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Volumn 52, Issue 5, 1997, Pages 1340-1350

Intracellular transport, cell-surface exposure and release of recombinant Tamm-Horsfall glycoprotein

Author keywords

Autoantigen; Glycoprotein; Immunocomplex formation; Protein; Tamm Horsfall glycoprotein; Transport

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; TAMM HORSFALL GLYCOPROTEIN;

EID: 0030724926     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1038/ki.1997.459     Document Type: Article
Times cited : (54)

References (57)
  • 1
    • 0002970919 scopus 로고
    • A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses
    • TAMM I, HORSFALL FL JR: A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses. J Exp Med 95:71-97, 1952
    • (1952) J Exp Med , vol.95 , pp. 71-97
    • Tamm, I.1    Horsfall Jr., F.L.2
  • 2
    • 0015578463 scopus 로고
    • The development of a radioimmunoassay for the measurement of urinary Tamm-Horsfall glycoprotein in the presence of sodium dodecyl sulphate
    • GRANT AMS, NEUBERGER A: The development of a radioimmunoassay for the measurement of urinary Tamm-Horsfall glycoprotein in the presence of sodium dodecyl sulphate. Clin Sci 44:163-179, 1973
    • (1973) Clin Sci , vol.44 , pp. 163-179
    • Grant, A.M.S.1    Neuberger, A.2
  • 3
    • 0025353820 scopus 로고
    • Tamm-Horsfall protein-uromodulin (1950-1990)
    • KUMAR S, MUCHMORE A: Tamm-Horsfall protein-uromodulin (1950-1990). Kidney Int 37:1395-1401, 1990
    • (1990) Kidney Int , vol.37 , pp. 1395-1401
    • Kumar, S.1    Muchmore, A.2
  • 6
    • 0015089756 scopus 로고
    • Tamm-Horsfall mucoprotein: 1. Localization in the kidney
    • SCHENK EA, SCHWARTZ RH, LEWIS RA: Tamm-Horsfall mucoprotein: 1. Localization in the kidney. Lab Invest 25:92-95, 1971
    • (1971) Lab Invest , vol.25 , pp. 92-95
    • Schenk, E.A.1    Schwartz, R.H.2    Lewis, R.A.3
  • 7
    • 0018733601 scopus 로고
    • Localization by immunofluorescence and by light- and electron-microscopic immunoperoxidase techniques of Tamm-Horsfall glycoprotein in adult hamster kidney
    • SIKRI KL, FOSTER CL, BLOOMFIELD FJ, MARSHALL RD: Localization by immunofluorescence and by light- and electron-microscopic immunoperoxidase techniques of Tamm-Horsfall glycoprotein in adult hamster kidney. Biochem J 181:525-532, 1978
    • (1978) Biochem J , vol.181 , pp. 525-532
    • Sikri, K.L.1    Foster, C.L.2    Bloomfield, F.J.3    Marshall, R.D.4
  • 8
    • 0019455684 scopus 로고
    • Localization of Tamm-Horsfall glycoprotein in the human kidney using immunofluorescence and immunoelectron microscopical techniques
    • SIKRI KL, FOSTER CL, MACHUGH N, MARSHALL RD: Localization of Tamm-Horsfall glycoprotein in the human kidney using immunofluorescence and immunoelectron microscopical techniques. J Anat 132:597-605, 1981
    • (1981) J Anat , vol.132 , pp. 597-605
    • Sikri, K.L.1    Foster, C.L.2    Machugh, N.3    Marshall, R.D.4
  • 9
    • 0025667675 scopus 로고
    • Uromodulin (TH glycoprotein/Uromucoid) is a phosphatidylinositol-linked membrane-protein
    • RINDLER MJ, NAIK SS, LI N, HOPPS TC. PERALDI M-N: Uromodulin (TH glycoprotein/Uromucoid) is a phosphatidylinositol-linked membrane-protein. J Biol Chem 265:20784-20789, 1990
    • (1990) J Biol Chem , vol.265 , pp. 20784-20789
    • Rindler, M.J.1    Naik, S.S.2    Li, N.3    Hopps, T.C.4    Peraldi, M.-N.5
  • 10
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structure
    • FERGUSON MAJ, WILLIAMS AF: Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structure. Ann Rev Biochem 57:285-320, 1988
    • (1988) Ann Rev Biochem , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 11
    • 0021031935 scopus 로고
    • Guinea-pig kidney β-N-acetylgalac-tosaminyltransferase towards Tamm-Horsfall glycoprotein
    • SERAFINI-CESSI F, DALL'OLIO F: Guinea-pig kidney β-N-acetylgalac-tosaminyltransferase towards Tamm-Horsfall glycoprotein. Biochem J 215:483-489, 1983
    • (1983) Biochem J , vol.215 , pp. 483-489
    • Serafini-Cessi, F.1    Dall'olio, F.2
  • 12
    • 0021764692 scopus 로고
    • Structural analysis of the carbohydrate moieties of human Tamm-Horsfall glycoprotein
    • WILLIAMS J, MARSHALL RD, VAN HALBEEK H, VLIEGENTHART JFG: Structural analysis of the carbohydrate moieties of human Tamm-Horsfall glycoprotein. Carbohydr Res 134:141-155, 1984
    • (1984) Carbohydr Res , vol.134 , pp. 141-155
    • Williams, J.1    Marshall, R.D.2    Van Halbeek, H.3    Vliegenthart, J.F.G.4
  • 13
    • 0021525437 scopus 로고
    • A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin
    • SERAEINI-CESSI F, MALAGOLINI N, DALL'OLIO F: A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin. Biosci Rep 4:973-978, 1984
    • (1984) Biosci Rep , vol.4 , pp. 973-978
    • Seraeini-Cessi, F.1    Malagolini, N.2    Dall'olio, F.3
  • 15
    • 0021400273 scopus 로고
    • High-mannose oligosaccharides from human Tamm-Horsfall glycoprotein
    • SERAFINI-CESSI F, DALL'OLIO F, MALAGOLINI N: High-mannose oligosaccharides from human Tamm-Horsfall glycoprotein. Biosci Rep 4:269-274, 1984
    • (1984) Biosci Rep , vol.4 , pp. 269-274
    • Serafini-Cessi, F.1    Dall'olio, F.2    Malagolini, N.3
  • 16
    • 0024288287 scopus 로고
    • Structural analysis of the preponderant high-mannose oligosaccharide of human Tamm-Horsfall glycoprotein
    • DALL'OLIO F, DE KANTER FJJ, VAN DEN EIJNDEN DH, SERAFINI-CESSI F: Structural analysis of the preponderant high-mannose oligosaccharide of human Tamm-Horsfall glycoprotein. Carbohydr Res 178:327-332, 1988
    • (1988) Carbohydr Res , vol.178 , pp. 327-332
    • Dall'olio, F.1    De Kanter, F.J.J.2    Van Den Eijnden, D.H.3    Serafini-Cessi, F.4
  • 17
    • 0025614879 scopus 로고
    • Pregnancy-associated changes in oligomannoside oligosaccharides of human and bovine uromodulin (Tamm-Horsfall glycoprotein)
    • SMAGULA RM, VAN HALBEEK H, DECKER JM, MUCHMORE AV, MOODY CE, SHERBLOM AP: Pregnancy-associated changes in oligomannoside oligosaccharides of human and bovine uromodulin (Tamm-Horsfall glycoprotein). Glycoconjugate J 7:609-624, 1990
    • (1990) Glycoconjugate J , vol.7 , pp. 609-624
    • Smagula, R.M.1    Van Halbeek, H.2    Decker, J.M.3    Muchmore, A.V.4    Moody, C.E.5    Sherblom, A.P.6
  • 18
    • 0027209562 scopus 로고
    • Biosynthesis and oligosaccharide processing of human Tamm-Horsfall glycoprotein permanently expressed in HeLa cells
    • SERAFINI-CESSI F, MALAGOLINI N, HOOPS TC, RINDLER MJ: Biosynthesis and oligosaccharide processing of human Tamm-Horsfall glycoprotein permanently expressed in HeLa cells. Biochem Bioph Res Commun 194:784-790, 1993
    • (1993) Biochem Bioph Res Commun , vol.194 , pp. 784-790
    • Serafini-Cessi, F.1    Malagolini, N.2    Hoops, T.C.3    Rindler, M.J.4
  • 19
    • 0015242002 scopus 로고
    • The effect of ions on the viscosimetric and ultracentrifugal behaviour of Tamm-Horsfall glycoprotein
    • STEVENSON FK, CLEAVE AJ, KENT DW: The effect of ions on the viscosimetric and ultracentrifugal behaviour of Tamm-Horsfall glycoprotein. Biochim Biophys Acta 236:59-66, 1971
    • (1971) Biochim Biophys Acta , vol.236 , pp. 59-66
    • Stevenson, F.K.1    Cleave, A.J.2    Kent, D.W.3
  • 21
    • 0026671080 scopus 로고
    • Mechanoelectrical transduction, ion movement and water stasis in uromodulin
    • MATTEY M, NAFTALIN L: Mechanoelectrical transduction, ion movement and water stasis in uromodulin. Experientia 48:975-980, 1992
    • (1992) Experientia , vol.48 , pp. 975-980
    • Mattey, M.1    Naftalin, L.2
  • 22
    • 0023695035 scopus 로고
    • Identification of factors in human urine that inhibit the binding of Escherichia colon adhesins
    • PARKKINEN J, VIRKOLA R, KORHONEN TK: Identification of factors in human urine that inhibit the binding of Escherichia colon adhesins. Infect Immun 56:2623-2630, 1988
    • (1988) Infect Immun , vol.56 , pp. 2623-2630
    • Parkkinen, J.1    Virkola, R.2    Korhonen, T.K.3
  • 23
    • 0017353708 scopus 로고
    • Some factor affecting the production by cultured baby-hamster kidney cell of BHK glycoprotein 1 which cross-reacts immunologically with THP
    • BLOOMFIELD FJ, DUNSTAN DR, FOSTER CL, SERAFINI-CESSI F, MARSHALL RD: Some factor affecting the production by cultured baby-hamster kidney cell of BHK glycoprotein 1 which cross-reacts immunologically with THP. Biochem J 164:41-51, 1977
    • (1977) Biochem J , vol.164 , pp. 41-51
    • Bloomfield, F.J.1    Dunstan, D.R.2    Foster, C.L.3    Serafini-Cessi, F.4    Marshall, R.D.5
  • 24
    • 0024459386 scopus 로고
    • Temporal aspects of O-glycosylation of glycoprotein C from herpes simplex virus type-1
    • SERAFINI-CESSI F, DALL'OLIO F, MALAGOLINI N, CAMPADELLI-FIUME G: Temporal aspects of O-glycosylation of glycoprotein C from herpes simplex virus type-1. Biochem J 262:479-484, 1989
    • (1989) Biochem J , vol.262 , pp. 479-484
    • Serafini-Cessi, F.1    Dall'olio, F.2    Malagolini, N.3    Campadelli-Fiume, G.4
  • 25
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • BRAAKMAN I, HELENIUS J, HELENIUS A0: Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J 11:1717-1722, 1992
    • (1992) EMBO J , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 26
    • 0025146994 scopus 로고
    • Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents
    • ALBERINI CM, BET P, MILSTEIN C, SITIA R: Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents. Nature 347:485-487, 1990
    • (1990) Nature , vol.347 , pp. 485-487
    • Alberini, C.M.1    Bet, P.2    Milstein, C.3    Sitia, R.4
  • 27
    • 0017146754 scopus 로고
    • The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin a sepharose
    • KRUSIUS T, FINNE J, RAUVALA H: The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin a sepharose. FEBS Lett 71:117-120, 1976
    • (1976) FEBS Lett , vol.71 , pp. 117-120
    • Krusius, T.1    Finne, J.2    Rauvala, H.3
  • 28
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • KORNFELD R, KORNFELD S: Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631-664, 1985
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 29
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parassitic protozoa and higher eukaryotes
    • MCCONVILLE MJ, FERGUSON MAJ: The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parassitic protozoa and higher eukaryotes. Biochem J 294:305-324, 1993
    • (1993) Biochem J , vol.294 , pp. 305-324
    • Mcconville, M.J.1    Ferguson, M.A.J.2
  • 30
    • 0025895044 scopus 로고
    • Mannosamine, a novel inhibitor of glycosylphosphatidylinositol incorporation into proteins
    • LISANTI MP, FIELD MC, CARAS IW, MENON AK, RODRIGUEZ-BOULAN E: Mannosamine, a novel inhibitor of glycosylphosphatidylinositol incorporation into proteins. EMBO J 10:1969-1977, 1991
    • (1991) EMBO J , vol.10 , pp. 1969-1977
    • Lisanti, M.P.1    Field, M.C.2    Caras, I.W.3    Menon, A.K.4    Rodriguez-Boulan, E.5
  • 32
    • 0027230527 scopus 로고
    • Inhibition of glycosylphosphatidylinositol biosynthesis in Leishmania mexicana by mannosamine
    • FIELD MC, MEDINA-ACOSTA E, CROOS GAM: Inhibition of glycosylphosphatidylinositol biosynthesis in Leishmania mexicana by mannosamine. J Biol Chem 268:9570-9577, 1993
    • (1993) J Biol Chem , vol.268 , pp. 9570-9577
    • Field, M.C.1    Medina-Acosta, E.2    Croos, G.A.M.3
  • 33
    • 0026488395 scopus 로고
    • Proteins containing an uncleaved signal for glycosylphosphatidylinositol membrane anchor attachment are retained in a post-ER compartment
    • MORAN P, CARAS IW: Proteins containing an uncleaved signal for glycosylphosphatidylinositol membrane anchor attachment are retained in a post-ER compartment. J Cell Biol 119:763-772, 1992
    • (1992) J Cell Biol , vol.119 , pp. 763-772
    • Moran, P.1    Caras, I.W.2
  • 34
    • 0022388742 scopus 로고
    • The effect of mannosamine on the formation of lipid-linked oligosaccharides and glycoproteins in canine kidney cells
    • PAN YT, ELBEIN AD: The effect of mannosamine on the formation of lipid-linked oligosaccharides and glycoproteins in canine kidney cells. Archiv Biochem Biophys 242:447-456, 1985
    • (1985) Archiv Biochem Biophys , vol.242 , pp. 447-456
    • Pan, Y.T.1    Elbein, A.D.2
  • 35
    • 0027511479 scopus 로고
    • Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1
    • CAMPADELLI G, BRANDIMARTI R, DI LAZZARO C, WARD PL, ROIZMAN B, TORRISI MR: Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1. Proc Nat Acad Sci USA 90:2798-2802, 1993
    • (1993) Proc Nat Acad Sci USA , vol.90 , pp. 2798-2802
    • Campadelli, G.1    Brandimarti, R.2    Di Lazzaro, C.3    Ward, P.L.4    Roizman, B.5    Torrisi, M.R.6
  • 36
    • 0021001213 scopus 로고
    • Perturbation of the structure and function of the Golgi complex by monovalent carboxylic ionophores
    • TARTAKOFF AM: Perturbation of the structure and function of the Golgi complex by monovalent carboxylic ionophores. Meth Enzymol 98:47-59, 1983
    • (1983) Meth Enzymol , vol.98 , pp. 47-59
    • Tartakoff, A.M.1
  • 37
    • 0024591235 scopus 로고
    • Rapid distribution of Golgi proteins into ER in cells treated with brefeldin A: Evidence for the membrane cycling from the Golgi to ER
    • LIPPINCOTT-SCHWARTZ L, YAUN L, BONIFACINO S, KLAUSNER RD: Rapid distribution of Golgi proteins into ER in cells treated with brefeldin A: Evidence for the membrane cycling from the Golgi to ER. Cell 56:801-813, 1989
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, L.1    Yaun, L.2    Bonifacino, S.3    Klausner, R.D.4
  • 38
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • GETHING M-J, SABROOK J: Protein folding in the cell. Nature 355:33-45, 1992
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sabrook, J.2
  • 39
    • 0014870017 scopus 로고
    • Tamm-Horsfall urinary glycoprotein: The subunit structure
    • FLETCHER AP, NEUBERGER A, RATCLIFFE WA: Tamm-Horsfall urinary glycoprotein: The subunit structure. Biochem J 120:425-432, 1970
    • (1970) Biochem J , vol.120 , pp. 425-432
    • Fletcher, A.P.1    Neuberger, A.2    Ratcliffe, W.A.3
  • 40
    • 0017625667 scopus 로고
    • Physical properties of Tamm-Horsfall glycoprotein and its glycopeptide
    • HAMLIN LM, FISH WW: Physical properties of Tamm-Horsfall glycoprotein and its glycopeptide. Int J Peptide Protein Res 10:270-276, 1977
    • (1977) Int J Peptide Protein Res , vol.10 , pp. 270-276
    • Hamlin, L.M.1    Fish, W.W.2
  • 41
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • BRAAKMAN I, HOOVER-LITTY H, WAGNAR KR, HELENIUS A: Folding of influenza hemagglutinin in the endoplasmic reticulum. J Cell Biol 114:401-411, 1991
    • (1991) J Cell Biol , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagnar, K.R.3    Helenius, A.4
  • 42
    • 0023292949 scopus 로고
    • A vesicular intermediate in the transport of hepatoma secretory proteins from ER to the Golgi complex
    • LODISH H, KONG N, HIRANI S, RUSMUSSEN J: A vesicular intermediate in the transport of hepatoma secretory proteins from ER to the Golgi complex. J Cell Biol 104:221-230, 1987
    • (1987) J Cell Biol , vol.104 , pp. 221-230
    • Lodish, H.1    Kong, N.2    Hirani, S.3    Rusmussen, J.4
  • 43
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gaslp transport from endoplasmic reticulum in COP II vesicles
    • DOERING TL, SCHEKMAN R: GPI anchor attachment is required for Gaslp transport from endoplasmic reticulum in COP II vesicles. EMRO J 15:182-196, 1996
    • (1996) EMRO J , vol.15 , pp. 182-196
    • Doering, T.L.1    Schekman, R.2
  • 44
    • 0028237432 scopus 로고
    • Retention and degradation of protein containing uncleaved glycosylphosphatidylinositol signal
    • FIELD MC, MORAN P, LI W, KELLER GA, CARAS J W: Retention and degradation of protein containing uncleaved glycosylphosphatidylinositol signal. J Biol Chem 269:10830-10837, 1994
    • (1994) J Biol Chem , vol.269 , pp. 10830-10837
    • Field, M.C.1    Moran, P.2    Li, W.3    Keller, G.A.4    Caras, J.W.5
  • 45
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored protein to glycolipidenriched membrane subdomains during transport to the apieal cell surface
    • BROWN DA, ROSE JK: Sorting of GPI-anchored protein to glycolipidenriched membrane subdomains during transport to the apieal cell surface. Cell 68:533-544, 1992
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 46
    • 0027275642 scopus 로고
    • Signal trasducing molecules and glycosylphosphatidylinositol-linked proteins from a caveolin-rich insoluble complex in MDCK cells
    • SARGIACOMO M, SUDOL M, TANG ZL, LISANTI MP: Signal trasducing molecules and glycosylphosphatidylinositol-linked proteins from a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 122:789-807, 1993
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.L.3    Lisanti, M.P.4
  • 47
    • 0026570855 scopus 로고
    • GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney
    • FUKUOKA S-I, FREEDMAN SD, YU H, SUKHATME VP, SCHEELE GA: GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney. Proc Nat Acad Sci USA 89:1189-1193, 1992
    • (1992) Proc Nat Acad Sci USA , vol.89 , pp. 1189-1193
    • Fukuoka, S.-I.1    Freedman, S.D.2    Yu, H.3    Sukhatme, V.P.4    Scheele, G.A.5
  • 48
    • 0027412124 scopus 로고
    • Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: Implication of GP-2
    • LEBLOND FA, VIAU G, LAINE J, LEBEL D: Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: Implication of GP-2. Biochem J 291:289-296, 1993
    • (1993) Biochem J , vol.291 , pp. 289-296
    • Leblond, F.A.1    Viau, G.2    Laine, J.3    Lebel, D.4
  • 49
    • 0022406053 scopus 로고
    • Ultrastructural localization of Tamm- Horsfall glycoprutein (THP) in rat kidney as revealed by protein-gold immunocytochemistry
    • BACHMANN S, KOEPPHAGEMA I, KRIZ W: Ultrastructural localization of Tamm- Horsfall glycoprutein (THP) in rat kidney as revealed by protein-gold immunocytochemistry. Histochemistry 83:531-538, 1985
    • (1985) Histochemistry , vol.83 , pp. 531-538
    • Bachmann, S.1    Koepphagema, I.2    Kriz, W.3
  • 52
    • 0018886290 scopus 로고
    • Tubulointerstitial immune complex nephritis in rats immunized with Tamm-Horsfall protein
    • HOYER JR: Tubulointerstitial immune complex nephritis in rats immunized with Tamm-Horsfall protein. Kidney Int 17:284-292, 1980
    • (1980) Kidney Int , vol.17 , pp. 284-292
    • Hoyer, J.R.1
  • 53
    • 0017819924 scopus 로고
    • Pathological localization of Tamm-Horsfall glycoprotein in interstitial deposits in renal disease
    • ZAGER RA, COTRAN RS, HOYER JR: Pathological localization of Tamm-Horsfall glycoprotein in interstitial deposits in renal disease. Lab Invest 38:52-75, 1978
    • (1978) Lab Invest , vol.38 , pp. 52-75
    • Zager, R.A.1    Cotran, R.S.2    Hoyer, J.R.3
  • 54
    • 0017264862 scopus 로고
    • Auto-antibodies to Tamm-Horsfall protein, a tool for diagnosing the level of urinary-tract infection
    • HANSON LA, FASTH A, JODAL U: Auto-antibodies to Tamm-Horsfall protein, a tool for diagnosing the level of urinary-tract infection. Lancet 1:226-228, 1976
    • (1976) Lancet , vol.1 , pp. 226-228
    • Hanson, L.A.1    Fasth, A.2    Jodal, U.3
  • 56
    • 0025190333 scopus 로고
    • Activation of the inflammatory response of neutrophils by Tamm-Horsfall glycoprotein
    • HORTON JK, DAVIES M, TOPLEY N, THOMAS D, WILLIAMS JD: Activation of the inflammatory response of neutrophils by Tamm-Horsfall glycoprotein. Kidney Int 37:717-726, 1990
    • (1990) Kidney Int , vol.37 , pp. 717-726
    • Horton, J.K.1    Davies, M.2    Topley, N.3    Thomas, D.4    Williams, J.D.5
  • 57
    • 0027326798 scopus 로고
    • Tamm-Horsfall protein binds to a single class of carbohydrate specific receptors on human neutrophils
    • THOMAS DBL, DAVIES M, PETERS JR, WILLIAMS JD: Tamm-Horsfall protein binds to a single class of carbohydrate specific receptors on human neutrophils. Kidney Int 44:423-429, 1993
    • (1993) Kidney Int , vol.44 , pp. 423-429
    • Thomas, D.B.L.1    Davies, M.2    Peters, J.R.3    Williams, J.D.4


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