메뉴 건너뛰기




Volumn 19, Issue , 1999, Pages 173-195

Receptor-mediated endocytosis of cobalamin (vitamin B12)

Author keywords

Cell surface receptors; Intrinsic factor; Receptor mediated endocytosis; Transcobalamin II

Indexed keywords

CYANOCOBALAMIN;

EID: 0032788555     PISSN: 01999885     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.nutr.19.1.173     Document Type: Review
Times cited : (72)

References (93)
  • 1
    • 0025000784 scopus 로고
    • Expression of transcobalamin II receptors by human leukemia K-562 and HL-60 cells
    • 1. Amagaski T, Green R, Jacobsen DW. 1990. Expression of transcobalamin II receptors by human leukemia K-562 and HL-60 cells. Blood 76:1380-86
    • (1990) Blood , vol.76 , pp. 1380-1386
    • Amagaski, T.1    Green, R.2    Jacobsen, D.W.3
  • 3
    • 0028981079 scopus 로고
    • Unusual processing of gp280, a protein associated with microvillar areas of yolk sac plasma membrane delivery of immature protein
    • 3. Baricault L, Galceran M, Ronco PM, Truganan G, Verroust PJ. 1995. Unusual processing of gp280, a protein associated with microvillar areas of yolk sac plasma membrane delivery of immature protein. Biochem. Biophys. Res. Commun. 212:353-59
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 353-359
    • Baricault, L.1    Galceran, M.2    Ronco, P.M.3    Truganan, G.4    Verroust, P.J.5
  • 4
    • 0025124497 scopus 로고
    • Transcobalamin II deficiency presenting with methylmalonic aciduria and homocystinuria and abnormal absorption of cobalamin
    • 4. Barshop BA, Wolf J, Nyhan WL, Yu A, Pronodos C, et al. 1990. Transcobalamin II deficiency presenting with methylmalonic aciduria and homocystinuria and abnormal absorption of cobalamin. Am. J. Med. Genet. 35:222-28
    • (1990) Am. J. Med. Genet. , vol.35 , pp. 222-228
    • Barshop, B.A.1    Wolf, J.2    Nyhan, W.L.3    Yu, A.4    Pronodos, C.5
  • 6
    • 0032569017 scopus 로고    scopus 로고
    • Brefeldin A (BFA) inhibits the basolateral membrane delivery and dimerization of transcobalamin in human intestinal epithelial Caco-2 cells
    • 6. Bose S, Chapin SJ, Seetharam S, Feix J, Mostov KE, Seetharam B. 1998. Brefeldin A (BFA) inhibits the basolateral membrane delivery and dimerization of transcobalamin in human intestinal epithelial Caco-2 cells. J. Biol. Chem. 273:16163-69
    • (1998) J. Biol. Chem. , vol.273 , pp. 16163-16169
    • Bose, S.1    Chapin, S.J.2    Seetharam, S.3    Feix, J.4    Mostov, K.E.5    Seetharam, B.6
  • 7
    • 0009570872 scopus 로고    scopus 로고
    • Bipolar functional expression of transcobalamin II receptor in human intestinal polarized Caco-2 cells
    • 7. Bose S, Dahms NM, Seetharam S, Seetharam B. 1997. Bipolar functional expression of transcobalamin II receptor in human intestinal polarized Caco-2 cells. J. Biol. Chem. 272:11718-25
    • (1997) J. Biol. Chem. , vol.272 , pp. 11718-11725
    • Bose, S.1    Dahms, N.M.2    Seetharam, S.3    Seetharam, B.4
  • 8
    • 0029939662 scopus 로고    scopus 로고
    • Dimerization of transcobalamin II-receptor: Requirement of a structurally ordered lipid bilayer
    • 8. Bose S, Feix J, Seetharam S, Seetharam B. 1996. Dimerization of transcobalamin II-receptor: requirement of a structurally ordered lipid bilayer. J. Biol. Chem. 271: 11718-25
    • (1996) J. Biol. Chem. , vol.271 , pp. 11718-11725
    • Bose, S.1    Feix, J.2    Seetharam, S.3    Seetharam, B.4
  • 10
    • 0030795115 scopus 로고    scopus 로고
    • Effect of disulfide bonds of transcobalamin II-receptor on its activity and basolateral targeting in human intestinal epithelial Caco-2 cells
    • 10. Bose S, Seetharam B. 1997. Effect of disulfide bonds of transcobalamin II-receptor on its activity and basolateral targeting in human intestinal epithelial Caco-2 cells. J. Biol. Chem. 272:20920-28
    • (1997) J. Biol. Chem. , vol.272 , pp. 20920-20928
    • Bose, S.1    Seetharam, B.2
  • 11
    • 0029147372 scopus 로고
    • Regulation of expression of transcobalamin II-receptor in the rat
    • 11. Bose S, Seetharam S, Hammond TG, Seetharam B. 1995. Regulation of expression of transcobalamin II-receptor in the rat. Biochem. J. 310:923-29
    • (1995) Biochem. J. , vol.310 , pp. 923-929
    • Bose, S.1    Seetharam, S.2    Hammond, T.G.3    Seetharam, B.4
  • 12
    • 0028907546 scopus 로고
    • Membrane expression and interactions of human transcobalamin II receptor
    • 12. Bose S, Seetharam S, Seetharam B. 1995. Membrane expression and interactions of human transcobalamin II receptor. J. Biol. Chem. 270:8152-57
    • (1995) J. Biol. Chem. , vol.270 , pp. 8152-8157
    • Bose, S.1    Seetharam, S.2    Seetharam, B.3
  • 13
    • 0027052270 scopus 로고
    • Transcobalamin II-cobalamin binding sites are present on rabbit germ cells
    • 13. Boukhzer E, Ennya A, Felden F, Gerard A, Nexo E, et al. 1992. Transcobalamin II-cobalamin binding sites are present on rabbit germ cells. Biochim. Biophys. Acta 1175:128-31
    • (1992) Biochim. Biophys. Acta , vol.1175 , pp. 128-131
    • Boukhzer, E.1    Ennya, A.2    Felden, F.3    Gerard, A.4    Nexo, E.5
  • 17
    • 0031000306 scopus 로고    scopus 로고
    • Transcobalamin II-receptor imaging via radiolabeled diethyl-triaminepentaacetate cobalamin analogs
    • 17. Collins DA, Hogenkemp HPC. 1997. Transcobalamin II-receptor imaging via radiolabeled diethyl-triaminepentaacetate cobalamin analogs. J. Nucl. Med. 38:717-23
    • (1997) J. Nucl. Med. , vol.38 , pp. 717-723
    • Collins, D.A.1    Hogenkemp, H.P.C.2
  • 19
    • 0028304450 scopus 로고
    • Transcytosis and processing of intrinsic factor-cobalamin in Caco-2 cells
    • 19. Dan N, Cutler DF, 1994. Transcytosis and processing of intrinsic factor-cobalamin in Caco-2 cells. J. Biol. Chem. 269:18849-55
    • (1994) J. Biol. Chem. , vol.269 , pp. 18849-18855
    • Dan, N.1    Cutler, D.F.2
  • 22
    • 0031748686 scopus 로고    scopus 로고
    • Overexpression of an unstable intrinsic factor-cobalamin receptor in Imerslund-Grasbeck syndrome
    • 22. Eaton DM, Livingston JH, Seetharam B, Puntis JW. 1998. Overexpression of an unstable intrinsic factor-cobalamin receptor in Imerslund-Grasbeck syndrome. Gastroenterology 115:173-76
    • (1998) Gastroenterology , vol.115 , pp. 173-176
    • Eaton, D.M.1    Livingston, J.H.2    Seetharam, B.3    Puntis, J.W.4
  • 23
    • 0000443712 scopus 로고
    • Inherited disorders of cobalamin transport and metabolism
    • ed. CR Scriver, AL Beaudet, WS Sly, D Valle. New York: MacGraw Hill. 7th ed.
    • 23. Fenton WA, Rosenberg LE. 1995. Inherited disorders of cobalamin transport and metabolism. In Metabolic Basis of Inherited Disease, ed. CR Scriver, AL Beaudet, WS Sly, D Valle, pp. 3111-28. New York: MacGraw Hill. 7th ed.
    • (1995) Metabolic Basis of Inherited Disease , pp. 3111-3128
    • Fenton, W.A.1    Rosenberg, L.E.2
  • 24
    • 17344369621 scopus 로고    scopus 로고
    • Disruption of a regulatory system involving cobalamin distribution and function in a methionine-dependent human glioma cell line
    • 24. Fiskerstrand T, Reidel B, Uleland PM, Seetharam B, Pezacka EH, et al. 1998. Disruption of a regulatory system involving cobalamin distribution and function in a methionine-dependent human glioma cell line. J. Biol. Chem. 273:20180-84
    • (1998) J. Biol. Chem. , vol.273 , pp. 20180-20184
    • Fiskerstrand, T.1    Reidel, B.2    Uleland, P.M.3    Seetharam, B.4    Pezacka, E.H.5
  • 25
    • 0026068730 scopus 로고
    • Inherited selective cobalamin malabsorption and cobalamin deficiency in dogs
    • 25. Fyfe JC, Giger U, Hall CA, Jezyk PF, Klumpp SA, et al. 1991. Inherited selective cobalamin malabsorption and cobalamin deficiency in dogs. Pediatr. Res. 29:24-31
    • (1991) Pediatr. Res. , vol.29 , pp. 24-31
    • Fyfe, J.C.1    Giger, U.2    Hall, C.A.3    Jezyk, P.F.4    Klumpp, S.A.5
  • 26
    • 0025865890 scopus 로고
    • Defective brush border expression of intrinsic-factor cobalamin receptor in inherited selective intestinal cobalamin malabsorption
    • 26. Fyfe JC, Ramanujam KS, Ramaswamy K, Patterson DF, Seetharam B. 1991. Defective brush border expression of intrinsic-factor cobalamin receptor in inherited selective intestinal cobalamin malabsorption. J. Biol. Chem. 266:4489-94
    • (1991) J. Biol. Chem. , vol.266 , pp. 4489-4494
    • Fyfe, J.C.1    Ramanujam, K.S.2    Ramaswamy, K.3    Patterson, D.F.4    Seetharam, B.5
  • 27
    • 0028796861 scopus 로고
    • Cathepsin L mediates intracellular ileal digestion of gastric intrinsic factor
    • 27. Gordon MM, Howard T, Becich MJ, Alpers DH. 1995. Cathepsin L mediates intracellular ileal digestion of gastric intrinsic factor. Am. J. Physiol. 268:G33-40
    • (1995) Am. J. Physiol. , vol.268
    • Gordon, M.M.1    Howard, T.2    Becich, M.J.3    Alpers, D.H.4
  • 28
    • 0025862978 scopus 로고
    • Glycosylation is not required for ligand or receptor binding by expressed rat intrinsic factor
    • 28. Gordon MM, Hu C, Chokshi H, Hewitt JE, Alpers DH. 1991. Glycosylation is not required for ligand or receptor binding by expressed rat intrinsic factor. Am. J. Physiol. 260:736-42
    • (1991) Am. J. Physiol. , vol.260 , pp. 736-742
    • Gordon, M.M.1    Hu, C.2    Chokshi, H.3    Hewitt, J.E.4    Alpers, D.H.5
  • 29
    • 0014452421 scopus 로고
    • 12 transport proteins
    • ed. EB Brown, CV Moore. New York: Grune & Stratton
    • 12 transport proteins. In Progress in Hematology, ed. EB Brown, CV Moore, 6:233-60. New York: Grune & Stratton
    • (1969) Progress in Hematology , vol.6 , pp. 233-260
    • Grasbeck, R.1
  • 32
    • 0026548585 scopus 로고
    • Receptor mediated endocytosis of the intrinsic factor-cobalamin complex in HT29, a human colon carcinoma cell line
    • 32. Gueant JL, Masson C, Schohn H, Girr M, Saunier M, Nicolas JP. 1992. Receptor mediated endocytosis of the intrinsic factor-cobalamin complex in HT29, a human colon carcinoma cell line. FEBS Lett. 297:229-32
    • (1992) FEBS Lett. , vol.297 , pp. 229-232
    • Gueant, J.L.1    Masson, C.2    Schohn, H.3    Girr, M.4    Saunier, M.5    Nicolas, J.P.6
  • 33
    • 0029051308 scopus 로고
    • Decreased activity of intestinal and urinary intrinsic factor in Imerslund-Grasbeck syndrome
    • 33. Gueant JL, Saunier M, Gastin I, Safi A, Lamireau T, et al. 1995. Decreased activity of intestinal and urinary intrinsic factor in Imerslund-Grasbeck syndrome. Gastroenterology 108:1622-28
    • (1995) Gastroenterology , vol.108 , pp. 1622-1628
    • Gueant, J.L.1    Saunier, M.2    Gastin, I.3    Safi, A.4    Lamireau, T.5
  • 36
    • 0026094535 scopus 로고
    • Human gastric intrinsic factor: Characterization of cDNA and genomic clones and localization to human chromosome 11
    • 36. Hewitt JE, Gordon MM, Taggart T, Mohandas TK, Alpers DH. 1991. Human gastric intrinsic factor: characterization of cDNA and genomic clones and localization to human chromosome 11. Genomics 10:432-40
    • (1991) Genomics , vol.10 , pp. 432-440
    • Hewitt, J.E.1    Gordon, M.M.2    Taggart, T.3    Mohandas, T.K.4    Alpers, D.H.5
  • 37
    • 0029857228 scopus 로고    scopus 로고
    • Human gastric intrinsic factor expression is not restricted to parietal cells
    • 37. Howard TA, Misra DN, Grove M, Becich MJ, Shao J-S, et al. 1996. Human gastric intrinsic factor expression is not restricted to parietal cells. J. Anat. 189:303-13
    • (1996) J. Anat. , vol.189 , pp. 303-313
    • Howard, T.A.1    Misra, D.N.2    Grove, M.3    Becich, M.J.4    Shao, J.-S.5
  • 38
    • 0025923631 scopus 로고
    • 12 transport by rat liver lysosomal membrane vesicles
    • 12 transport by rat liver lysosomal membrane vesicles. J. Biol. Chem. 266:9438-41
    • (1992) J. Biol. Chem. , vol.266 , pp. 9438-9441
    • Idriss, J.M.1    Jonas, A.J.2
  • 39
    • 72849184034 scopus 로고
    • Idiopathic chronic megaloblastic anemia in children
    • 39. Imerslund O. 1960. Idiopathic chronic megaloblastic anemia in children. Acta Pediatr. Scand. 49(Suppl. 119): 1-115
    • (1960) Acta Pediatr. Scand. , vol.49 , Issue.SUPPL. 119 , pp. 1-115
    • Imerslund, O.1
  • 40
    • 0024434211 scopus 로고
    • Structure and expression of the cDNA encoding transcobalamin I, a neutrophil granule protein
    • 40. Johnston J, Bollekens J, Allen RH, Berliner N. 1989. Structure and expression of the cDNA encoding transcobalamin I, a neutrophil granule protein. J. Biol. Chem. 264: 15754-57
    • (1989) J. Biol. Chem. , vol.264 , pp. 15754-15757
    • Johnston, J.1    Bollekens, J.2    Allen, R.H.3    Berliner, N.4
  • 41
    • 0026596803 scopus 로고
    • Genomic structure and mapping of the chromosomal gene for transcobalamin I (TCN1): Comparison to human intrinsic factor
    • 41. Johnston J, Yang-Feng T, Berliner N. 1992. Genomic structure and mapping of the chromosomal gene for transcobalamin I (TCN1): comparison to human intrinsic factor. Genomics 12:459-64
    • (1992) Genomics , vol.12 , pp. 459-464
    • Johnston, J.1    Yang-Feng, T.2    Berliner, N.3
  • 42
    • 0023663543 scopus 로고
    • Oligosaccharyl transferase: The central enzyme in the pathway of glycoprotein assembly
    • 42. Kaplan HA, Welply JK, Lennarz WJ. 1987. Oligosaccharyl transferase: the central enzyme in the pathway of glycoprotein assembly. Biochim. Biophys. Acta 906:161-73
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 161-173
    • Kaplan, H.A.1    Welply, J.K.2    Lennarz, W.J.3
  • 43
    • 0032525203 scopus 로고    scopus 로고
    • 12 receptor, cubulin: Molecular characterization and chromosomal mapping of the gene to 10p wilhin the autosomal recessive megaloblastic anemia (MGAI) region
    • 12 receptor, cubulin: molecular characterization and chromosomal mapping of the gene to 10p wilhin the autosomal recessive megaloblastic anemia (MGAI) region. Blood 91:3593-600
    • (1998) Blood , vol.91 , pp. 3593-3600
    • Kozyraki, R.1    Kristiansen, M.2    Silahtaroglu, A.3    Hansen, C.4    Jacobsen, C.5
  • 44
    • 0029073103 scopus 로고
    • Immunofunctional properties of a yolk sac epithelial cell line expressing two proteins gp280 and megalin of the intramicrovilar area of proximal tubule cells: Inhibition of endocytosis by the specific antibodies
    • 44. LePanse S, Galceran M, Ponotilion F, Le-Longt B, Van de Putte M, et al. 1995. Immunofunctional properties of a yolk sac epithelial cell line expressing two proteins gp280 and megalin of the intramicrovilar area of proximal tubule cells: inhibition of endocytosis by the specific antibodies. Eur. J. Cell Biol. 67:120-29
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 120-129
    • LePanse, S.1    Galceran, M.2    Ponotilion, F.3    Le-Longt, B.4    Van De Putte, M.5
  • 45
    • 0021350826 scopus 로고
    • Immunoelectron microscopic localization of intrinsic factor cobalamin receptor
    • 45. Levine JS, Allen RH, Alpers DH, Seetharam B. 1984. Immunoelectron microscopic localization of intrinsic factor cobalamin receptor. J. Cell Biol. 98:1111-17
    • (1984) J. Cell Biol. , vol.98 , pp. 1111-1117
    • Levine, J.S.1    Allen, R.H.2    Alpers, D.H.3    Seetharam, B.4
  • 46
  • 49
    • 0027989584 scopus 로고
    • Expression of transcobalamin II mRNA in human tissues and cultured fibroblasts form normal and TC II deficient patients
    • 49. Li N, Seetharam S, Rosenblatt DS, Seetharam B. 1994. Expression of transcobalamin II mRNA in human tissues and cultured fibroblasts form normal and TC II deficient patients. Biochem. J. 301:585-90
    • (1994) Biochem. J. , vol.301 , pp. 585-590
    • Li, N.1    Seetharam, S.2    Rosenblatt, D.S.3    Seetharam, B.4
  • 50
    • 0028898342 scopus 로고
    • Genomic organization of human transcobalamin II gene: Comparison to human intrinsic factor and transcobalamin I
    • 50. Li N, Seetharam S, Seetharam B. 1995. Genomic organization of human transcobalamin II gene: comparison to human intrinsic factor and transcobalamin I. Biochem. Biophys. Res. Commun. 208:756-64
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 756-764
    • Li, N.1    Seetharam, S.2    Seetharam, B.3
  • 51
    • 0032568951 scopus 로고    scopus 로고
    • Characterization of the human transcobalamin II promoter: A proximal GC/GT box is a dominant negative element
    • 51. Li N, Seetharam S, Seetharam B. 1998. Characterization of the human transcobalamin II promoter: a proximal GC/GT box is a dominant negative element. J. Biol. Chem. 273:16104-11
    • (1998) J. Biol. Chem. , vol.273 , pp. 16104-16111
    • Li, N.1    Seetharam, S.2    Seetharam, B.3
  • 52
    • 0030024841 scopus 로고    scopus 로고
    • Diphtheria toxin-mediated ablation of parietal cells in the stomach of transgenic mice
    • 52. Li Q, Karam SM, Gordon JI. 1996. Diphtheria toxin-mediated ablation of parietal cells in the stomach of transgenic mice. J. Biol. Chem. 271:3671-76
    • (1996) J. Biol. Chem. , vol.271 , pp. 3671-3676
    • Li, Q.1    Karam, S.M.2    Gordon, J.I.3
  • 53
    • 0024453815 scopus 로고
    • Uptake of transcobalamin II-bound cobalamin by HL-60 cells: Effects of differentiation induction
    • 53. Lindemans J, Kroes ACM, Geel V, van Kapel J, Schoester M, Abels J. 1989. Uptake of transcobalamin II-bound cobalamin by HL-60 cells: effects of differentiation induction. Exp. Cell Res. 184:449-60
    • (1989) Exp. Cell Res. , vol.184 , pp. 449-460
    • Lindemans, J.1    Kroes, A.C.M.2    Geel, V.3    Van Kapel, J.4    Schoester, M.5    Abels, J.6
  • 54
    • 0026776945 scopus 로고
    • Growth hormone (GH) regulation of gastric structure and function in the GH deficient rat: Up-regulation of intrinsic factor
    • 54. Lobie PE, Garcia-Aragon J, Waters MJ. 1992. Growth hormone (GH) regulation of gastric structure and function in the GH deficient rat: up-regulation of intrinsic factor. Endocrinology 130:3015-24
    • (1992) Endocrinology , vol.130 , pp. 3015-3024
    • Lobie, P.E.1    Garcia-Aragon, J.2    Waters, M.J.3
  • 55
    • 0027375279 scopus 로고
    • Use of transgenic mice to study the regulation of gene expression in the parietal cell lineage of gastric units
    • 55. Lorenz RG, Gordon JI. 1993. Use of transgenic mice to study the regulation of gene expression in the parietal cell lineage of gastric units. J. Biol. Chem. 268:26559-70
    • (1993) J. Biol. Chem. , vol.268 , pp. 26559-26570
    • Lorenz, R.G.1    Gordon, J.I.2
  • 57
    • 0032570583 scopus 로고    scopus 로고
    • 12 receptor and target of teratogenic antibodies is a megalin-binding peripheral protein with homology to developmental proteins
    • 12 receptor and target of teratogenic antibodies is a megalin-binding peripheral protein with homology to developmental proteins. J. Biol. Chem. 273:5235-42
    • (1998) J. Biol. Chem. , vol.273 , pp. 5235-5242
    • Moestrup, S.K.1    Kozyarki, R.2    Kristiansen, M.3    Kaysen, J.H.4    Rasmussen, H.H.5
  • 58
    • 0025880644 scopus 로고
    • The cDNA sequence and the deduced amino acid sequence of human transcobalamin II show homology with rat intrinsic factor and human transcobalamin I
    • 58. Platica O, Janeczko R, Quadros EV, Regec A, Romain R, Rothenberg SP. 1991. The cDNA sequence and the deduced amino acid sequence of human transcobalamin II show homology with rat intrinsic factor and human transcobalamin I. J. Biol. Chem. 266:7860-63
    • (1991) J. Biol. Chem. , vol.266 , pp. 7860-7863
    • Platica, O.1    Janeczko, R.2    Quadros, E.V.3    Regec, A.4    Romain, R.5    Rothenberg, S.P.6
  • 59
    • 0029930159 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies to epitopes of human transcobalamin II
    • 59. Quadros EV, Rothenberg SP, McLoughlin P. 1996. Characterization of monoclonal antibodies to epitopes of human transcobalamin II. Biochem. Biophys. Res. Commun. 222:149-54
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 149-154
    • Quadros, E.V.1    Rothenberg, S.P.2    McLoughlin, P.3
  • 61
    • 0025873513 scopus 로고
    • Functional expression of intrinsic factor-cobalamin receptor by renal proximal tubular epithelial cells
    • 61. Ramanujam KS, Seetharam S, Dahms N, Seetharam B. 1991. Functional expression of intrinsic factor-cobalamin receptor by renal proximal tubular epithelial cells. J. Biol. Chem. 266:13135-40
    • (1991) J. Biol. Chem. , vol.266 , pp. 13135-13140
    • Ramanujam, K.S.1    Seetharam, S.2    Dahms, N.3    Seetharam, B.4
  • 62
    • 0027949405 scopus 로고
    • Effect of processing inhibitors on cobalamin transcytosis in polarized opossum kidney cells
    • 62. Ramanujam KS, Seetharam S, Dahms NM, Seetharam B. 1994. Effect of processing inhibitors on cobalamin transcytosis in polarized opossum kidney cells. Arch. Biochem. Biophys. 315:8-15
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 8-15
    • Ramanujam, K.S.1    Seetharam, S.2    Dahms, N.M.3    Seetharam, B.4
  • 63
    • 0025753579 scopus 로고
    • Cellular expression of cobalamin transport proteins and cobalamin transcytosis in human colon adenocarcinoma cells
    • 63. Ramanujam KS, Seetharam S, Ramasamy M, Seetharam B. 1991. Cellular expression of cobalamin transport proteins and cobalamin transcytosis in human colon adenocarcinoma cells. Am. J. Physiol. 260: G416-22
    • (1991) Am. J. Physiol. , vol.260
    • Ramanujam, K.S.1    Seetharam, S.2    Ramasamy, M.3    Seetharam, B.4
  • 64
    • 0025995913 scopus 로고
    • Synthesis and secretion of cobalamin binding proteins by opossum kidney cells
    • 64. Ramanujam KS, Seetharam S, Seetharam B. 1991. Synthesis and secretion of cobalamin binding proteins by opossum kidney cells. Biochem. Biophys. Res. Commun. 179:543-50
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 543-550
    • Ramanujam, K.S.1    Seetharam, S.2    Seetharam, B.3
  • 65
    • 0026542764 scopus 로고
    • Leupeptin and ammonium chloride inhibit cellular transcytosis of cobalamin in opossum kidney cells
    • 65. Ramanujam KS, Seetharam S, Seetharam B. 1992. Leupeptin and ammonium chloride inhibit cellular transcytosis of cobalamin in opossum kidney cells. Biochem. Biophys. Res. Commun. 182:439-46
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 439-446
    • Ramanujam, K.S.1    Seetharam, S.2    Seetharam, B.3
  • 66
    • 0027509803 scopus 로고
    • Intrinsic factor-cobalamin receptor activity in a marsupial, the American opossum (Didelphis virginiana)
    • 66. Ramanujam KS, Seetharam S, Seetharam B. 1993. Intrinsic factor-cobalamin receptor activity in a marsupial, the American opossum (Didelphis virginiana). Comp. Biochem. Physiol. 104:771-5
    • (1993) Comp. Biochem. Physiol. , vol.104 , pp. 771-775
    • Ramanujam, K.S.1    Seetharam, S.2    Seetharam, B.3
  • 67
    • 0027511650 scopus 로고
    • Regulated expression of intrinsic factor-cobalamin receptor by rat visceral yolk sac and placental membranes
    • 67. Ramanujam KS, Seetharam S, Seetharam B. 1993. Regulated expression of intrinsic factor-cobalamin receptor by rat visceral yolk sac and placental membranes. Biochim. Biophys. Acta 1146:243-46
    • (1993) Biochim. Biophys. Acta , vol.1146 , pp. 243-246
    • Ramanujam, K.S.1    Seetharam, S.2    Seetharam, B.3
  • 68
    • 0024378767 scopus 로고
    • Cobalamin release from intrinsic factor and transfer to transcobalamin II within the rat enterocyte
    • 68. Ramasamy M, Alpers DH, Tiruppathi C, Seetharam B. 1989. Cobalamin release from intrinsic factor and transfer to transcobalamin II within the rat enterocyte. Am. J. Physiol. 257:G791-97
    • (1989) Am. J. Physiol. , vol.257
    • Ramasamy, M.1    Alpers, D.H.2    Tiruppathi, C.3    Seetharam, B.4
  • 69
    • 0022413725 scopus 로고
    • Intrinsic factor-cobalamin accumulates in the ilea of mice treated with chloroquine
    • 69. Robertson JA, Gallagher ND. 1985. Intrinsic factor-cobalamin accumulates in the ilea of mice treated with chloroquine. Gastroenterology 89:1353-59
    • (1985) Gastroenterology , vol.89 , pp. 1353-1359
    • Robertson, J.A.1    Gallagher, N.D.2
  • 71
    • 0028815179 scopus 로고
    • Intrinsic factor covalently bound to sepharose affinity medium for the purification of a soluble intrinsic factor receptor from human urine
    • 71. Safi A, Saunier M, Gastin I, Alibada Y, Dugue B, Gueant JL. 1995. Intrinsic factor covalently bound to sepharose affinity medium for the purification of a soluble intrinsic factor receptor from human urine. J. Chromatol. 664:253-59
    • (1995) J. Chromatol. , vol.664 , pp. 253-259
    • Safi, A.1    Saunier, M.2    Gastin, I.3    Alibada, Y.4    Dugue, B.5    Gueant, J.L.6
  • 72
    • 0023948431 scopus 로고
    • Characterization of a 280 protein restricted to the coated pits of the renal brush border and the epithelial cells of the yolk sac
    • 72. Sahali D, Mulliez N, Chatlet F, Dupuis R, Ronco P, Verroust PJ. 1988. Characterization of a 280 protein restricted to the coated pits of the renal brush border and the epithelial cells of the yolk sac. J. Exp. Med. 167:213-18
    • (1988) J. Exp. Med. , vol.167 , pp. 213-218
    • Sahali, D.1    Mulliez, N.2    Chatlet, F.3    Dupuis, R.4    Ronco, P.5    Verroust, P.J.6
  • 73
    • 0026585415 scopus 로고
    • Coexpression in man by kidney and fetal envelopes of a 280 kDa coated pit restricted protein: Similarity with the murine target of teralogenic antibodies
    • 73. Sahali D, Mulliez N, Chatelet F, Laurent-Winter C, Citadelle D, et al. 1992. Coexpression in man by kidney and fetal envelopes of a 280 kDa coated pit restricted protein: similarity with the murine target of teralogenic antibodies. Am. J. Pathol. 140:33-44
    • (1992) Am. J. Pathol. , vol.140 , pp. 33-44
    • Sahali, D.1    Mulliez, N.2    Chatelet, F.3    Laurent-Winter, C.4    Citadelle, D.5
  • 75
    • 0024804201 scopus 로고
    • 12 absorption and malabsorption
    • 12 absorption and malabsorption. Gut 30:1686-91
    • (1989) Gut , vol.30 , pp. 1686-1691
    • Schonsby, H.1
  • 76
    • 0001111389 scopus 로고
    • Gastric intrinsic factor and cobalamin absorption
    • ed. L Johnson. New York: Raven
    • 76. Seetharam B. 1994. Gastric intrinsic factor and cobalamin absorption. In Physiology of the Gastrointestinal Tract, ed. L Johnson, pp. 1997-2026. New York: Raven
    • (1994) Physiology of the Gastrointestinal Tract , pp. 1997-2026
    • Seetharam, B.1
  • 77
    • 0022048408 scopus 로고
    • Cellular uptake of cobalamin
    • 77. Seetharam B, Alpers DH. 1985. Cellular uptake of cobalamin. Nutr. Rev. 43:97-102
    • (1985) Nutr. Rev. , vol.43 , pp. 97-102
    • Seetharam, B.1    Alpers, D.H.2
  • 78
    • 0001573103 scopus 로고
    • Gastric intrinsic factor and cobalamin absorption
    • ed. SG Schultz. Washington, DC: Am. Physiol. Soc.
    • 78. Seetharam B, Alpers DH. 1991. Gastric intrinsic factor and cobalamin absorption. In Handbook of Physiology, ed. SG Schultz. 4:421-61. Washington, DC: Am. Physiol. Soc.
    • (1991) Handbook of Physiology , vol.4 , pp. 421-461
    • Seetharam, B.1    Alpers, D.H.2
  • 79
    • 0019806801 scopus 로고
    • Interaction of receptor for intrinsic factor-cobalamin complex with synthetic and brush border lipids
    • 79. Seetharam B, Bagur SS, Alpers DH. 1981. Interaction of receptor for intrinsic factor-cobalamin complex with synthetic and brush border lipids. J. Biol. Chem. 256:9813-15
    • (1981) J. Biol. Chem. , vol.256 , pp. 9813-9815
    • Seetharam, B.1    Bagur, S.S.2    Alpers, D.H.3
  • 80
    • 0020025572 scopus 로고
    • Isolation and characterization of proteolytically derived receptor for intrinsic factor-cobalamin
    • 80. Seetharam B, Bagur SS, Alpers DH. 1982. Isolation and characterization of proteolytically derived receptor for intrinsic factor-cobalamin. J. Biol. Chem. 257:183-89
    • (1982) J. Biol. Chem. , vol.257 , pp. 183-189
    • Seetharam, B.1    Bagur, S.S.2    Alpers, D.H.3
  • 81
    • 0030988207 scopus 로고    scopus 로고
    • Identification of rat yolk sac teratogenic antibodies, gp280, as intrinsic factor-cobalamin receptor
    • 81. Seetharam B, Christensen I, Moestrup SK, Hammond TG, Verroust PJ. 1997. Identification of rat yolk sac teratogenic antibodies, gp280, as intrinsic factor-cobalamin receptor. J. Clin. Invest. 99:2317-22
    • (1997) J. Clin. Invest. , vol.99 , pp. 2317-2322
    • Seetharam, B.1    Christensen, I.2    Moestrup, S.K.3    Hammond, T.G.4    Verroust, P.J.5
  • 82
    • 0023885093 scopus 로고
    • Purification, properties and immunochemical localization of a receptor for intrinsic factor-cobalamin complex in the rat kidney
    • 82. Seetharam B, Levine JS, Ramasamy M, Alpers DH. 1988. Purification, properties and immunochemical localization of a receptor for intrinsic factor-cobalamin complex in the rat kidney. J. Biol. Chem. 263:4443-49
    • (1988) J. Biol. Chem. , vol.263 , pp. 4443-4449
    • Seetharam, B.1    Levine, J.S.2    Ramasamy, M.3    Alpers, D.H.4
  • 83
    • 0001913147 scopus 로고
    • Intrinsic factor-cobalamin receptor, an overview
    • ed. HR Bhatt, VHT James, GM Besser, H Keen. Almondsbury, UK: Soc. Endocrinol./ Thomas Addison Soc.
    • 83. Seetharam B, Seetharam S, Li N, Ramanujam KS. 1994. Intrinsic factor-cobalamin receptor, an overview. In Advances in Thomas Addison's Diseases, ed. HR Bhatt, VHT James, GM Besser, H Keen, 2:293-302. Almondsbury, UK: Soc. Endocrinol./ Thomas Addison Soc.
    • (1994) Advances in Thomas Addison's Diseases , vol.2 , pp. 293-302
    • Seetharam, B.1    Seetharam, S.2    Li, N.3    Ramanujam, K.S.4
  • 85
    • 0026661986 scopus 로고
    • Biosynthesis and processing of intrinsic factor cobalamin receptor
    • 85. Seetharam S, Ramanujam K, Seetharam B. 1992. Biosynthesis and processing of intrinsic factor cobalamin receptor. J. Biol. Chem. 267:7421-27
    • (1992) J. Biol. Chem. , vol.267 , pp. 7421-7427
    • Seetharam, S.1    Ramanujam, K.2    Seetharam, B.3
  • 86
    • 0031913326 scopus 로고    scopus 로고
    • Expression of intrinsic factor and pepsinogen in the rat stomach identifies a subset of parietal cells
    • 86. Shao J-S, Schepp W, Alpers DH. 1998. Expression of intrinsic factor and pepsinogen in the rat stomach identifies a subset of parietal cells. Am. J. Physiol. 274:G62-70
    • (1998) Am. J. Physiol. , vol.274
    • Shao, J.-S.1    Schepp, W.2    Alpers, D.H.3
  • 88
    • 0025055330 scopus 로고
    • Monoclonal antibodies to human intrinsic factor
    • 88. Smolka A, Donaldson RM. 1990. Monoclonal antibodies to human intrinsic factor. Gastroenterology 98:607-14
    • (1990) Gastroenterology , vol.98 , pp. 607-614
    • Smolka, A.1    Donaldson, R.M.2
  • 89
    • 0026453587 scopus 로고
    • The intrinsic factor-cobalamin receptor binding site is located in the amino terminal portion of IF
    • 89. Tang LH, Chokshi H, Hu C, Gordon MM, Alpers DH. 1992. The intrinsic factor-cobalamin receptor binding site is located in the amino terminal portion of IF. J. Biol. Chem. 267:22982-86
    • (1992) J. Biol. Chem. , vol.267 , pp. 22982-22986
    • Tang, L.H.1    Chokshi, H.2    Hu, C.3    Gordon, M.M.4    Alpers, D.H.5
  • 90
    • 0025881389 scopus 로고
    • Lysosomal cobalamin accumulation in fibroblasts from a patient with an inborn error of cobalamin metabolism (Cbl F complementation group): Visualization by electronmicroscope autoradiography
    • 90. Vassiliadis A, Rosenblatt DS, Cooper BA, Bergeron JJM. 1991. Lysosomal cobalamin accumulation in fibroblasts from a patient with an inborn error of cobalamin metabolism (Cbl F complementation group): visualization by electronmicroscope autoradiography. Exp. Cell Res. 195:295-302
    • (1991) Exp. Cell Res. , vol.195 , pp. 295-302
    • Vassiliadis, A.1    Rosenblatt, D.S.2    Cooper, B.A.3    Bergeron, J.J.M.4
  • 91
    • 46549091809 scopus 로고
    • Cobalamin-binding proteins in human urine. Identification and quantitation
    • 91. Wahlstedt V, Grasbeck R. 1985. Cobalamin-binding proteins in human urine. Identification and quantitation. J. Lab. Clin. Med. 106:439-46
    • (1985) J. Lab. Clin. Med. , vol.106 , pp. 439-446
    • Wahlstedt, V.1    Grasbeck, R.2
  • 92
    • 0031566261 scopus 로고    scopus 로고
    • A receptor binding site on intrinsic factor is located between amino acids 25-44 and interacts with other parts of the protein
    • 92. Wen J, Gordon MM, Alpers DH. 1997. A receptor binding site on intrinsic factor is located between amino acids 25-44 and interacts with other parts of the protein. Biochem. Biophys. Res. Commun. 231:348-51
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 348-351
    • Wen, J.1    Gordon, M.M.2    Alpers, D.H.3
  • 93
    • 0029671134 scopus 로고    scopus 로고
    • Purification by cobalamin-sepharose affinity chromatography intrinsic factor-binding activity of an extramembrane proteolytic fragment from pig ileal mucosa
    • 93. Yerima A, Safi A, Gastin I, Michalski JC, Saunier M, Gueant JL. 1996. Purification by cobalamin-sepharose affinity chromatography intrinsic factor-binding activity of an extramembrane proteolytic fragment from pig ileal mucosa. Biochem. J. 313:675-81
    • (1996) Biochem. J. , vol.313 , pp. 675-681
    • Yerima, A.1    Safi, A.2    Gastin, I.3    Michalski, J.C.4    Saunier, M.5    Gueant, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.