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)

The effects have been investigated of the regulatory peptides, substance P (SP) and bombesin, on the secretion of [14C]glucosamine-labeled trichloroacetic acid-phosphotungstic acid precipitable glycoproteins by canine tracheal explants. SP (10(10) to 10(-7) M) induced a dose-dependent increase in secretion of high-molecular-weight (greater than 2 X 10(6) radiolabeled glycoproteins predominantly from the submucosal glands. On a molar basis, SP [median effective concentration (EC50) = 8.2 X 10(-10) M] was about 1,000-fold more potent than methacholine (EC50 = 6.3 X 10(-7) M). Bombesin (10(-10) to 10(-4) M) had no effect on glycoprotein secretion. The time course of SP effect was characterized by an initial stimulation of glycoprotein secretion followed by a period of inhibition, suggesting that it rapidly exhausts a pool of glycoprotein, possibly that present within the duct lumen of the submucosal gland. Consistent with this are the findings that SP-induced secretion of glycoprotein was augmented by preincubation with methacholine while methacholine-induced secretion was diminished by preincubation with SP. Our findings show that SP is a potent stimulant of airway glycoprotein secretion in vitro and suggest that it acts by increasing the rate of clearance of mucus from the ducts of the submucosal gland, possibly by induced constriction of the secretory tubules and collecting duct. A role is discussed for SP in mucus hypersecretion induced by local axonal reflexes in the airway mucosa.
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PMID:Potent stimulation of glycoprotein secretion in canine trachea by substance P. 608 1

A sulfated, proline-rich glycoprotein (gpCDI, apparent molecular weight 200,000 in column chromatography and 150,000 in SDS-PAGE) was isolated from cultured renal collecting duct epithelium by centrifugation. Triton X100 extraction and DEAE-cellulose ion exchange chromatography. A DEAE-cellulose ion exchange chromatography fraction with the enriched gpCDI was used for immunization of guinea pigs. The antiserum was prepared for antigen localization by indirect immunofluorescence in collecting duct cell cultures and in tissue sections of neonatal and adult rabbit kidneys. In the cultured collecting duct epithelium, antibody staining of the epithelium and structures of the extracellular matrix was age dependent. Cultures of dedifferentiated collecting duct monolayers revealed positive reaction in the cytoplasm. In neonatal and adult rabbit kidneys, the antibody was localized in the entire collecting duct system but not in the collecting duct ampullae of the newborn kidney. Staining of the cytoplasm was found only in medullary collecting ducts of the neonatal kidney; other portions revealed staining mostly at the basal circumference of the tubule and at the luminal cell borders. Apart from collecting ducts, no other tubular segments were reactive. The cortical and the medullary interstitium contained fluorescent fibres which were concentrated around vascular structures. A possible relation between gpCDI and collagenous compounds is discussed. Bowman's capsule reacted positively, whereas staining of the mesangial matrix was weak. The localization of the antigen, as revealed by indirect immunofluorescence, suggests that gpCDI occurs both in intracellular and extracellular (interstitial) location. Two main points are emphasized: Firstly gpCDI is considered an important constituent in different stages of collecting duct development, and secondly, the staining pattern of the antibody varies with the different portions of both young and adult kidney collecting ducts; this staining heterogeneity may correspond with the known regional differences of collecting duct functions.
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PMID:Immunocytochemical localization of a renal glycoprotein (gpCDI) synthesized by cultured collecting duct cells. 637 Sep 31

Studies were carried out to define antigenic characteristics of the rabbit renal collecting duct. Renal papillae of adult rabbits were homogenized, centrifuged, and the 600 X g pellet was extracted with 0.5% Triton X-100 in the presence of 1 M NaCl. The crude extract was fractionated on an anion exchange column (DEAE cellulose). A fraction enriched in acidic proteins that co-purified with a radioactive 150 kd glycoprotein from cultured collecting duct cells (Minuth 1982), was used for immunization of guinea pigs. The antiserum shows the following characteristics as revealed by indirect immunofluorescence on the rabbit kidney: 1) Among all tubular epithelial cells only principal cells of the collecting duct and the connecting tubule cell show immunoreactivity. 2) The antiserum decorates the epithelial-interstitial interface of the whole collecting duct as well as of connecting tubule and thick ascending limb of Henle's loop. 3) There is immunoreactivity of interstitial fibers throughout the kidney. 4) Epithelial cells in a variety of other organs in rabbit did not react with the antiserum. Our data demonstrate an antigenic distinction of both, the connecting tubule cell and the principal cell, discriminating these cells from other tubular epithelial cells including the intercalated cells of the collecting duct system. Furthermore, our findings point to a heterogeneity along the distal nephron with respect to the constituents of the epithelial-interstitial interface.
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PMID:Immunohistochemical localization of a protein fraction derived from rabbit renal papilla. 639 56

The biochemical and morphological extent of glycoprotein synthesis inhibition of cellular and extracellular proteins was studied on cultured renal collecting duct (CD) epithelium. We found that tunicamycin (4 micrograms/ml) inhibits the glycosylation of a 150,000 d glycoprotein (gpCDI). A 85,000 d glycoprotein (gpCDII) was not affected. The inhibition by tunicamycin demonstrates that gpCDI has characteristics of a N-glycan, whereas gpCDII seems to be an O-glycan. 6-diazo-5-oxo-norleucine (4 X 10(-5) M) which was used as glutamine analogue, did not show a comparable inhibitory effect as seen with tunicamycin. The lack of effect of norleucine demonstrates that glutamine is not the locus of glycosylation in both proteins. However, because of the tunicamycin inhibition it points to asparagine as the site of glycosylation in the gpCDI. Long term cultures of the tissue up to 15 days in the presence of tunicamycin and norleucine and of substances usually used as basement membrane inhibitors, such as hydroxy-D-proline (1 mM), L-azetidine-2-carboxylic acid (1 mM) and o- and p-nitrophenyl-xylopyranoside 1 mM), revealed that it is possible to eliminate completely the fibroblasts beneath the cultured epithelium and within the degenerating corematerial. Experiments with hydroxy-D-proline showed the most striking effect. Experiments with L-azetidine-2-carboxylic acid and nitrophenyl-xylopyranoside resulted in the elimination of fibroblasts and dedifferentiation of the collecting duct epithelium.
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PMID:Effects of glycoprotein and basement membrane synthesis inhibitors on the growth of cultured renal collecting duct epithelium. 648 Apr 14

The current report presents findings from a comparative histological and histochemical investigation of murine congenital polycystic kidney disease. The studies revealed that the morphological changes are initiated in the developing proximal tubules of the nephron; differences from control sections first become evident at 16 days' gestation. As the disease progresses, obvious changes include hyperplasia and dilation of the tubule, cellular vacuolization, and alterations in the apical cell brush border. Included among the latter changes are decreases in enzyme (alkaline phosphatase) staining and decreases in glycoprotein staining (periodic acid Schiff). All such changes continue until the kidney is markedly cystic and apical cell cytochemical staining is absent. Some cellular vacuolization, assumed to be a normal developmental event, is also seen within the same segment of the proximal tubule at 17 days' gestation through the 1st postnatal day. Dilation of the collecting duct is noted to be a later or secondary change evident after the initial onset of the disease.
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PMID:Development of the embryonic murine kidney in normal and congenital polycystic kidney disease: characterization of a proximal tubular degenerative process as the first observable light microscopic defect. 669 Jul 41

Renal cortical explants consisting of capsula fibrosa with an adherent thin layer of collecting duct anlagen, S-shaped bodies, and nephrogenic blastema were isolated from newborn New Zealand rabbits and cultured in Dulbecco's Modified Eagle's medium for 24 hours. Within this period of time, the explants formed globular bodies surrounded by an epithelium of differentiated collecting duct cells. The outgrowth of the collecting duct cells and the formation of the epithelium occurred only when serum was added to the cultivation medium. Different types and different concentrations of serum were tested; fetal bovine serum and newborn and adult rabbit sera at concentrations of at least 5% induced the outgrowth and spreading of the cells. The surrounding epithelium did not develop in the absence of serum. The outgrowth of the collecting duct cells in serum-supplemented cultivation media was arrested by inhibitors of protein and glycoprotein synthesis and by cytoskeletonal-blocking agents such as cycloheximide (1 x 10(-6) M), actinomycin C1 (2 micrograms/ml), tunica-mycin (1 microgram/ml), 6-diazo-5-oxo-norleucine (2 x 10(-5) M), vinblastine (5 x 10(-6) M), colchicine (1 x 10(-3) M), and cytochalasin B (2 micrograms/ml). In contrast, inhibitors of DNA synthesis, e.g., cytosine arabinoside (2.5 x 10(-5) M), mitomycin (1 x 10(-6) M), and hydroxyurea (2.5 x 10(-3) M), had no influence on the outgrowth.
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PMID:Induction and inhibition of outgrowth and development of renal collecting duct epithelium. 684 85

Cortical kidney explants from newborn New Zealand rabbits were cultured in Dulbecco's minimum essential medium (DMEM) containing 10% fetal calf serum. Within 24 h the explants formed 'globular bodies' which were completely covered by a monolayered epithelium. The cells were differentiated and resembled collecting duct epithelium. By culturing the globular bodies in Dulbecco's MEM with D-valine instead of L-valine, a monolayer of collecting duct cells was obtained and used for control experiments. For analysis and identification of synthesized glycoproteins, the globular bodies were incubated with various labelled carbohydrates and amino acids, and then fractionated. Glycoproteins secreted into the culture medium were not detected. Cell-associated glycoproteins were found in crude membrane fractions and then extracted with Triton X-100 for column chromatography, SDS-polyacrylamide electrophoresis in 6 M urea, isoelectrofocusing, and two-dimensional electrophoresis. Two prominent glycoproteins containing galactose and glucosamine were synthesized during the spreading of the epithelium, with an apparent molecular weight of 150,000 and 85,000 (SDS-PAGE). The synthesized glycoproteins differ in their content of radioactive glycoprotein precursor and leucine. The 85,000 dalton monomer glycoprotein has an isoelectric point of 3.5 and was identified by two-dimensional electrophoresis.
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PMID:Glycoprotein synthesis of renal collecting duct epithelium cultured as globular bodies. 685 45

The distribution of neutral and acid (sialylated and sulfated) glycoprotein in the urinary apparatus of a marine and a fresh water cottid teleost (Bull rout and Bullhead) has been studied. The renal morphology of the Bullhead Cottus gobio is similar to that of the marine Bullrout Myoxocephalus scorpius: The glomerular nephron consists of 2 tubular segments (PI and PII), leading to the collecting duct-archinephric duct system (CD/AD). Sialoglycoprotein is present in the secretion of the proximal tubule segment PII cells in breeding males of Cottus gobio, resembling the mucus production of nest building male sticklebacks Gasterosteidae. The acid mucus coat in the CD/AD system of Myoxocephalus is discussed in relation to the excretion of salts by the kidney.
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PMID:Histochemical observations on glycoproteins in the urinary apparatus of the bullhead Cottus gobio L. and the bull rout Myoxocephalus scorpius (L.). 710 34

Thin cortical kidney explants from newborn New Zealand rabbits were cultured in Dulbecco's MEM containing 10% fetal bovine serum. Within 24 h the explants formed globular bodies which were completely covered by a monolayered epithelium. The cells show polar differentiation and resemble the renal collecting duct epithelium. By culturing the globular bodies in Dulbecco's MEM with D-valine instead of L-valine additionally a monolayer of renal collecting duct cells was obtained. For the study of glycoprotein synthesis the globular bodies and the collecting duct monolayers were incubated with various labelled carbohydrates, protein and collagen precursors and then fractionated into coarse membrane pellets. The synthesized glycoproteins were regained in 600 x g and 12,000 x g coarse membrane fractions and extracted with Triton X 100 buffer for column chromatography and SDS-polyacrylamide electrophoresis in 6 M urea. In addition to a 85,000 d glycoprotein, a carbohydrate rich collagen like protein (apparent molecular weight in column chromatography 200,000 d, in the SDS-polyacrylamide electrophoresis 150,000 d) was found. The 150,000 d glycoprotein incorporates favorably radioactive proline, sulfate, and smaller amounts of lysine, and leucine. Compared to the 85,000 d glycoprotein a double amount of glucosamine and galactose and four fold amount of fucose was detected. The 85,000 d protein has to be ascribed as a usual glycoprotein, in contrast the 150,000 d protein shows an unusual combination of characteristics and has to be considered as a new type of renal glycoprotein.
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PMID:Cell associated glycoproteins synthesized by cultured renal tubular cells. 717 68

C57BL/6J mice homozygous for the cpk gene exhibit an autosomal recessive (AR) form of polycystic kidney disease (PKD), similar to human ARPKD, with massive collecting duct cysts. These cysts are lined by epithelial with an immature phenotype. Since renal expression of epidermal growth factor (EGF) is also significantly decreased in affected mice, we hypothesized that renal EGF is necessary for normal developmental maturation of the collecting duct. To determine if the lack of EGF may be a decisive factor in the initiation and/or growth of collecting duct cysts, we administered exogenous EGF (1 microgram/g body wt subcutaneously) daily for Postnatal Days 3-9 (a critical period for collecting duct maturation) to C57BL/6J-cpk mice. EGF but not sham or albumin treatment retarded the development of PKD, reduced the degree of renal failure associated with the disease, and prolonged the survival of cystic mice. Sulfated glycoprotein-2 gene expression, a marker of immaturity in collecting duct cells, was reduced in cystic kidney by EGF treatment. This finding indicates that EGF treatment was associated with an increase in the maturation of the collecting duct epithelial cells. These findings support the view that decreased EGF may play a significant role in promoting the enlargement of collecting duct cysts in a hereditary model of ARPKD and that PKD involves defective and/or arrested collecting duct cell maturation.
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PMID:Epidermal growth factor ameliorates autosomal recessive polycystic kidney disease in mice. 778 94


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