Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P41181 (collecting duct)
 5,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We investigated the diversity of cellular localization of the GLUT-1 glucose transporter protein at epithelial and endothelial barriers either possessing or lacking occluding junctions. The avidin-biotin immunoperoxidase and the immunogold-silver staining (IGSS) techniques were used. A rabbit polyclonal antiserum prepared against a synthetic peptide encoding the 13 amino acids at the carboxyl terminus of the GLUT-1 glucose transporter protein was used. Both techniques were found to have comparable sensitivity in detecting immunoreactive GLUT-1. The IGSS experiments employed a light-insensitive stabilizer, and no immunoreactive GLUT-1 was found in brain cells (neurons, glial cells), but abundant immunoreactive GLUT-1 was found in brain capillary endothelium, which is composed of cells with occluding junctions. However, immunoreactive GLUT-1 was also found in endothelium known not to contain occluding junctions, such as testicular microvascular endothelium and endothelium on the fetal side of the syncytiotrophoblast of the placenta. In epithelial barriers, GLUT-1 was also found in the basolateral membrane of renal collecting duct epithelium, choroid plexus, and the placental syncytiotrophoblast layer. However, immunoreactive GLUT-1 was found in the apical membrane of ependymal epithelium near the lower portion of the third ventricle. In conclusion, there is diversity underlying the expression of the GLUT-1 glucose transporter protein in different cell types, and the transporter protein can be found in endothelium with and without occluding junctions, and in both apical and basolateral membranes of epithelial barriers.
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PMID:GLUT-1 glucose transporter is present within apical and basolateral membranes of brain epithelial interfaces and in microvascular endothelia with and without tight junctions. 155 63

1,25-dihydroxyvitamin D3 [1,25(OH)2D3] binding sites were studied along the nephron of rats. The animals were pretreated with the diphosphonate EHDP at doses that inhibit the endogenous production of 1,25(OH)2D3. A dry film autoradiographic technique was applied to tubular segments isolated by microdissection from kidneys incubated in vitro with various concentrations (0.2-12 nM) of [3H]1,25(OH)2D3 in the presence or absence of an excess unlabeled hormone (X200) in order to determine specific binding. Total, nonspecific, and specific labeling were quantified by silver grain counting over cytoplasmic and nuclear areas. Specific nuclear labeling appeared in the cortical ascending limb and papillary collecting tubule at 1 nM. In the distal tubule and, to a lesser extent, in the cortical collecting tubule a specific nuclear labeling was also present, but only at higher concentrations. No specific nuclear labeling was detected in the proximal tubule. All along the nephron, a significant and nonspecific labeling was observed in the cytoplasm, either alone or superimposed over the specific nuclear labeling. In conclusion 1,25(OH)2D3 specific binding sites appear to be localized mainly in the cortical ascending limb of the loop of Henle, in the distal and cortical collecting duct, and in the papillary collecting duct.
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PMID:1,25(OH)2D3 binding along the rat nephron: autoradiographic study in isolated tubular segments. 383 21

Gentamicin is a nephrotoxic antibiotic of the aminoglycoside group, which accumulates within the renal cortex. The present study is an attempt to localize precisely the sites of gentamicin accumulation along isolated tubular segments. We performed autoradiography of 3 H-gentamicin (3H-G) uptake on isolated tubules from kidneys of 6 rabbits previously treated by a single dose of this drug (125 muCi/kg of body wt; 140 microgram/kg of body wt). Isolated tubules were obtained by microdissection following collagenase incubation, 4 hours after 3H-G administration. Autoradiography of single isolated tubular segments was performed according to a dry-film technique. Results were as follows. Almost no gentamicin incorporation (less than 2 silver grains per 150 micrometer2) takes place along the distal parts of the nephron, from the beginning of the loop of Henle to the end of the medullary collecting duct. No differences were visible along these parts of the nephron, whatever their localization, cortical or medullary, In the proximal tubule (PT), we observed a gradual regular increase in 3H-G accumulation, from the glomerulus to the end of the pars recta. The silver grain density progressively increased along this structure from the very early PT (5 per 150 micrometer2) to the last millimeter of the pars recta (40 per 150 micrometers). No clear difference between superficial and juxtamedullary nephrons was detected. The possible mechanisms that could account for this observed variation in 3H-G cellular uptake along the PT are discussed.
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PMID:Gentamicin incorporation along the nephron: autoradiographic study on isolated tubules. 724 87

The vitamin D-receptor protein and its mRNA were localized in microscope sections of paraffin-embedded mammalian kidneys by means of immunocytochemistry and in situ hybridization, respectively. A monoclonal antibody against chicken intestinal vitamin D receptor immunostained the nucleus and cytoplasm of cells within the distal convoluted tubule, connecting segment, and initial cortical collecting duct of both rats and pigs. Although fainter, immunostaining also was present over proximal tubular cells. (35S)UTP-labeled cRNA probes were detected over both the proximal and distal portions of the mouse nephron, but silver grain densities were 5.8-fold greater over the latter. In conclusion, localization of both the vitamin D-receptor protein and its mRNA in both the proximal and distal nephron of adult mammals suggests that the gene for this protein is expressed in cells at both of these sites. The intensity of immunostaining and the density of cRNA-associated silver grains suggest that vitamin D-receptor gene expression is greatest in the distal nephron.
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PMID:Vitamin D receptor gene expression in mammalian kidney. 787 36

Structurally and functionally distinct populations of intercalated cells have been described in the collecting duct of both rat and rabbit. However, little is known about these cells in the mouse kidney. The study presented here examines ultrastructural and immunological characteristics of different types of intercalated cells in the mouse. Kidneys of two strains of normal female mice, C57BL/6 and IBR, were preserved by in vivo perfusion with 1% glutaraldehyde or paraformaldehyde-picric acid fixatives and processed for morphological evaluation or light and electron microscopic immunohistochemistry, respectively. The avidin-biotin-horseradish peroxidase procedure was performed on was sections using antibodies against carbonic anhydrase II, H+ -ATPase and Band 3 protein. Immunogold cytochemistry was performed on Lowicryl sections using antibodies to H+ -ATPase and Band 3 protein. Colocalization of H+ -ATPase and Band 3 protein was performed by double labeling using an immunogold technique with silver enhancement. Intercalated cells identified by positive staining for H+ -ATPase and carbonic anhydrase II constituted 35% to 40% of all cells in the connecting tubule (CNT), cortical collecting duct (CCD), and outer medullary collecting duct (OMCD). Type A intercalated cells identified by positive Band 3 staining constituted 16%, 24%, and 33% of the total cell population in the CNT, CCD, and OMCD, respectively. Electron microscopy and immunogold cytochemistry demonstrated three distinct populations of intercalated cells. Type A intercalated cells with apical H+ -ATPase and basolateral Band 3 immunoreactivity were present in all segments examined, and had prominent apical microprojections and characteristic tubulovesicular structures beneath the apical surface, both coated with studs on the cytoplasmic face. Type B intercalated cells with basolateral and cytoplasmic H+-ATPase and no Band 3 immunoreactivity were most frequently observed in the initial collecting tubule, but were present also in the CNT and early CCD. Type B intercalated cells had a fairly smooth apical surface, a gray zone free of organelles beneath the apical plasma membrane, and small cytoplasmic vesicles without studs throughout the cell. A third type of intercalated cell with apical and cytoplasmic H+-ATPase, but no basolateral Band 3 protein, was observed exclusively in the CNT and the initial collecting tubule. This type of cell was large, with numerous mitochondria, and vesicles coated with studs were present throughout the cell. It resembled a third type of intercalated cell described previously in the rat. It is concluded that three morphologically and immunologically distinct types of intercalated cells are present in the mouse kidney.
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PMID:Identification of distinct subpopulations of intercalated cells in the mouse collecting duct. 878 96

The cellular localization of endothelin receptors in the inner medulla of the rat kidney was investigated by using high resolution light and electron microscopic autoradiography, with the microwave irradiation fixation methods. Kidney slices were incubated with 125I-endothelin-1 alone or with selective ligands for the endothelin ETB and/or ETA receptors for light microscopic autoradiography. At the microscopic level, 125I-endothelin-1 was found to bind specifically to the glomeruli, arterioles and peritubular spaces in the cortex and vasa recta and surrounding tissues in the inner medulla. These bindings were also observed when the tissue slices were incubated in the presence of IRL1620 (ETB receptor agonist) or 97-139 (ETA receptor antagonist). Electron microscopic autoradiography using 125I-endothelin-1 in the inner medulla revealed silver grains over endothelial cells of the vasa recta and interstitial and collecting duct cells. No grains were detected over inner lining cells of the thin limbs of Henle's loop. These interstitial cells contained abundant microorganelles and lipid droplets, and had extensive cytoplasmic processes that closely related to the basement membranes of the vasa recta and loop of Henle. These findings demonstrate that type 1 interstitial cells are also primary sites for endothelin receptors as well as endothelial cells of the vasa recta and collecting duct cells in the inner medulla.
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PMID:High resolution localization of endothelin receptors in rat renal medulla. 880 82

Morphological study of the kidney is generally the first step in the diagnosis of Alport's syndrome. Light microscopy study allows to suggest the diagnosis with the association of focal and segmental glomerulosclerosis, GBM anomalies when studied with silver staining, interstitial foam cells, and negative standard immunofluorescence study. GBM anomalies observed by electron microscopy are nearly specific with thickening splitting and fragmenting of the lamina densa. GBM anomalies are the consequence of a collagen IV disease. Thus, immunohistochemical results obtained with 6 different alpha(IV) are essential and allow to evaluate the mode of inheritance. Schematically, in the X dominant AS form, GBM, distal tubular BM and collecting duct BM do not express alpha3/alpha4, alpha5(IV). In the autosomic recessive AS form, collecting duct BM alone express alpha5(IV) without expression of alpha3(IV) and alpha5(IV) chains along the GBM and distal TBM.
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PMID:Renal pathology and ultrastructural findings in Alport's syndrome. 1110 62

The aim of this study was to assess cellular proliferation using silver-stained nucleolar organizer regions (AgNOR) and the proliferating cell nuclear antigen (PCNA) in various tissues in the prostate of ram lambs implanted with increasing zeranol doses and to compare the sensitivity of different tissues of lamb prostate to zeranol. Twenty-four Akkaraman lambs were implanted with increasing zeranol doses, including 12 mg (n = 8), 24 mg (n = 8) and 96 mg (n = 8), with eight lambs serving as controls. After 33 days, the prostate tissues of the lambs were stained using AgNOR and PCNA techniques. The prostate tissues were divided into two compartments--the epithelial tissues, including glandular acinus, collecting duct and penile urethra, and the non-epithelial tissues, including interstitial tissue and striated muscle. AgNOR dots and PCNA index on each prostatic tissue were counted under a light microscope and were evaluated statistically. AgNOR staining in the treatment groups showed a higher score in the non-epithelial tissues than the epithelial components, whereas the PCNA index was significant in the epithelial tissues and non-epithelial tissues had very low PCNA immunostaining. According to the PCNA index, collecting duct epithelium showed more sensitivity to increasing zeranol doses and according to AgNOR counts, there was no difference of sensitivity to zeranol among tissues of the same origin. Both AgNOR counts and PCNA indexes seem to be valuable proliferating markers for the epithelial components of ram prostate, but PCNA index had no significance in relation to the non-epithelial components in contrast to AgNOR counts. Therefore, the controversial results arising from the combined use of both techniques as proliferating markers for the ram prostate should be considered in further studies.
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PMID:Assessment of proliferative activity by AgNOR and PCNA in prostatic tissues of ram lambs implanted with zeranol. 1614 54

Here we present a detailed morphological description of the alligator (Alligator mississippiensis) kidney and nephron. We present a series of histological, histochemical, and immunohistochemical markers that clearly define the seven regions of the alligator nephron. The alligator kidney is composed of many paired (mirrored) lobules on each kidney (lobe). Single nephrons span the width of lobules three times. The fine structure of glomeruli, lying in rows spanning the height of the lobule, is resolved by periodic acid methionine silver (PAMS) and periodic acid Schiff's (PAS) histochemistry. Glomeruli are connected to the proximal tubule (PT) via a neck segment. The PT is alcian blue-negative, making it distinct from the distal tubule (DT), connecting segment (CS), and collecting duct (CD). The PT is clearly identifiable by a PAS-positive brush border membrane. The PT is connected to the DT via an intermediate segment (IS) that makes a 180 degrees turn to connect these tubules. PAMS-positive material is found in the lumens of the PT, IS, and DT. Also, PAMS-positive granules are found in the DT, CS, and CD. Immunolocalization of the Na(+), K(+)-ATPase to the basolateral membrane of the DT, CS, and CD suggests a role of this enzyme in driving primary and secondary transport processes in these segments, including bicarbonate transport into the lumen of the DT (leading to an alkaline urine). Through the techniques described here, we have identified a series of distinct markers to be used by pathologists, veterinarians, and researchers to easily identify alligator nephron segments. Anat Rec, 2009. (c) 2009 Wiley-Liss, Inc.
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PMID:Morphology and histochemistry of juvenile American alligator (Alligator mississippiensis) nephrons. 1968 9