Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0403608 (ureter)
 9,655 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mucin layer covering the bladder transitional cell mucosa appears to function as a primary defense mechanism against bacterial infection. We have previously prepared a glycoprotein fraction (GP1) from the urinary bladder mucosa of NZW rabbits and raised murine antisera against it. These antisera react with bladder, ureter and kidney tissue from rabbits, rats, guinea pigs, and hamsters. We now show that a similar substance occurs in human kidneys and bladder. In order to remove antibodies reactive with the Tamm-Horsfall protein (THP), the antisera were initially absorbed with an immunoadsorbent composed of purified human THP covalently bound to Sepharose CL-4B gel. Using an enzyme linked immunosorbent assay (ELISA) it could be shown that the absorbed antisera did not react with THP but retained a high titer in binding to GP1. Immunohistochemical procedures involving avidin-biotin-immunoperoxidase staining demonstrated that the absorbed anti-GP1 reacted well with six human urinary bladder biopsy specimens and two kidney autopsy specimens while normal murine sera showed little or no binding. Although this reactivity was not as strong as that found with homologous tissue (rabbit) these studies suggest that GP1, an antigen common to several animal species, is also related to a human urinary tract component.
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PMID:Antisera to a rabbit urinary tract antigen also react with human bladder and kidney tissue. 240 92

Pemphigus foliaceus (PF) is a human autoimmune disease in which autoantibodies are directed against the cell surface of epidermal cells. Using an immunoblotting technique, we recently demonstrated that a subgroup of PF patients have autoantibodies to the desmosomal core glycoprotein, desmoglein I (DGI). There are desmosomes in all epithelia and in heart, yet PF affects only stratified squamous epithelia. One explanation for this finding might be that there are tissue-specific differences in desmosomes. Thus, to determine whether certain epitopes of DGI are tissue-restricted, we performed immunofluorescence studies on various monkey tissues with the following antibodies: a rabbit polyclonal antiserum against whole desmosomes, which demonstrated the desmosomes in all tissues tested; a mouse monoclonal antibody against DGI, MmDGI-1; and PF sera that bound DGI on immunoblotting (PF IB+). In addition, we tested the tissues with PF sera that did not bind DGI by immunoblotting (PF IB-) to determine if these sera were different from PF IB+ sera in their tissue specificity. PF IB+, PF IB-, and MmDGI-1 antibodies stained all stratified squamous epithelia tested, including skin, tongue, upper esophagus, conjunctiva, and cornea; however, they did not stain heart or any nonstratified squamous epithelia, including gall bladder, small intestine, liver, ureter, and bladder. These results indicate that there is tissue heterogeneity of desmosomes, and that epitopes on DGI defined by both PF antibodies and a monoclonal antibody are present only in stratified squamous epithelia. In addition, PF IB- sera had the same tissue specificity as PF IB+ sera. These results may partially explain why PF involves only stratified squamous epithelia.
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PMID:Pemphigus foliaceus antibodies and a monoclonal antibody to desmoglein I demonstrate stratified squamous epithelial-specific epitopes of desmosomes. 245 47

The iron-transporting serum glycoprotein, transferrin, is necessary for the cell proliferation, morphogenesis, and differentiation of mouse embryonic teeth and kidneys in organ culture. The stimulatory effect of transferrin is mediated by the binding of transferrin to its specific cell-surface receptor and by receptor-mediated endocytosis. Since, in both teeth and kidneys, the requirement for and responsiveness to transferrin depend on the developmental stage of the organ, we studied the binding of transferrin at various stages of tooth and kidney development by incubating tissues with 125I-labeled transferrin. The amount of bound transferrin was determined by measuring the tissue-incorporated radioactivity, and the binding sites were localized by autoradiography. During tooth development in vitro, the requirement for exogenous transferrin is lost as the teeth proceed from the early cap stage to the bell stage. The level of transferrin binding was found to decrease simultaneously, and in bell-stage teeth, the transferrin receptors were concentrated in the areas of most active cell proliferation. In kidneys, the number of transferrin receptors was highest at the stage during which the undifferentiated kidney mesenchyme becomes responsive to transferrin. These receptors were located in both the ureter epithelium and the metanephric mesenchyme, and they dramatically decreased in number with advancing kidney differentiation. The results of the present study indicate that, during the embryonic development of teeth and kidneys, the amount and localization of transferrin binding are correlated with cell proliferation. The number of transferrin receptors is highest during the developmental stages when cell proliferation is most active, and decreases with advancing differentiation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Levels and patterns of 125I-labeled transferrin binding in mouse embryonic teeth and kidneys at various developmental stages. 360 30

Thrombomodulin (TM) is a surface glycoprotein reported to be expressed in a variety of tumors, including mesotheliomas, endothelial vascular tumors, squamous carcinomas, and various adenocarcinomas. This study evaluated TM expression in transitional cell carcinomas (TCCs) and determined whether immunostaining for TM has practical value in the diagnosis of TCCs. TM expression was observed in 96 of 106 primary tumors (bladder, 64/72; renal pelvis, 12/14; ureter, 3/3; prostate, 17/17) and in 21 of 23 metastatic TCCs. Among the adenocarcinomas, only 3 of 18 originating in the bladder, 7 of 46 in the lung, 4 of 21 in the breast, 2 of 24 in the ovary, and 2 of 4 in the pancreas expressed this marker. No staining was observed in the 22 renal cell carcinomas or the 35 adenocarcinomas of the prostate, 13 of the endometrium, or 12 of the colon. Nearly all squamous cell carcinomas (lung, 21/27; skin, 7/7; uterine cervix, 6/6; esophagus, 2/2; bladder, 2/2) reacted for TM. TM is a sensitive marker for TCC. TM immunostaining can assist in distinguishing this tumor from others, especially renal cell carcinomas and adenocarcinomas of the prostate, colon, and bladder, but it has no value in separating TCC from squamous cell carcinomas.
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PMID:Thrombomodulin expression in transitional cell carcinoma. 972 15

Urea transporter UT-B has been proposed to be the major urea transporter in erythrocytes and kidney-descending vasa recta. The mouse UT-B cDNA was isolated and encodes a 384-amino acid urea-transporting glycoprotein expressed in kidney, spleen, brain, ureter, and urinary bladder. The mouse UT-B gene was analyzed, and UT-B knockout mice were generated by targeted gene deletion of exons 3-6. The survival and growth of UT-B knockout mice were not different from wild-type littermates. Urea permeability was 45-fold lower in erythrocytes from knockout mice than from those in wild-type mice. Daily urine output was 1.5-fold greater in UT-B- deficient mice (p < 0.01), and urine osmolality (U(osm)) was lower (1532 +/- 71 versus 2056 +/- 83 mosM/kg H(2)O, mean +/- S.E., p < 0.001). After 24 h of water deprivation, U(osm) (in mosM/kg H(2)O) was 2403 +/- 38 in UT-B null mice and 3438 +/- 98 in wild-type mice (p < 0.001). Plasma urea concentration (P(urea)) was 30% higher, and urine urea concentration (U(urea)) was 35% lower in knockout mice than in wild-type mice, resulting in a much lower U(urea)/P(urea) ratio (61 +/- 5 versus 124 +/- 9, p < 0.001). Thus, the capacity to concentrate urea in the urine is more severely impaired than the capacity to concentrate other solutes. Together with data showing a disproportionate reduction in the concentration of urea compared with salt in homogenized renal inner medullas of UT-B null mice, these data define a novel "urea-selective" urinary concentrating defect in UT-B null mice. The UT-B null mice generated for these studies should also be useful in establishing the role of facilitated urea transport in extrarenal organs expressing UT-B.
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PMID:Urea-selective concentrating defect in transgenic mice lacking urea transporter UT-B. 1179 14

The 40-kilodalton processed glycoprotein, mesothelin, is highly expressed in epithelial mesotheliomas and adenocarcinomas of the ovary (serous papillary) and pancreas, but its expression in a large series of other common carcinomas has not been completely explored. In the present study, we used oligonucleotide and tissue microarrays to profile the expression of the mesothelin gene (MSLN) and encoded protein, respectively. Among 150 carcinomas of multiple anatomic sites, we found the highest average expression of MSLN in serous carcinomas of the ovary and adenocarcinomas of the pancreas, consistent with previous reports, as well as measurable but less-striking expression in pulmonary, gastric/esophageal, and colorectal adenocarcinomas. On tissue microarrays containing 621 carcinomas derived from the same and additional sites as those profiled by gene expression, mesothelin immunoreactivity was highest in cancers of the ovary (serous papillary, endometrioid, and undifferentiated) and pancreas, with less frequent staining seen in adenocarcinomas of the endometrium, lung, and stomach/esophagus. Some immunopositivity was observed in 42% of pulmonary adenocarcinomas, including 18% that had >50% of tumor cells that were immunoreactive. Some 14% of breast and 30% of colorectal adenocarcinomas showed immunopositivity, but no case contained >50% tumor cells that were immunoreactive. Mesothelin was either entirely absent or present in <5% of carcinomas of the prostate, bladder/ureter, liver, kidney, and thyroid. Overall, we observed good concordance between the results obtained by oligonucleotide and tissue microarrays. This large study of the MSLN gene and protein expression in common carcinomas provides data for future investigations that evaluate the utility of mesothelin/megakaryocyte potentiating factor as a potential serum tumor marker or target of immunotoxin-based therapy in human cancers.
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PMID:Large-scale molecular and tissue microarray analysis of mesothelin expression in common human carcinomas. 1282 15

Bone morphogenetic protein (BMP) signaling pathway plays important roles in urinary tract development although the detailed regulation of its activity in this process remains unclear. Here we report that follistatin-like 1 (Fstl1), encoding a secreted extracellular glycoprotein, is expressed in developing ureter and antagonizes BMP signaling activity. Mouse embryos carrying disrupted Fstl1 gene displayed prominent hydroureter arising from proximal segment and ureterovesical junction defects. These defects were associated with significant reduction in ureteric epithelial cell proliferation at E15.5 and E16.5 as well as absence of subepithelial ureteral mesenchymal cells in the urinary tract at E16.5 and E18.5. At the molecular level, increased BMP signaling was found in Fstl1 deficient ureters, indicated by elevated pSmad1/5/8 activity. In vitro study also indicated that Fstl1 can directly bind to ALK6 which is specifically expressed in ureteric epithelial cells in developing ureter. Furthermore, Sonic hedgehog (SHH) signaling, which is crucial for differentiation of ureteral subepithelial cell proliferation, was also impaired in Fstl1(-/-) ureter. Altogether, our data suggest that Fstl1 is essential in maintaining normal ureter development by antagonizing BMP signaling.
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PMID:Fstl1 antagonizes BMP signaling and regulates ureter development. 2248 32