Lectin staining of renal tubules in normal kidney

Engel, Uwe; Breborowicz, D; Bøg-Hansen, T.C.; Francis, Dorthe

doi:10.1111/j.1699-0463.1997.tb00536.x

Cited by 17 publications

(19 citation statements)

References 4 publications

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“…N-cadherin staining was located at the lateral and basolateral borders of the cells with intense punctate staining at the sub-apical junctional complex region of cells, whereas L. tetragonolobus strongly stained the apical regions and luminal material in the tubules. E-cadherin staining was strongly positive in tubules that correlated with reactivity to the antigen recognized by D. biflorus lectin, which is found in the thick ascending limb (TAL) of the Loop of Henle [26] and a subset of cells in the distal tubule and collecting duct (Figure 1B and D, arrows). E-cadherin staining appeared weak or absent in tubules that corresponded to those clearly positive for L. tetragonolobus and N-cadherin (Figure 1A–C, asterisks).…”

Section: Resultsmentioning

confidence: 99%

“…Discrimination with calbindin and aquaporin-2 staining [37] indicated that claudin-1, -3, -4, -7 and -8 were present in distal convoluted tubule and collecting duct, whereas claudin-14 could only be confidently confirmed in the distal convoluted tubule. Together, THP, calbindin and aquaporin-2 provided superior TAL, distal tubule and collecting duct markers than the D. biflorus lectin, which was found to give very heterogeneous staining in the TAL, reducing in intensity in more distal structures [26]. …”

Section: Discussionmentioning

confidence: 99%

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Differential expression of claudin tight junction proteins in the human cortical nephron

Kirk

Campbell

Bass

et al. 2010

Nephrology Dialysis Transplantation

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Background. In renal tubules, paracellular permeability is tightly controlled to facilitate solute absorption and urinary concentration and is regulated by tight junctions, which incorporate claudin proteins. There is very limited information confirming the localization of these proteins in the human renal cortex. Most data is inferred from mouse, bovine and rabbit studies and differences exist between mouse and other species.Methods. A survey of claudin staining was performed on human kidney cortex embedded in glycolmethacrylate resin to enhance tissue morphology and facilitate the cutting of 2 µm serial sections.Results. Claudin-2, -10 and -11 antibodies labelled renal tubular epithelial cells, correlating with Lotus tetragonolobus and N-cadherin positive proximal tubules. Claudin-3, -10, -11 and -16 antibodies strongly stained a population of tubules that were positive for Tamm Horsfall protein on adjacent sections, confirming expression in the thick ascending limb of the Loop of Henle. Claudin-3, -4 and -8 antibodies reacted with tubules that correlated with the distal nephron markers, E-cadherin, epithelial membrane antigen and Dolichos biflorus and claudin-3, -4, -7 and -8 with the distal tubule marker, calbindin, and the collecting duct marker, aquaporin-2. Claudin-14 was localized in distal convoluted tubules, correlating positively with calbindin but negatively with aquaporin-2, whereas claudin-1 staining was identified in the parietal epithelium of Bowman's capsule, distal convoluted tubule and collecting duct. Cellular and tight junction localization of claudin staining in renal tubules was heterogeneous and is discussed.Conclusions. Complex variation in the expression of human claudins likely determines paracellular permeability in the kidney. Altered claudin expression may influence pathologies involving abnormalities of absorption.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Differential expression of claudin tight junction proteins in the human cortical nephron

Kirk

Campbell

Bass

et al. 2010

Nephrology Dialysis Transplantation

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“…Lectins with different carbohydrates specificities were able to bind distinct renal cells (Holthofer 1983;Murata et al 1983). It has been demonstrated that jacalin, a galactosebinding lectin, strongly binds to renal cells of the distal convoluted tubules and collecting ducts, but does not bind to the cells of proximal convoluted tubules (Engel et al 1997).…”

Section: Resultsmentioning

confidence: 99%

Renal effects induced by the lectin from Vatairea macrocarpa seeds

Monteiro

Havt

Barbosa

et al. 2005

Journal of Pharmacy and Pharmacology

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Lectins are glycoproteins that interact reversibly and specifically with carbohydrates. The renal effects of the galactose-binding lectin from the seeds of Vatairea macrocarpa were investigated. Isolated kidneys from Wistar rats (240-280 g) were perfused with Krebs-Henseleit solution containing 6% bovine serum albumin. The V. macrocarpa lectin (10 microg mL(-1)) increased the perfusion pressure, renal vascular resistance, urinary flow and glomerular filtration rate. However, V. macrocarpa lectin did not change the percentage sodium, potassium or chloride tubular transport. Pre-treatment with lectin-galactose complex significantly blocked the increase in perfusion pressure, renal vascular resistance, urinary flow and glomerular filtration rate. The control group showed a small amount of a proteinaceous material in the urinary space, although no alteration in the renal tubules was detected. The administration of galactose alone did not modify the functional parameters of the kidney. Kidneys perfused with V. macrocarpa lectin showed moderate deposits of a proteinaceous material in the tubules and urinary space. Those pre-treated with lectin-galactose complex had only small amount of a proteinaceous material in the urinary space. No abnormalities were seen in renal tubules. The results suggest that lectin from V. macrocarpa seeds has important effects on the carbohydrate-binding sites of the renal system, given the reversal of renal effects with the use of that specific inhibitor.

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“…All antibodies were diluted in blocking buVer and washed from glass slides with PBS. In addition, kidneys were stained with Xuorescently labeled peanut agglutinin (PNA, Vector Laboratories, Burlingame, CA, USA), which labels distal tubules in human kidney (Engel et al 1997), or rhodaminephalloidin to visualize the actin cytoskeleton. Nuclei were labeled with DAPI (4Ј,6-diamidino-2-phenylindole) diluted in PBS.…”

Section: Cell Culture and Atp Depletionmentioning

confidence: 99%

N-cadherin is depleted from proximal tubules in experimental and human acute kidney injury

Nürnberger

Feldkamp

Kavapurackal

et al. 2010

Histochem Cell Biol

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Ischemia remains the most common cause of acute kidney injury (AKI). Decreased intercellular adhesion and alterations in adhesion molecules may contribute to the loss of renal function observed in AKI. In the present study, we evaluated the distribution of adhesion molecules in the human kidney and analyzed their expression in human and experimental AKI. Specimens of human kidneys obtained from patients with and without AKI were stained for the cell adhesion molecules E-cadherin, N-cadherin and beta-catenin. Experimental AKI in rats was induced by renal artery clamping. Immunostaining and immunoblotting were carried out for E-cadherin, N-cadherin and beta-catenin. Proximal tubule cells from opossum kidneys (OKs) were used to analyze the effect of chemical hypoxia (ATP depletion) in vitro. In the adult human kidney, N-cadherin was expressed in proximal tubules, while E-cadherin was expressed in other nephron segments. beta-Catenin was expressed in both proximal and distal tubules. In human AKI and in ischemic rat kidneys, N-cadherin immunostaining was depleted from proximal tubules. There was no change in E-cadherin or beta-catenin. In vitro, OK cells expressed N-cadherin only in the presence of collagen, and ATP depletion led to a depletion of N-cadherin. Collagen IV staining was reduced in ischemic rat kidneys compared to controls. The results of the study suggest that N-cadherin may play a significant role in human and experimental AKI.

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Lectin staining of renal tubules in normal kidney

Cited by 17 publications

References 4 publications

Differential expression of claudin tight junction proteins in the human cortical nephron

Differential expression of claudin tight junction proteins in the human cortical nephron

Renal effects induced by the lectin from Vatairea macrocarpa seeds

N-cadherin is depleted from proximal tubules in experimental and human acute kidney injury

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