has a role at the level of the eel gill chloride cell regulating sodium balance, and therefore osmoregulation; the purpose of the present study was to extend these findings to another important osmoregulatory organ, the kidney. By catalytic histochemistry Na(+)/K(+)ATPase activity was found in both sea water (SW)- and freshwater (FW)-adapted eel kidney, particularly at the level of both proximal and distal tubules. Quantitation of tubular cell Na(+)/K(+)ATPase activity, by imaging, gave values in SW-adapted eels which were double those found in FW-adapted eels (Student's t-test: P<0.0001). This was due to a reduced number of positive tubules present in FW-adapted eels compared with SW-adapted eels. By conventional enzymatic assay, the Na(+)/K(+)ATPase activity in isolated tubular cells from SW-adapted eels showed values 1.85-fold higher those found in FW-adapted eels (Student's ttest: P<0.0001). Perfusion of kidney for 20 min with 100 nM Ang II provoked a significant increase (1.8-fold) in Na(+)/K(+)ATPase activity in FW, due to up-regulation of Na(+)/K(+)ATPase activity in a significantly larger number of tubules (Student's t-test: P<0.0001). The effect of 100 nM Ang II in SW-adapted kidneys was not significant. Stimulation with increasing Ang II concentrations was performed on isolated kidney tubule cells: Ang II provoked a dose-dependent stimulation of the Na(+)/K(+)ATPase activity in FW-adapted eels, reaching a maximum at 100 nM (1.82-fold stimulation), but no significant effect was found in SW-adapted eels (ANOVA: P<0.001 and P>0.05 respectively). Isolated tubule cells stimulated with 100 nM Ang II showed a significant generation of inositol trisphosphate (InsP(3)) and an increment in calcium release from intracellular stores. In conclusion, our results suggest that tubular Na(+)/K(+)ATPase is modulated by environmental salinity, and that Ang II has a role in regulating its activity in FW-adapted eels, probably through an InsP(3)-dependent mechanism.

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Abrahamson, D. R. "Origin of the glomerular basement membrane visualized after in vivo labeling of laminin in newborn rat kidneys." Journal of Cell Biology 100, no. 6 (June 1, 1985): 1988–2000. http://dx.doi.org/10.1083/jcb.100.6.1988.

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To examine the origin and assembly of glomerular basement membranes (GBMs), affinity purified anti-laminin IgG was directly coupled to horseradish peroxidase (HRP) and intravenously injected into newborn rats. Kidneys were then processed for peroxidase histochemistry and microscopy. Within 1 h after injection, anti-laminin bound to basement membranes of nephrons in all developmental stages (vesicle, comma, S-shaped, developing capillary loop, and maturing glomeruli). In S-shaped and capillary loop glomeruli, anti-laminin-HRP labeled a double basal lamina between the endothelium and epithelium. Sections incubated with anti-laminin in vitro showed labeling within the rough endoplasmic reticulum of endothelium and epithelium, indicating that both cell types synthesized laminin for the double basement membrane. In maturing glomeruli, injected anti-laminin-HRP bound throughout the GBMs, and double basement membranes were rarely observed. At this stage, however, numerous knobs or outpockets of basement membrane material extending far into the epithelial side of the capillary wall were identified and these were also labeled throughout their full thickness. No such outpockets were found in the endothelial cell layer of newborn rats (and they normally are completely absent in fully mature, adult glomeruli). In contrast with these results, in kidneys fixed 4-6 d after anti-laminin IgG-HRP injection, basement membranes of vesicle, comma, and S-shaped nephrons were unlabeled, indicating that they were assembled after injection. GBM labeling was seen in maturing glomeruli, however. In addition, the outpockets of basement membrane extending into the epithelium were often completely unlabeled whereas GBMs lying immediately beneath them were labeled intensely, which indicates that the outpockets were probably assembled by the epithelium. Injections of sheep anti-laminin IgG followed 8 d later with injections of biotin-rabbit anti-laminin IgG and double-label immunofluorescence microscopy confirmed that GBM formation continued during individual capillary loop expansion. GBM assembly therefore occurs by at least two different processes at separate times in development: (a) fusion of endothelial and epithelial basement membranes followed by (b) addition of new basement membrane from the epithelium into existing GBMs.

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Gross, M. L., G. Piecha, A. Bierhaus, W. Hanke, T. Henle, P. Schirmacher, and E. Ritz. "Glycated and carbamylated albumin are more “nephrotoxic” than unmodified albumin in the amphibian kidney." American Journal of Physiology-Renal Physiology 301, no. 3 (September 2011): F476—F485. http://dx.doi.org/10.1152/ajprenal.00342.2010.

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There is increasing evidence that proteins in tubular fluid are “nephrotoxic.” In vivo it is difficult to study protein loading of tubular epithelial cells in isolation, i.e., without concomitant glomerular damage or changes of renal hemodynamics, etc. Recently, a unique amphibian model has been described which takes advantage of the special anatomy of the amphibian kidney in which a subset of nephrons drains the peritoneal cavity (open nephrons) so that intraperitoneal injection of protein selectively causes protein storage in and peritubular fibrosis around open but not around closed tubules. There is an ongoing debate as to what degree albumin per se is nephrotoxic and whether modification of albumin alters its nephrotoxicity. We tested the hypothesis that carbamylation and glycation render albumin more nephrotoxic compared with native albumin and alternative albumin modifications, e.g., lipid oxidation and lipid depletion. Preparations of native and modified albumin were injected into the axolotl peritoneum. The kidneys were retrieved after 10 days and studied by light microscopy as well as by immunohistochemistry [transforming growth factor (TGF)-β, PDGF, NF-κB, collagen I and IV, RAGE], nonradioactive in situ hybridization, and Western blotting. Two investigators unaware of the animal groups evaluated and scored renal histology. Compared with unmodified albumin, glycated and carbamylated albumin caused more pronounced protein storage. After no more than 10 days, selective peritubular fibrosis was seen around nephrons draining the peritoneal cavity (open nephrons), but not around closed nephrons. Additionally, more intense expression of RAGE, NF-κB, as well as PDGF, TGF-β, EGF, ET-1, and others was noted by histochemistry and confirmed by RT-PCR for fibronectin and TGF-β as well as nonradioactive in situ hybridization for TGF-β and fibronectin. The data indicate that carbamylation and glycation increase the capacity of albumin to cause tubular cell damage and peritubular fibrosis.

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Díaz, Eduardo Alfonso, Gustavo Donoso, Carolina Sáenz, Ivette Dueñas, and Francisco Cabrera. "Clinical and pathological findings in a Dwarf Red Brocket Mazama rufina (Mammalia: Cetartiodactyla: Cervidae) attacked by dogs." Journal of Threatened Taxa 12, no. 13 (September 26, 2020): 16885–90. http://dx.doi.org/10.11609/jott.5552.12.13.16885-16890.

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Capture myopathy is a common fatal syndrome in wild ungulates resulting from anthropogenic stressful events such as the capture or transport of specimens. There are, however, few published data on this issue due to predator attacks. The present report describes for the first time the capture myopathy syndrome in a Dwarf Red Brocket Mazama rufina following dog Canis familiaris attack. Clinical signs included pale mucous with increase capillary refill time, tachycardia, tachypnea, hypertension, hypothermia, hypoglycemia, and red brown urine. Muscle tremors, ataxia, prostration, paralysis, and opisthotonus were progressively observed. Laboratory tests showed increased levels of cortisol, creatinine, creatine kinase, lactate dehydrogenase, and potassium; decreased blood urea nitrogen-creatinine ratio; and myoglobinuria. The animal died 72 hours after hospital admission. At necropsy, findings included injuries on both hindlimbs with edema, emphysema, and soft-friable texture in affected muscles, dark kidneys and brown urine in bladder. Histopathological exams were indicative of skeletal-cardiac muscle degenerative lesions and myoglobinuric nephrosis. Immuno-histochemistry revealed myoglobin depletion in degenerate muscles and myoglobin accumulation in renal tissues. We strongly recommend that treatment for capture myopathy be initiated when a wild ungulate is admitted with history of predator attack, since the syndrome may have already established. This report adds to the instances of negative impacts caused by domestic dogs on threatened wildlife species.

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Xu, Shanqin, Jia Ying, Bingbing Jiang, Wei Guo, Takeshi Adachi, Viktor Sharov, Harold Lazar, et al. "Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 6 (June 2006): H2220—H2227. http://dx.doi.org/10.1152/ajpheart.01293.2005.

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Nitration of protein tyrosine residues (nY) is a marker of oxidative stress and may alter the biological activity of the modified proteins. The aim of this study was to develop antibodies toward site-specific nY-modified proteins and to use histochemistry and immunoblotting to demonstrate protein nitration in tissues. Affinity-purified polyclonal antibodies toward peptides with known nY sites in MnSOD nY-34 and of two adjacent nY in the sarcoplasmic endoplasmic reticulum calcium ATPase (SERCA2 di-nY-294,295) were developed. Kidneys from rats infused with ANG II with known MnSOD nY and aorta from atherosclerotic rabbits and aging rat skeletal and cardiac sarcoplasmic reticulum with known SERCA di-nY were used for positive controls. Staining for MnSOD nY-34 was most intense in distal renal tubules and collecting ducts. Staining of atherosclerotic aorta for SERCA2 di-nY was most intense in atherosclerotic plaques. Aging rat skeletal muscle and atherosclerotic aorta and cardiac atrium from human diabetic patients also stained positively. Staining was decreased by sodium dithionite, which chemically reduces nitrotyrosine to aminotyrosine, and the antigenic nY-peptide blocked staining for each respective nY site but not for the other. As previously demonstrated, immunoblotting failed to detect these modified proteins in whole tissue lysates but did when the proteins were concentrated. Immunohistochemical staining for specific nY-modified tyrosine residues offers the ability to assess the effects of oxidant stress associated with pathological conditions on individual proteins whose function may be affected in specific tissue sites.

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Napoleone, Paolo, Elena Bronzetti, and Francesco Amenta. "Enzyme histochemistry of aging rat kidney." Mechanisms of Ageing and Development 61, no. 2 (December 1991): 187–95. http://dx.doi.org/10.1016/0047-6374(91)90016-s.

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Hanai, T., N. Usuda, T. Morita, and T. Nagata. "Light microscopic lectin histochemistry in aging mouse kidney: study of compositional changes in glycoconjugates." Journal of Histochemistry & Cytochemistry 42, no. 7 (July 1994): 897–906. http://dx.doi.org/10.1177/42.7.8014473.

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We report compositional changes in glycoconjugates in mouse kidney cortex due to aging, as analyzed by lectin histochemistry and Western blot analysis. Mouse kidney tissues of prenatal and postnatal ages (prenatal, 19 days of gestation; postnatal 2 and 8 days, 4 and 13 weeks, and 10 months) were fixed in 4% paraformaldehyde and cryosections were made. They were stained with 16 kinds of biotinylated lectin, followed by ABC, for light microscopy. Tissue homogenate was also examined by Western blotting for WGA, ConA, and Lotus. Changes in glycoconjugates due to prenatal and postnatal aging were detected by both lectin histochemistry and Western blotting.

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Pretlow, T. P., A. S. Lapinsky, L. C. Flowers, R. W. Grane, and T. G. Pretlow. "Enzymatic histochemistry of mouse kidney in plastic." Journal of Histochemistry & Cytochemistry 35, no. 4 (April 1987): 483–87. http://dx.doi.org/10.1177/35.4.2880890.

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Two-micrometer sections of methacrylate-embedded kidney were used to investigate the enzymatic activities of mouse kidney where the proximal tubule and Bowman's capsule from the same corpuscle were viewed in the same section. Alkaline phosphatase, acid phosphatase, 5'-nucleotidase, gamma-glutamyl transpeptidase, N-acetyl-beta-glucosaminidase, leucine aminopeptidase, alpha-naphthyl butyrate esterase, and adenosine triphosphatase activities were observed in the proximal tubule, but only 5'-nucleotidase, alpha-naphthyl butyrate esterase, and alkaline phosphatase were observed in the squamous portion of the parietal epithelium of Bowman's capsule. The use of methacrylate-embedded tissue allowed more precise localization of enzymatic activity than is possible with most frozen sections. This may provide interesting applications not only for characterization of kidney diseases but also for characterization of other normal and abnormal tissues.

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23

Cathro, Helen P., Steven S. Shen, and Luan D. Truong. "Diagnostic histochemistry in medical diseases of the kidney." Seminars in Diagnostic Pathology 35, no. 6 (November 2018): 360–69. http://dx.doi.org/10.1053/j.semdp.2018.10.001.

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24

Nishikawa, M., T. Nakazawa, N. Kanda, E. Aikawa, and H. Toma. "Ultrastructural distribution of steroid sulfatase activity and mRNA in the human kidney." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 1056–57. http://dx.doi.org/10.1017/s0424820100141652.

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Steroid sulfatase (STS) is a microsomal enzyme catalyzing hydrolysis of 3β-hydroxysteroid sulfatases, including dehydroepiandrosterone sulfate, cholesterol and estrogen precursors. STS exists widely in various tissues and is involved in the metabolism of steroid hormones which play a critical role in cell proliferation and may be related to cancer induction in several organ systems. In the kidney, the proximal and distal portions of the nephrons have been suggested as possible sites of synthesis or as target tissues for steroid hormones. However, the presence and the role of STS in the human kidney have not been fully investigated. In this study, we examined the distribution of STS activity and mRNA in human renal tissue by enzyme histochemistry and in situ hybridization at the light and electron microscopic level.Renal tissue specimens were taken from normal areas in the surgically resected kidney from patients with renal cancer. STS activity was analyzed by enzyme histochemistry using 4-methylumbelliferyl sulfate. STS-mRNA distribution was detected by in situ hybridization using an STS cDNA probe cloned from human placenta.

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25

ULRICH, W., R. HORVAT, and K. KRISCH. "Lectin histochemistry of kidney tumours and its pathomorphological relevance." Histopathology 9, no. 10 (April 3, 2007): 1037–50. http://dx.doi.org/10.1111/j.1365-2559.1985.tb02783.x.

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26

Kugler, P. "Demonstration of cathepsin B in the rat kidney using fluorescence histochemistry." Histochemistry 82, no. 3 (1985): 299–300. http://dx.doi.org/10.1007/bf00501409.

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27

Yabuki, Akira, Sawane Mitani, Keijiro Mizukami, and Osamu Yamato. "Nephron segment identification in the normal canine kidney by using lectin histochemistry." Research in Veterinary Science 93, no. 2 (October 2012): 560–64. http://dx.doi.org/10.1016/j.rvsc.2011.12.001.

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28

Yeger, Herman, Reuben Baumal, Patricia Harason, and M. James Phillips. "Lectin Histochemistry of Wilms’ Tumor: Comparison with Normal Adult and Fetal Kidney." American Journal of Clinical Pathology 88, no. 3 (September 1, 1987): 278–85. http://dx.doi.org/10.1093/ajcp/88.3.278.

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29

McAloose, D., M. Casal, D. F. Patterson, and D. M. Dambach. "Polycystic Kidney and Liver Disease in Two Related West Highland White Terrier Litters." Veterinary Pathology 35, no. 1 (January 1998): 77–80. http://dx.doi.org/10.1177/030098589803500110.

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Polycystic kidney and liver disease was present in four of six female and three of five male offspring born in two matings between the same pair of West Highland White Terriers. Clinical signs were apparent and serum biochemistry analysis consistent with liver failure was evident by 5 weeks of age. Affected pups were euthanatized because of their disease. Renal cysts were confirmed to be of collecting duct origin by Dolichos bifluros agglutinin lectin histochemistry, and hepatic cysts were of biliary origin. The clinically unaffected parents were related through multiple common ancestors, and there were no reports of similar disease in related dogs. An autosomal recessive mode of inheritance is therefore suggested. This is the first report of polycystic kidney and liver disease in the West Highland White Terrier. The features of the disease in these pups are similar to those of autosomal recessive polycystic kidney disease (ARPKD) in humans. The West Highland White Terrier may therefore be a potential animal model for ARPKD.

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30

Deng, L. Y., R. Day, and E. L. Schiffrin. "Localization of sites of enhanced expression of endothelin-1 in the kidney of DOCA-salt hypertensive rats." Journal of the American Society of Nephrology 7, no. 8 (August 1996): 1158–64. http://dx.doi.org/10.1681/asn.v781158.

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Although the role of endothelin-1, a potent vasoconstrictor peptide, in hypertension remains unclear, there is evidence of its involvement in deoxycorticosterone acetate (DOCA)-salt hypertensive rats, in which enhanced vascular production of endothelin-1 has been documented. The study presented here examined endothelin-1 gene expression in the kidney in DOCA-salt hypertensive rats by in situ hybridization histochemistry. A high specific activity 35S-labeled complementary RNA probe was used. Significant increases in abundance of endothelin-1 mRNA transcripts were found in the endothelium of renal vessels, and in capillary endothelial and mesangial cells of glomeruli of the remaining kidney of DOCA-salt hypertensive rats, in comparison with unilaterally nephrectomized control rats. Enhanced expression of the endothelin-1 gene in the kidney of DOCA-salt hypertensive rats may participate in abnormalities of renal function in this model of hypertension, and thus contribute to the development and maintenance of elevated blood pressure.

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31

McGuire, D. M., M. D. Gross, R. P. Elde, and J. F. van Pilsum. "Localization of L-arginine-glycine amidinotransferase protein in rat tissues by immunofluorescence microscopy." Journal of Histochemistry & Cytochemistry 34, no. 4 (April 1986): 429–35. http://dx.doi.org/10.1177/34.4.3512696.

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Creatine is a major component of energy metabolism and enzymes involved in its synthesis have therefore been of considerable interest. L-arginine-glycine amidinotransferase, commonly called transamidinase, catalyzes the first reaction in the biosynthesis of creatine. This first reaction is believed to occur in the kidney because of the high concentration of transamidinase in that tissue. Transamidinase activity is also found in many other tissues of the rat, but its role in these tissues is not known. Immunochemical studies with antisera and monoclonal antibodies were used to confirm and refine our understanding of the presence of transamidinase in rat tissues. Immunofluorescence histochemistry was performed to localize transamidinase immunoreactivity within specific tissues including cells in the proximal tubules of the kidney, hepatocytes of the liver, and alpha cells of the pancreatic islet. Immunochemical studies with monoclonal antibodies confirm localization of transamidinase immunoreactivity in the proximal tubules of the kidney. The localization of such immunoreactivity in specialized cells yields insight into possible physiological role(s) of transamidinase in the rat.

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32

Song, Q., D. Z. Wang, R. A. Harley, L. Chao, and J. Chao. "Cellular localization of low-molecular-weight kininogen and bradykinin B2 receptor mRNAs in human kidney." American Journal of Physiology-Renal Physiology 270, no. 6 (June 1, 1996): F919—F926. http://dx.doi.org/10.1152/ajprenal.1996.270.6.f919.

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Kininogen is the precursor of the kinin peptide, which binds to kinin receptors and mediates a broad spectrum of physiological effects. To understand the function of kinin in the kidney, we have identified the cellular localization of the human low-molecular-weight (LMW) kininogen and bradykinin B2 receptor mRNAs in the human kidney by in situ hybridization histochemistry. Kininogen mRNA was found in the juxtaglomerular cells, mesangial areas, epithelium of parietal and visceral (podocytes) layers of Bowman's capsule, proximal and distal tubules, thin and thick segments of Henle's loop, collecting ducts, and the endothelial cells of the blood vessels. B2 receptor mRNA was colocalized with kininogen mRNA in the kidney except the podocytes. The most intense signals were observed in the distal tubules and collecting ducts for both kininogen and B2 receptor mRNAs. No signals were observed in the interstitial cells and macula densa. Control sections did not stain with either the kininogen or B2 receptor sense riboprobe. A Northern blot showed that the expression of LMW kininogen is in the liver and the kidney. Reverse transcription-polymerase chain reaction Southern blot showed expression of B2 receptor mRNA in the endothelial cells, renal proximal tubular cells, and kidney. Our results show the sites of action of kinin in the human kidney and provide further insight into the physiological role of the kallikrein-kinin system on renal function.

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Reid, Philip D., and David Bickar. "Plant anatomy, histochemistry, and gene expression as visualized by tissue printing." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 126–27. http://dx.doi.org/10.1017/s0424820100146473.

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Tissue printing on nitrocellulose membranes followed by localization with appropriate probes has been used to study the distribution of protein and mRNA as well as the timing of gene expression in a variety of plant tissues. Included in these studies are cell wall proteins in soybean and cellulase activity in relation to abscission in kidney bean. Our recent studies have focused on the distribution of enzymes involved in crassulacean acid metabolism in the leaves of various species of Peperomia, the localization of ubiquitinated protein in various plant tissues, and the development of a stain for total protein transferred to nitrocellulose by tissue printing.Tissue prints made on dry nitrocellulose membranes (0.45μm pore size) and viewed with side illumination at low (10X) magnification show the characteristic morphology and anatomical organization of the printed tissue (Figs. 1 and 2). Treatment of the membranes with 12 mM HC1 followed by a two minute incubation in an acidic 0.05% solution of copper phthalocyanine 3,4',4'',4'''-tetrasulfonic acid tetrasodium salt (CPTS) (Figs. 3 and 4) shows the distribution of total protein transferred to the membrane.

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34

Risvanis, J., C. I. Johnston, P. A. Phillips, and L. M. Burrell. "Vasopressin V1a and V2 Receptor mRNA in Deoxycorticosterone Acetate-Salt Hypertension in the Rat." Clinical Science 94, no. 5 (May 1, 1998): 517–23. http://dx.doi.org/10.1042/cs0940517.

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1. Vasopressin V1a and V2 receptors are differentially regulated in deoxycorticosterone acetate-salt hypertension. This paper investigated whether the changes were due to transcription changes in receptor mRNA assessed by in situ hybridization histochemistry (liver V1a receptor) and by reverse transcription—polymerase chain reaction (kidney V1a and V2 receptor). 2. Systolic blood pressure and plasma vasopressin levels were significantly elevated in deoxycorticosterone acetate-salt rats (n = 24) compared with water-control (n = 28) and salt-control rats (n = 28) (P < 0.001). Plasma sodium was elevated in deoxycorticosterone acetate-salt rats compared with both control groups (P < 0.01) and plasma osmolality was elevated in deoxycorticosterone acetate-salt rats compared with water-control rats (P < 0.05). 3. Binding kinetic studies demonstrated downregulation of liver V1a and kidney V2 receptors in deoxycorticosterone acetate-salt rats compared with water-control and salt-control rats (P < 0.05). This was not associated with any change in liver V1a receptor mRNA (P = 0.95), or in kidney V1a (P = 0.79) or V2 receptor mRNA (P = 0.96). 4. In deoxycorticosterone acetate-salt hypertension, downregulation of liver V1a and kidney V2 receptors occurs in the setting of stable vasopressin gene transcription. These results suggest that changes in receptor processing may be responsible for the differential regulation of vasopressin receptors that occurs in deoxycorticosterone acetate-salt hypertension.

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35

Robertson, JC, and JR Hazel. "Elevated 5'-nucleotidase and alkaline phosphodiesterase activities in trout gill localize to endothelial (pillar) cells." Journal of Experimental Biology 201, no. 13 (July 1, 1998): 2011–19. http://dx.doi.org/10.1242/jeb.201.13.2011.

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Tissue homogenates from rainbow trout gill had three- to fivefold higher specific activity for 5'-nucleotidase (5'NT) and more than twofold greater alkaline phosphodiesterase (APD) activity than liver or kidney homogenates. In isolated plasma membranes, gill 5'NT activity was 3-5 times greater than that of the kidney or liver; gill and kidney plasma membranes had similar APD specific activities, both more than five times that of liver. 5'NT and APD activities were localized by histochemistry to the endothelial (pillar) cells of trout gill secondary lamellae. Staining was consistent with the concentration of both activities at the apical plasma membranes of pillar cells (i.e. at the lamellar microvascular surfaces). This localization may reflect a capacity for processing nucleotide metabolites circulating in the blood, perhaps relating to purinergic regulation of local lamellar hemodynamics. There was no histochemical evidence of either 5'NT or APD activity in the gill epithelial (pavement) cells that interface directly with the environment. In contrast, in trout kidney, both enzyme activities localized to the apical region of tubule epithelial cells. The absence of 5'NT and APD activity in pavement cells reinforces the unique structural and functional character of the gill-environment epithelial barrier. The results indicate that 5'NT and APD activities have particular potential application as markers in efforts to isolate and characterize specific gill plasma membrane fractions.

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36

Zemanova, Z., and R. Gossrau. "Light microscopic visualization of transport ATPase in the chick kidney and intestine using catalytic histochemistry." Acta Histochemica 96, no. 3 (September 1994): 325–34. http://dx.doi.org/10.1016/s0065-1281(11)80043-7.

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37

Wijkhuisen, A., F. Djouadi, J. Vilar, C. Merlet-Benichou, and J. Bastin. "Birth-related changes in energy metabolism enzymes and Na-K-ATPase in kidney proximal convoluted tubule cells." American Journal of Physiology-Cell Physiology 272, no. 3 (March 1, 1997): C787—C793. http://dx.doi.org/10.1152/ajpcell.1997.272.3.c787.

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In the proximal convoluted tubule (PCT) of rat kidney, reabsorption is known to take place during fetal life, but no data on Na-K-ATPase and mitochondrial energy metabolism enzymes in this epithelium were available at fetal and neonatal stages. With use of the quantitative histochemistry approach, Na-K-ATPase, citrate synthase (tricarboxylic acid cycle), 3-ketoacid CoA-transferase and thiolase (ketone body oxidation), beta-hydroxyacyl-CoA dehydrogenase (fatty acid oxidation), and acetylcarnitine transferase (acetyl-CoA transport through mitochondrial membrane) were microassayed in PCT and metanephric mesenchyme of fetal and newborn rat kidney. The data indicate that, during fetal life, PCT differentiation involves concomitant increases in Na-K-ATPase and oxidative enzyme activities, supporting the hypothesis that mitochondria could play an active role in cellular ATP turnover when reabsorptive functions develop. Birth resulted in marked increases in the activities of Na-K-ATPase and of fatty acid and ketone body oxidation enzymes in the PCT, whereas no changes in enzyme activities occurred in the metanephric mesenchyme between the fetal and the newborn stage.

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38

Gerrits, P. O., R. W. Horobin, and M. J. Hardonk. "Use of tissue-free glycol methacrylate sections as semi-permeable membranes: a simple way to shorten incubation times and to improve localization in enzyme histochemistry." Journal of Histochemistry & Cytochemistry 37, no. 2 (February 1989): 173–76. http://dx.doi.org/10.1177/37.2.2642939.

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Placing 2-microns sections of tissue-free glycol methacrylate on top of tissue sections is a simple way of forming semipermeable membranes to enhance enzyme histochemical staining. For demonstrating alkaline phosphatase in glycol methacrylate-embedded kidney by a standard azo dye method, such membranes enabled incubation times to be reduced to 1-2 hr, with azo dye reaction product being more crisply localized as compared to sections stained without membranes. Such effects are possible because the membranes are highly permeable to small molecules (e.g., substrate and diazonium salt), slightly permeable to molecules of moderate size (e.g., the final reaction product), and impermeable to large molecules (e.g., alkaline phosphatase and other tissue biopolymers). The implications of these findings for enzyme histochemistry and for enzyme-labeled antibody staining are discussed.

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39

Harris, D. C., Y. C. Tay, J. Chen, L. Chen, and B. J. Nankivell. "Mechanisms of iron-induced proximal tubule injury in rat remnant kidney." American Journal of Physiology-Renal Physiology 269, no. 2 (August 1, 1995): F218—F224. http://dx.doi.org/10.1152/ajprenal.1995.269.2.f218.

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The proposition that proximal tubule (PT) iron accumulation may cause PT injury by lysosomal destabilization or reactive oxygen species generation in human and animal chronic renal disease was examined in partially nephrectomized [remnant kidney (RK)] and sham-operated (SO) Wistar rats. Electron microscopic histochemistry with horseradish peroxidase indicated iron uptake into and release from lysosomes. PT cytoplasmic iron was seen in RK but not in SO by energy-dispersive X-ray spectrometry. Total (9.66 +/- 1.89 vs. 3.30 +/- 0.31 nmol/mg protein; P < 0.01), low-molecular-weight (1.39 +/- 0.09 vs. 0.91 +/- 0.07; P < 0.001), and catalytic iron (1.88 +/- 0.27 vs. 1.28 +/- 0.09; P = 0.05) were higher in RK cytoplasm than in SO. Lysosomal enzyme activity was greater in RK than in SO [e.g., N-acetyl-beta-D-glucosaminidase (NAG): 0.75 +/- 0.05 vs. 0.57 +/- 0.06 mumol p-nitrophenol.h-1.mg protein-1; P < 0.05] and was increased further by chronic iron loading (e.g., RK and NAG: 0.84 +/- 0.04 vs. 0.60 +/- 0.07; P < 0.05). There was no enzymatic evidence of lysosomal fragility, and chronic iron loading of RK decreased fragility as assessed by NAG release (1.36 +/- 0.14 vs. 2.17 +/- 0.14; P < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)

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40

Schlegel, P. N., G. J. Matthews, Z. Cichon, W. K. Aulitzky, C. Y. Cheng, C. L. Chen, L. Saso, M. Goldstein, O. A. Jänne, and C. W. Bardin. "Clusterin production in the obstructed rabbit kidney: correlations with loss of renal function." Journal of the American Society of Nephrology 3, no. 5 (November 1992): 1163–71. http://dx.doi.org/10.1681/asn.v351163.

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Clusterin, a protein associated with cell death, has been suggested as a marker of renal injury. Correlation of clusterin gene expression with changes in renal function and quantitative measurement of clusterin protein levels after ureteral obstruction have not been previously reported. With unilateral ureteral obstruction in rabbits as the experimental model, the time course of alterations in renal function, clusterin mRNA accumulation, and concentrations of clusterin protein in serum, urine, and renal tissue were investigated. RBF, GFR, and renal concentrating ability (percent sodium reabsorption and urine osmolarity) all decreased (P < 0.05) in the obstructed kidney from control values within 1 day of ureteral obstruction. Clusterin mRNA levels started to rise in the ipsilateral kidney within 12 h of ureteral obstruction and increased up to 10-fold above control levels after 3 days of obstruction. Hybridization histochemistry showed that clusterin mRNA was initially detectable in collecting ducts and distal tubules within 12 h of ureteral obstruction. After 7 days of obstruction, increased accumulation of clusterin mRNA was also detectable in proximal tubular epithelial cells. Clusterin gene expression remained elevated in collecting ducts after 60 days of obstruction. Clusterin expression in the contralateral kidney was increased twofold over control values after 12 h of obstruction. No increase in clusterin mRNA accumulation was detectable after 24 h in the contralateral kidney. Total clusterin protein in the obstructed kidney increased from 0.59 +/- 0.66 (mean +/- 1 SD) to 2.5 +/- 1.3 micrograms after 7 days of ureteral obstruction (P < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)

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41

Imaki, Junko, Hidetaka Onodera, Ken Tsuchiya, Toshihiro Imaki, Toshio Mochizuki, Takuya Mishima, Kazuo Yamashita, Kazuhiko Yoshida, and Masaharu Sakai. "Developmental Expression of maf-1 Messenger Ribonucleic Acids in Rat Kidney by in Situ Hybridization Histochemistry." Biochemical and Biophysical Research Communications 272, no. 3 (June 2000): 777–82. http://dx.doi.org/10.1006/bbrc.2000.2865.

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42

Huang, Z., W. You, R. P. Haugland, V. B. Paragas, N. A. Olson, and R. P. Haugland. "A novel fluorogenic substrate for detecting alkaline phosphatase activity in situ." Journal of Histochemistry & Cytochemistry 41, no. 2 (February 1993): 313–17. http://dx.doi.org/10.1177/41.2.8419466.

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We describe here the in situ detection of alkaline phosphatase (APase) activity with a new fluorogenic substrate, 2-(5'-chloro-2'-phosphoryloxyphenyl)-6-chloro-4-(3H)-quinazolinone (CPPCQ). CPPCQ is very soluble and colorless. APase converts it into a rapidly precipitating product, whose strong fluorescence marks the sites of APase activity. The detected APase was either a probing enzyme anchored to epidermal growth factor (EGF) receptors of fixed human epidermoid carcinoma cell line (A431) by biotinylated EGF and streptavidin-APase conjugates or an endogenous marker existing in a fixed canine kidney cell line (MDCK). With CPPCQ staining, the EGF receptors and the endogenous APase were both visualized by fluorescence microscopy as contrasting, photostable, and well-resolved fluorescent stains. The EGF receptor staining was specific since it could be blocked by excessive unlabeled EGF. In contrast, fluorescein-labeled EGF failed to specifically stain the EGF receptors under the same fluorescent microscope. The endogenous APase staining with CPPCQ was sensitive to heating, levamisole and L-homoarginine, showing an APase tissue specificity of the liver/bone/kidney type. Therefore, CPPCQ appears to be a novel substrate dye for sensitive fluorescence APase histochemistry.

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43

Morsy, Fatma A., Manal A. Badawy, and Abdel Razik H. Farrag. "The Protective Effect of Melatonin against Fumonisin-Induced Renal Damage in Rats." International Journal of Toxicology 25, no. 6 (November 2006): 523–29. http://dx.doi.org/10.1080/10915810600961648.

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The present study was designed to investigate the potential protective effect of melatonin against the renal toxicity of fumonisin in female rats. Six groups of animals were used in this study. The first group served as control. The second group was given melatonin only at a dose level of 10 mg/kg. The third group was fed ration contaminated with fumonisin (100 mg/kg diet). The fourth group was fed ration contaminated with fumonisin (200 mg/kg diet). The fifth group was given daily interperitoneal injection (IP) 10 mg/kg melatonin and fed ration contaminated with fumonisin (100 mg/kg diet). The sixth group was given daily interperitoneal injection of 10 mg/kg melatonin and fed ration contaminated with fumonisin (200 mg/kg diet). The rats were treated for 1 month. Histopathological and histochemical changes in the kidney were investigated. In addition, DNA ploidy was measured in the kidney. Fumonisin administration (100 or 200 mg/Kg diet) to unpretreated control rats caused extensive renal damage as evaluated by histopathology, histochemistry, and/or DNA ploidy measurement. No apparent changes following administration of melatonin. Melatonin coadministration to the fumonisin-administered rats reduced kidney damage and the tissues appeared more or less like the normal. The present study indicates that melatonin has a protective effect in fumonisin-induced renal damage.

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44

Van Riel, D., J. M. A. Van Den Brand, V. J. Munster, T. M. Besteboer, R. A. M. Fouchier, A. D. M. E. Osterhaus, and T. Kuiken. "Pathology and Virus Distribution in Chickens Naturally Infected with Highly Pathogenic Avian Influenza A Virus (H7N7) During the 2003 Outbreak in The Netherlands." Veterinary Pathology 46, no. 5 (May 9, 2009): 971–76. http://dx.doi.org/10.1354/vp.08-vp-0215-k-bc.

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The largest recorded outbreak of highly pathogenic avian influenza virus of the subtype H7N7 occurred in the Netherlands in 2003. We describe the immunohistochemical and histopathologic findings of 3 chickens naturally infected during this outbreak. Influenza virus antigen occurred in endothelial cells and mononuclear cells of all tissues examined and occurred in parenchymal cells of heart, lung, kidney, pancreas, and trachea, often associated with multifocal inflammation and necrosis. These findings are consistent with the acute stage of highly pathogenic avian influenza from other subtypes. In the severely edematous wattle skin, most endothelial cells contained virus antigen, while in all other tissues virus antigen was only detected in a few endothelial cells. Virus histochemistry showed that this H7N7 virus attached to more endothelial cells in wattle skin than in other vascular beds. This might explain, at least partly, the tropism of the virus and the associated severity of lesions in this tissue.

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Lka, Jn, Jn Jakubovsk, Mria Ruikov, Eva Surmkov, and Milan Zaviai. "The use of lectins identified with specific antibodies in lectin histochemistry of NZB/W F1 mouse kidney." Acta Histochemica 94, no. 2 (May 1993): 185–88. http://dx.doi.org/10.1016/s0065-1281(11)80373-9.

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46

Fu, P., P.-J. Shen, C.-X. Zhao, D. J. Scott, C. S. Samuel, J. D. Wade, G. W. Tregear, R. A. D. Bathgate, and A. L. Gundlach. "Leucine-rich repeat-containing G-protein-coupled receptor 8 in mature glomeruli of developing and adult rat kidney and inhibition by insulin-like peptide-3 of glomerular cell proliferation." Journal of Endocrinology 189, no. 2 (May 2006): 397–408. http://dx.doi.org/10.1677/joe.1.06697.

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Leucine-rich repeat-containing G-protein-coupled receptor 8 (LGR8, or RXFP2) is a member of the type C leucine-rich repeat-containing G protein-coupled receptor family, and its endogenous ligand is insulin-like peptide-3 (INSL3). Although LGR8 expression has been demonstrated in various human tissues, including testis, ovary, brain and kidney, the precise roles of this receptor in many of these tissues are unknown. In an effort to better understand INSL3–LGR8 systems in the rat, we cloned the full-length Lgr8 cDNA and investigated the presence and cellular localization of Lgr8 mRNA expression in adult and developing rat kidney. On the basis of these findings, we investigated the presence and distribution of renal 125I-labelled human INSL3-binding sites and the nature of INSL3–LGR8 signalling in cultured renal cells. Thus, using in situ hybridization histochemistry, cells expressing Lgr8 mRNA were observed in glomeruli of renal cortex from adult rats and were tentatively identified as mesangial cells. Quantitative, real-time PCR analysis of the developmental profile of Lgr8 mRNA expression in kidney revealed highest relative levels at late stage gestation (embryonic day 18), with a sharp decrease after birth and lowest levels in the adult. During development, silver grains associated with Lgr8 mRNA hybridization were observed overlying putative mesangial cells in mature glomeruli, with little or no signal associated with less-mature glomeruli. In adult and developing kidney, specific 125I-INSL3-binding sites were associated with glomeruli throughout the renal cortex. In primary cultures of glomerular cells, synthetic human INSL3 specifically and dose-dependently inhibited cell proliferation over a 48 h period, further suggesting the presence of functional LGR8 (receptors) on these cells (mesangial and others). These findings suggest INSL3–LGR8 signalling may be involved in the genesis and/or developmental maturation of renal glomeruli and possibly in regulating mesangial cell density in adult rat kidney.

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47

Damkier, Helle Hasager, Søren Nielsen, and Jeppe Praetorius. "Molecular expression of SLC4-derived Na+-dependent anion transporters in selected human tissues." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 293, no. 5 (November 2007): R2136—R2146. http://dx.doi.org/10.1152/ajpregu.00356.2007.

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NaHCO3 transporters are involved in maintenance of intracellular pH and transepithelial HCO3− movement in many rodent tissues. To establish the human relevance of the many investigations on rodents, this study aimed to map these transporters and a related polypeptide, NaBC1 [solute carrier 4 (SLC4)A11], to several human tissues by using PCR on reverse transcribed human mRNA and immunoperoxidase histochemistry. The mRNA encoding the electroneutral Na+:HCO3− cotransporter (NBCe1; SLC4A4), was expressed in renal cortex, renal medulla, stomach, duodenum, jejunum, ileum, colon, pancreas, choroid plexus, cerebellum, cerebrum, and hippocampus. NBCe2 (SLC4A5) and NBCn1 (SLC4A7) mRNAs were mainly found in kidney and brain tissues, as was mRNA encoding the Na+-dependent anion exchangers NCBE (SLC4A10) and NDCBE1 (SLC4A8). In addition to previous findings, NBCn1 protein was localized to human renal medullary thick ascending limbs and duodenal epithelial villus cells and NBCe2 protein to renal collecting ducts. Finally, the message encoding NaBC1 was found in kidney, stomach, duodenum, pancreas, and brain, and the corresponding protein in the anterior and posterior corneal epithelia, renal corpuscules, proximal tubules, collecting ducts, pancreatic ducts, and the choroid plexus epithelium. In conclusion, the selected human tissues display distinct expression patterns of HCO3− transporters, which closely resemble that of rodent tissues.

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Pekkarinen, M. "Scanning electron microscopy, whole-mount histology, and histochemistry of two anodontine glochidia (Bivalvia: Unionidae)." Canadian Journal of Zoology 74, no. 11 (November 1, 1996): 1964–73. http://dx.doi.org/10.1139/z96-223.

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Intramarsupial glochidia of Anodonta anatina (L.) and Pseudanodonta complanata (Rossmässler) were studied in southern Finland. Material staining positively with periodic acid – Schiff's reagent (PAS), neutral lipid reserves, and acid phosphatase activity have different distributions in the mantle of the two species. Moreover, the mucous covering of the mantle of the two glochidia behaves differently on critical-point drying. The presence of microvilli with alkaline phosphatase activity on the mantle surface and acid phosphatase activity in the mantle cells in both glochidia suggest that the mantle plays a role in nutrient uptake and digestion and possibly also in electrolyte uptake. The primordia of the stomach, digestive diverticula, and intestine, at least in A. anatina glochidia, contain neutral lipids and exhibit acid phosphatase activity: In A. anatina glochidia, a microvillous layer with alkaline phosphatase activity continues from the ventral walls of the lateral pits to the suspected kidney diverticula. In both glochidia, there may be three pairs of rudimentary ganglia, which do not stain with methylene blue. The eight ciliated sense organs of the glochidia are methylene blue- and PAS-positive and they exhibit succinate dehydrogenase and acid phosphatase activity. In each mantle lobe, the enveloping cell of the dorsal ciliary organ is interconnected with those of the ventral triad via a cellular fold or "tract," and the ciliated central cells of the organs send axons towards each other.

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McWilliams, Thomas G., Alan R. Prescott, George F. G. Allen, Jevgenia Tamjar, Michael J. Munson, Calum Thomson, Miratul M. K. Muqit, and Ian G. Ganley. "mito-QC illuminates mitophagy and mitochondrial architecture in vivo." Journal of Cell Biology 214, no. 3 (July 25, 2016): 333–45. http://dx.doi.org/10.1083/jcb.201603039.

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Autophagic turnover of mitochondria, termed mitophagy, is proposed to be an essential quality-control (QC) mechanism of pathophysiological relevance in mammals. However, if and how mitophagy proceeds within specific cellular subtypes in vivo remains unclear, largely because of a lack of tractable tools and models. To address this, we have developed “mito-QC,” a transgenic mouse with a pH-sensitive fluorescent mitochondrial signal. This allows the assessment of mitophagy and mitochondrial architecture in vivo. Using confocal microscopy, we demonstrate that mito-QC is compatible with classical and contemporary techniques in histochemistry and allows unambiguous in vivo detection of mitophagy and mitochondrial morphology at single-cell resolution within multiple organ systems. Strikingly, our model uncovers highly enriched and differential zones of mitophagy in the developing heart and within specific cells of the adult kidney. mito-QC is an experimentally advantageous tool of broad relevance to cell biology researchers within both discovery-based and translational research communities.

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Matsumoto, T., C. A. Winkler, L. P. Brion, and G. J. Schwartz. "Expression of acid-base-related proteins in mesonephric kidney of the rabbit." American Journal of Physiology-Renal Physiology 267, no. 6 (December 1, 1994): F987—F997. http://dx.doi.org/10.1152/ajprenal.1994.267.6.f987.

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The mesonephric kidney, precursor to the metanephric kidney, comprises 30-50 nephrons, each with a glomerulus and proximal, distal, and collecting tubules. Although two different cell types have been identified in the mesonephric collecting tubule, no relationship to cells of the metanephric collecting duct has been established. To characterize expression of some of the acid-base-related proteins, we assayed for carbonic anhydrase (CA) activity and performed immunocytochemistry in mesonephroi from 15- to 20-day-old fetal rabbits. From total RNA, we detected expression of CA II and CA IV mRNA. Microdissected proximal and collecting tubules abundantly expressed both CA II and CA IV, at least to the extent observed in mature metanephric proximal tubules and collecting ducts. Histochemistry confirmed the expression of CA activity in these segments; in the collecting tubule, 28% of the collecting tubule cells were CA rich. Most CA-rich cells showed apical H(+)-ATPase and basolateral band 3 anion exchanger staining consistent with the findings in mature H(+)-secreting (alpha) intercalated cells of the metanephric collecting duct. CA-negative cells could be labeled with an antibody that identifies mature metanephric principal cells. Thus the mesonephric collecting tubule has many cells resembling mature alpha-intercalated cells and a majority of cells resembling principal cells. The similarity to the metanephric collecting duct suggests that the lineages of metanephric alpha-intercalated and principal cells may be closely related to those of the mesonephros.

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Journal articles on the topic 'Kidneys – Histochemistry'

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