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)

Immunohistochemical and immunochemical analyses were performed on a monoclonal antibody designated 1-2B7B which was derived from immunizing mice with human prostate epithelial tissue. The 1-2B7B antigen was expressed not only along the acinous basement membrane zone (BMZ) of the prostate and testis, but also along the BMZ of the epithelia of several other organs including the skin, oesophagus, urinary bladder, ureter, stomach, intestine and bile duct. The antigenic epitope was not expressed in these tissues of lower mammals. Immunoelectron microscopic studies on normal human skin revealed that the 1-2B7B antigen was localized mainly just beneath the hemidesmosomes of basal keratinocytes, but not beneath melanocytes. Indirect immunofluorescence and immunoelectron microscopic studies on 1 M NaCl-split skin confirmed that this antigen was not separated from the cytoplasmic membrane of basal cells after salt treatment. SDS polyacrylamide gel electrophoresis of immunochemically purified protein from the epidermis demonstrated the molecular weight of the antigen to be 120 kDa. 1-2B7B monoclonal antibody should be a useful probe for studying the pathomechanism of some blistering diseases, as well as the assembly and function of the epidermal-dermal junction.
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PMID:1-2B7B: monoclonal antibody reacting to the 120 kDa polypeptide component of human epidermal hemidesmosomes. 192 54

Using an SDS-polyacrylamide gel electrophoresis, the contractile protein content of the normal rabbit ureter was compared with that of the dilated ureter. The relative amounts of the actin and myosin were significantly decreased in the dilated ureter.
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PMID:The contents of contractile proteins in the normal and dilated ureter. 663 44

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play a key role in docking and fusion of intracellular transport vesicles and may regulate apical and basolateral membrane protein delivery in epithelial cells. In a previous study, syntaxin 3 (a target SNARE) protein was detectable in the kidney only in intercalated cells. We now report a more widespread distribution of syntaxin 3 in a variety of renal epithelial cells after antigen retrieval. Sections of rat kidney were treated with SDS and incubated with antisyntaxin 3 antibodies. Strong basolateral membrane staining was seen in descending and ascending thin limbs of Henle, thick ascending limbs of Henle, the macula densa, distal and connecting tubules, and all cells of the collecting duct including A- and B-intercalated cells. The papillary surface epithelium and the transitional epithelium of the ureter were also stained, but proximal tubules were negative. Western blotting revealed a strong signal at 37 kDa in all regions, and the antigen was restricted to membrane fractions. SDS treatment was not necessary to reveal syntaxin 3 in intercalated cells. These data show that syntaxin 3 might be involved in basolateral trafficking pathways in most renal epithelial cell types. The exclusive basolateral location of syntaxin 3 in situ, however, contrasts with the apical location of this SNARE protein in some kidney epithelial cells in culture.
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PMID:Antigen retrieval reveals widespread basolateral expression of syntaxin 3 in renal epithelia. 1183 35

The kidney glomerulus plays a pivotal role in ultrafiltration of plasma into urine and also is the locus of kidney disease progressing to chronic renal failure. We have focused proteomic analysis on the glomerulus that is most proximal to the disease locus. In the present study, we aimed to provide a confident, in-depth profiling of the glomerulus proteome. The glomeruli were highly purified from the kidney cortex from a male, 68-year-old patient who underwent nephroureterectomy due to ureter carcinoma. The patient was normal in clinical examinations including serum creatinine and urea levels and liver function, and did not receive any chemotherapy and radiotherapy. The cortical tissue was histologically normal, and no significant deposition of immunoglobulins and complement C3 was observed. We employed a novel strategy of protein separation using 1D (SDS-PAGE) and 2D (solution-phase IEF in combination with SDS-PAGE) prefractionation prior to the shotgun analysis with LC-MS/MS. The protein prefractionation produced 90 fractions, and eventually provided a confident set of identified proteins consisting of 6686 unique proteins (3679 proteins with two or more peptide matches and 3007 proteins with one peptide match), representing 2966 distinct genes. All the identified proteins were annotated and classified in terms of molecular function and biological process, compiled into 1D and 2D protein arrays, consisting of 15 and 75 sections, corresponding to the protein fractions which were defined by MW and pI range, and deposited on a Web-based database (http://www.hkupp.org). The most remarkable feature of the glomerulus proteome was a high incidence of identification of cytoskeleton-related proteins, presumably reflecting the well-developed, cytoskeletal organization of glomerular cells related to their physiological functions.
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PMID:In-depth proteomic profiling of the normal human kidney glomerulus using two-dimensional protein prefractionation in combination with liquid chromatography-tandem mass spectrometry. 1771 22