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)

Distribution of lectin-binding sites in adult and developing mouse kidney was studied with fluorochrome- and peroxidase-coupled lectins. Effects of fixation methods on lectin-binding patterns were also compared. Un-induced mesenchymal cells and ureter bud of the early metanephros reacted with Concanavalin A, Lens culinaris, Ricinus communis I, and wheat germ agglutinins, whereas binding sites for both soybean and peanut (PNA) agglutinins were seen only in ureter bud tissue. On induction, PNA positivity rapidly appeared in the induced, condensed areas of the metanephrogenic mesenchyme. Early glomeruli expressed heterogeneously terminal galactosyl and N-acetylgalactosaminyl moieties in the podocytes. Later, these sites disappeared and were apparently covered by sialic acids. Endothelia also displayed a comparable sialylation of terminal saccharide moieties during maturation. Binding sites for many of the above lectins were also found in the developing proximal and distal tubules. Terminal fucosyl residues, characteristic of mature proximal tubules, appeared during day 13 of development. Dolichos biflorus agglutinin reactivity, typically seen in the collecting ducts, appeared by day 13. Griffonia simplicifolia-I-B4 isolectin reactivity was exclusively localized to endothelial in adult kidney cortex, but in embryonic kidneys reactivity with collecting duct and podocytes was also seen. These results suggest that the compartmentalized expression of cell glycoconjugates in adult mouse kidney is acquired in a sequential manner during development. Such sequential appearance of the mature glycosylation pattern probably reflects functional maturation of the nephron.
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PMID:Changes in the glycosylation pattern during embryonic development of mouse kidney as revealed with lectin conjugates. 379 9

The lectin-gold technique was used to detect Helix pomatia and Dolichos biflorus lectin binding sites directly on semithin and thin sections of rat kidney collecting ducts. Intercalated cell apical plasma membranes and the membranes of apical cytoplasmic vesicles were heavily labeled in the cortex and outer stripe of the outer medulla but were negative or very weakly labeled in the inner stripe and inner medulla. In contrast, clear cell apical membranes were labeled along the entire length of the collecting duct. Double labeling of semithin cryostat sections with a specific antibody and lectin-gold complexes was used to demonstrate that the intercalated cells in all regions studied contained carbonic anhydrase, even though the lectin binding differed. These results indicate that, in terms of their glycocalyx composition, intercalated cells represent a heterogeneous population in different regions of the collecting duct.
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PMID:Lectin-gold cytochemistry reveals intercalated cell heterogeneity along rat kidney collecting ducts. 391 93

In order to estimate the usefulness of lectins in the study of the functional segmentation of the nephron, the sites of binding of four lectins were identified in the rabbit kidney. Lectin-peroxidase conjugates were applied to unfixed cryostat sections. The bound conjugates were stained with 3,3'-diaminobenzidine for light microscopical observation. Each lectin has a specific binding pattern along the nephron. The patterns generally fit in with the segmentation of the nephron established by conventional histology. However, in the proximal tubule and in the thick ascending limb the lectin binding suggests functional transitions in histologically homogeneous tubular portions. In contrast to the other cell types of the connecting tubule and of the collecting duct the intercalated cells bind two lectins at their luminal membrane. Segmental differences in the lectin affinity of the basement membrane suggest that this structure has not only mechanical functions. The binding of lectins to luminal membranes in some segments indicate the possibility to use lectins for the separation of particular cell types and for modification of the transport properties of their membranes.
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PMID:The cellular specificity of lectin binding in the kidney. II. A light microscopical study in the rabbit. 710 28

Long-Evans (Eker) rats carry a mutation that predisposes them to develop spontaneous renal cell tumors of two morphologic patterns: solid chromophilic masses or cystic lesions lined by eosinophilic cells. Previous studies have suggested that these tumors arise from the proximal tubules. In the present study, lectin-binding characteristics and cytokeratin expression of various stages of hereditary rat renal epithelial neoplasia were examined to localize the portion of the nephron from which tumors arise. Lectin-binding histochemistry has been used as a marker of cell surface glycoprotein expression, thought to be important in the differentiation of benign from malignant epithelial lesions and in the determination of their cell of origin. The presence or absence of keratin intermediate filaments in the rat nephron has been used to identify nephron segments. The polyclonal antibody to high- and low-molecular-weight cytokeratin stained the cells of the collecting ducts but not the proximal or distal tubules. Binding to the proximal tubules by the lectins Conavalia ensiformis (Con A), Dolichas biflorus, Ricinus communis (RCA-1), and Triticum vulgare and to the distal tubules by Con A, RCA-1, Arachis hypogaea (PNA) with and without neuraminidase, and the antibody for cytokeratins was demonstrated. The lectin binding and cytokeratin staining patterns of rat hereditary renal cell carcinoma, adenoma and the preneoplastic lesions of atypical tubules and hyperplasias suggest that cystic adenomas arise from the distal nephron, principally the collecting duct, whereas the solid atypical tubules, hyperplasias, and adenomas arise from the proximal nephron, principally the proximal tubule.
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PMID:Preneoplastic and neoplastic lesions of rat hereditary renal cell tumors express markers of proximal and distal nephron. 748 12

Sarcomatoid renal cell carcinoma is a well-known entity, but sarcomatoid collecting duct carcinoma has not been reported. We recently encountered five cases. The patients were men whose ages ranged from 59 to 82 years (mean age, 68 years). All presented with gross hematuria and three had abdominal fullness. Tumor size ranged from 6 to 9 cm in greatest dimension. The Fuhrman's nuclear grade of the carcinomatous components was 3 in three cases and 4 in two. The sarcomatoid areas were composed of pleomorphic spindle cells forming a malignant fibrous histiocytomatous pattern in four cases and a fibrosarcomatous pattern in one. The immunohistochemical findings in the carcinomatous and sarcomatoid components were identical. Wide-spectrum anti-cytokeratin cocktail, epithelial membrane antigen, and vimentin antibodies demonstrated immunoreactivity, while Leu-M1 did not react in all five cases. Three of the five tumors were positive for Ulex europaeus agglutinin I lectin. One sarcomatoid carcinoma reacted with monoclonal antibody to high molecular weight keratins, and all five tumors reacted with a monoclonal antibody to low molecular weight keratins. Two patients died at 5 months and 13 months after diagnosis, two are alive with metastatic disease at 1 and 14 months, and one is alive with no evidence of disease at 36 months.
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PMID:Sarcomatoid collecting duct carcinoma: a clinicopathologic and immunohistochemical study of five cases. 750 49

Intercalated cells (ICC) of the collecting duct are believed to secrete acid (alpha-type) or HCO3 (beta-type). Although these two types of ICC are functionally mirror images of each other, several components in their cell membranes are clearly unique. As a first step in defining the molecular composition of beta-ICC membranes, we raised cell-specific monoclonal antibodies (MAb) against surface antigens. One of these MAb, designated B63, reacts with the apical membrane of peanut lectin agglutinin (PNA)-positive cells of the kidney cortex. B63-positive cells do not react with antibodies against band 3 (the basolateral C1/HCO3 exchanger) or ST.48, markers for alpha-ICC and principal cells, respectively. Despite a significant positive correlation between PNA and B63 staining intensities, determined by flow cytometry, these markers react with separate antigens, as indicated by competition studies and the different distribution of the two antigens. In addition to renal beta-ICC, B63 antigen is present in tissues that are involved in HCO3 secretion, such as the pancreas, salivary glands, and the small intestine, suggesting that it might play a role in HCO3 secretion. To test this hypothesis more directly, we tested the effect of MAb B63 on HCO3 secretion and on changes in intracellular pH (pHi) in isolated perfused cortical collecting ducts. Luminal Cl removal in the presence of luminal 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid resulted in a reversible increase in pHi. Luminal application of MAb B63 prevented this change in pHi. MAb B63 also significantly inhibited (by 37.7 +/- 7.3%) HCO3 secretion by isolated perfused tubules, whereas another MAb (MAb 601), which reacts with a separate antigen on beta-ICC, did not alter HCO3 secretion or pHi. These results indicate that B63 antigen plays an important role in HCO3 secretion: it might be either the apical anion exchanger of beta-ICC or an associated regulatory protein.
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PMID:Inhibition of bicarbonate transport in peanut lectin-positive intercalated cells by a monoclonal antibody. 751 43

Morphological and histoenzymological differences have been observed between intercalated and principal cells of the quail Coturnix coturnix japonica collecting ducts. The present study was designed to shed light on the lectin affinity of the collecting duct cells within cortex and medulla by the use of HRP-labelled lectins combined with glycosidase degradation. Binding of PNA and RCA-I lectins consequent to enzymatic release of sialic acid revealed abundant sialylated carbohydrate moieties within the principal cell cytoplasm. This characteristic binding pattern differed considerably from the staining observed in the intercalated cells. Interesting information also emerged about the presence of sialoglycoconjugates having the terminal disaccharide sialic acid-beta-N-acetylgalactosamine originating from the increased SBA binding and the unmodified DBA labelling after removal of sialic acid. Sequential degradation by sialidase/beta-galactosidase followed by incubation with DBA offered the possibility to suspect that the receptor sugar for the penultimate beta-galactose may be N-acetylgalactosamine. Conversely, we were not able to define the accept sugar for penultimate beta-GalNAc owing to the lack of availability of beta-N-acetylgalactosaminidase enzyme. When although further studies are clearly needed to elucidate the physiological role of the cellular sialoglycoconjugates detected, the present results already provide valuable insight into the carbohydrate composition of intercalated and principal cells in the quail collecting ducts.
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PMID:Mosaic lectin labelling in the quail collecting ducts. 754 Dec 64

The ampullary collecting duct epithelium acts as an inductor in the embryonic and neonatal kidney. It induces the formation of all nephron generations and thus determines the whole architecture of the kidney. As the organ matures, the collecting duct epithelium itself transdifferentiates. The ampullary inductor epithelium, which appears homogeneous as revealed by light microscopy, develops into the well-known heterogeneous epithelium of the mature collecting duct consisting of light principal and dark intercalated cells. Up to now the mechanisms initiating and regulating this transdifferentiation step are unknown. Only very few data are available concerning functional characteristics of the ampullary epithelial cells of neonatal rabbit kidney. Therefore, a characterization of the collecting duct ampullary cells was carried out by means of immunohistological techniques using a set of different monoclonal antibodies and the lectin peanut agglutinin. All epithelial cells within the ampullary tip and neck were positive for cytokeratin 19, an intermediate filament protein. On the other hand, the monoclonal antibody CD 7 revealed a clear cut boundary between the ampullary neck and the ampullary tip region. Furthermore, after incubation with the monoclonal antibody BO-7 specifically reacting with intercalated cells of the mature collecting duct, both labeled and unlabeled cells were observed within the whole ampullary epithelium. These results were confirmed by scanning electron microscopical investigations which revealed two distinct epithelial cell populations. Thus, an unexpected heterogeneity of the ampullary epithelium could be demonstrated.
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PMID:Histochemical markers reveal an unexpected heterogeneous composition of the renal embryonic collecting duct epithelium. 769 94

Madin-Darby canine kidney (MDCK) cells originate from the renal collecting duct and consist of different cell subtypes. We cloned two MDCK cell subtypes denominated as C7 and C11 with different morphology and different function. The two clones maintained their functional differences after cloning. C7 monolayers exhibit a high transepithelial resistance (Rte = 5648 +/- 206 omega.cm2, n = 20) and secrete K+ (delta K+ = 1.31 +/- 0.08 mmol/l, n = 10) into the apical medium. C11 monolayers display a low Rte (330 +/- 52 omega.cm2, n = 20) and secrete Cl- (delta Cl- = 16.9 +/- 1.8 mmol/l, n = 10) into the apical medium. Aldosterone (1 mumol/l) stimulates K+ secretion (delta K+ of 3.58 +/- 0.11 mmol/l, n = 7) in C7 cells and H+ secretion in C11 cells (delta pH = 0.060 +/- 0.007, n = 10). Aldosterone-induced stimulation of K+ secretion is inhibited by apical application of amiloride (1 mumol/l). cAMP stimulates H+ secretion in C11 cells (delta pH = -0.068 +/- 0.004, n = 10). Furthermore, C7 cells are peanut-lectin(PNA)-negative and exhibit an intracellular pH of 7.39 +/- 0.05 (n = 7), whereas C11 cells maintain intracellular pH at 7.16 +/- 0.05 (n = 8) and a major fraction of cells is PNA positive. We conclude that we have cloned two subtypes of MDCK cells which stably express different functional characteristics. The C7 subtype resembles principal cells (PC) of the renal collecting duct, whereas the C11 subtype resembles intercalated cells (ICC) of the renal collecting duct.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characterization of two MDCK-cell subtypes as a model system to study principal cell and intercalated cell properties. 797 Nov 72

The Madin-Darby canine kidney (MDCK) cell line has been proposed as a model for studying intercalated (IC) cells of the renal cortical collecting duct. The IC cells are characterized by peanut lectin (PNA) binding capacity, carbonic anhydrase (CA) activity and Cl(-)-HCO3- exchange mediated by a band 3-related protein. It has been suggested that these properties are also expressed in MDCK cells. So far however, the nature of the specific protein involved in Cl(-)-HCO3- exchange, the type of CA isozyme and the relationship between these two characteristics and PNA binding, have not been investigated in MDCK cells by immunocytochemical methods. Using two antibodies raised against human erythrocyte band 3 protein and two against human erythrocyte CA I and II isozymes, our study provides evidence that a protein related to band 3 is expressed in about 5% of cultured MDCK cells; these band 3-positive cells do not bind PNA and are not reactive for CAI or CAII. About 30% of the MDCK cells bind PNA, two-thirds of which are also CAII-positive. A majority (about 65%) of MDCK cells is not reactive for the three markers used; their density is increased after incubation with aldosterone. These data indicate (i) that the Cl(-)-HCO3- exchange of the MDCK cells could be related to human erythrocyte band 3, (ii) that the CA activity of the MDCK cell line bears antigenic identity with the erythrocyte CA II isozyme and (iii) that the latter is always co-localized with PNA binding.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Subtypes of Madin-Darby canine kidney (MDCK) cells defined by immunocytochemistry: further evidence for properties of renal collecting duct cells. 808 17


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