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Volumn 198, Issue 3, 2004, Pages 441-451

Enterocytin: A New Specific Enterocyte Marker Bearing a B30.2-Like Domain

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; CELL MARKER; CELL PROTEIN; ENTEROCYTIN; ENTEROCYTIN, RABBIT; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; PROTEIN; UNCLASSIFIED DRUG;

EID: 1242339715     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.10418     Document Type: Article
Times cited : (5)

References (54)
  • 1
    • 0036721401 scopus 로고    scopus 로고
    • The epithelial cell cytoskeleton and intracellular trafficking. III. How is villin involved in the actin cytoskeleton dynamics in intestinal cells?
    • Athman R, Louvard D, Robine S. 2002. The epithelial cell cytoskeleton and intracellular trafficking. III. How is villin involved in the actin cytoskeleton dynamics in intestinal cells? Am J Physiol Gastrointest Liver Physiol 283(3):G496-G502.
    • (2002) Am J Physiol Gastrointest Liver Physiol , vol.283 , Issue.3
    • Athman, R.1    Louvard, D.2    Robine, S.3
  • 2
    • 0036716876 scopus 로고    scopus 로고
    • Homeobox genes in gut development
    • Beck F. 2002. Homeobox genes in gut development. Gut 51(3):450-454.
    • (2002) Gut , vol.51 , Issue.3 , pp. 450-454
    • Beck, F.1
  • 3
    • 0034080251 scopus 로고    scopus 로고
    • Gut instincts: Thoughts on intestinal epithelial stem cells
    • Booth C, Potten CS. 2000. Gut instincts: Thoughts on intestinal epithelial stem cells. J Clin Invest 105(11):1493-1499.
    • (2000) J Clin Invest , vol.105 , Issue.11 , pp. 1493-1499
    • Booth, C.1    Potten, C.S.2
  • 4
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg JP, Ooi J, Levy E, Margolis B. 1996. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol Cell Biol 16(11): 6229-6241.
    • (1996) Mol Cell Biol , vol.16 , Issue.11 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 5
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard P, Stetefeld J, Strelkov SV. 2001. Coiled coils: A highly versatile protein folding motif. Trends Cell Biol 11(2):82-88.
    • (2001) Trends Cell Biol , vol.11 , Issue.2 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 6
    • 0025308617 scopus 로고
    • Migration of fetal intestinal intervillous cells in neonatal mice
    • Calvert R, Pothier P. 1990. Migration of fetal intestinal intervillous cells in neonatal mice. Anat Rec 227(2):199-206.
    • (1990) Anat Rec , vol.227 , Issue.2 , pp. 199-206
    • Calvert, R.1    Pothier, P.2
  • 7
    • 0023925328 scopus 로고
    • Epithelial polarity, villin expression, and enterocytic differentiation of cultured human colon carcinoma cells: A survey of twenty cell lines
    • Chantret I, Barbat A, Dussaulx E, Brattain MG, Zweibaum A. 1988. Epithelial polarity, villin expression, and enterocytic differentiation of cultured human colon carcinoma cells: A survey of twenty cell lines. Cancer Res 48(7):1936-1942.
    • (1988) Cancer Res , vol.48 , Issue.7 , pp. 1936-1942
    • Chantret, I.1    Barbat, A.2    Dussaulx, E.3    Brattain, M.G.4    Zweibaum, A.5
  • 9
    • 0019784949 scopus 로고
    • Microvillus membrane vesicles from pig small intestine. Purity and lipid composition
    • Christiansen K, Carlsen J. 1981. Microvillus membrane vesicles from pig small intestine. Purity and lipid composition. Biochim Biophys Acta 647(2):188-195.
    • (1981) Biochim Biophys Acta , vol.647 , Issue.2 , pp. 188-195
    • Christiansen, K.1    Carlsen, J.2
  • 10
    • 0035119361 scopus 로고    scopus 로고
    • Stem cells and the regulation of proliferation, differentiation, and patterning in the intestinal epithelium: Emerging insights from gene expression patterns, transgenic, and gene ablation studies
    • Clatworthy JP, Subramanian V. 2001. Stem cells and the regulation of proliferation, differentiation, and patterning in the intestinal epithelium: Emerging insights from gene expression patterns, transgenic, and gene ablation studies. Mech Dev 101(1-2):3-9.
    • (2001) Mech Dev , vol.101 , Issue.1-2 , pp. 3-9
    • Clatworthy, J.P.1    Subramanian, V.2
  • 12
    • 0034641894 scopus 로고    scopus 로고
    • New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome
    • Cox TC, Allen LR, Cox LL, Hopwood B, Goodwin B, Haan E, Suthers GK. 2000. New mutations in MID1 provide support for loss of function as the cause of X-linked Opitz syndrome. Hum Mol Genet 9(17):2553-2562.
    • (2000) Hum Mol Genet , vol.9 , Issue.17 , pp. 2553-2562
    • Cox, T.C.1    Allen, L.R.2    Cox, L.L.3    Hopwood, B.4    Goodwin, B.5    Haan, E.6    Suthers, G.K.7
  • 13
    • 0035479996 scopus 로고    scopus 로고
    • Genetically determined recurrent fevers
    • Delpech M, Grateau G. 2001. Genetically determined recurrent fevers. Curr Opin Immunol 13(5):539-542.
    • (2001) Curr Opin Immunol , vol.13 , Issue.5 , pp. 539-542
    • Delpech, M.1    Grateau, G.2
  • 14
    • 0034254089 scopus 로고    scopus 로고
    • What are oligomerization domains good for?
    • Engel J, Kammerer RA. 2000. What are oligomerization domains good for? Matrix Biol 19(4):283-288.
    • (2000) Matrix Biol , vol.19 , Issue.4 , pp. 283-288
    • Engel, J.1    Kammerer, R.A.2
  • 15
    • 0020070074 scopus 로고
    • Localization by immunofluorescence and histochemical labeling of aminopeptidase N in relation to its biosynthesis in rabbit and pig enterocytes
    • Feracci H, Bernadac A, Gorvel JP, Maroux S. 1982. Localization by immunofluorescence and histochemical labeling of aminopeptidase N in relation to its biosynthesis in rabbit and pig enterocytes. Gastroenterology 82(2):317-324.
    • (1982) Gastroenterology , vol.82 , Issue.2 , pp. 317-324
    • Feracci, H.1    Bernadac, A.2    Gorvel, J.P.3    Maroux, S.4
  • 16
    • 0021956858 scopus 로고
    • Biosynthesis and intracellular pool of aminopeptidase N in rabbit enterocytes
    • Feracci H, Rigal A, Maroux S. 1985. Biosynthesis and intracellular pool of aminopeptidase N in rabbit enterocytes. J Membr Biol 83(1-2):139-146.
    • (1985) J Membr Biol , vol.83 , Issue.1-2 , pp. 139-146
    • Feracci, H.1    Rigal, A.2    Maroux, S.3
  • 18
    • 0025492527 scopus 로고
    • From the structure to the function of villin, an actin-binding protein of the brush border
    • Friederich E, Pringault E, Arpin M, Louvard D. 1990. From the structure to the function of villin, an actin-binding protein of the brush border. Bioessays 12(9):403-408.
    • (1990) Bioessays , vol.12 , Issue.9 , pp. 403-408
    • Friederich, E.1    Pringault, E.2    Arpin, M.3    Louvard, D.4
  • 19
    • 0024831621 scopus 로고
    • Brush border membrane sucrase-isomaltase, maltase-glucoamylase, and trehalase in mammals. Comparative development, effects of glucocorticoids, molecular mechanisms, and phylogenetic implications
    • Galand G. 1989. Brush border membrane sucrase-isomaltase, maltase-glucoamylase, and trehalase in mammals. Comparative development, effects of glucocorticoids, molecular mechanisms, and phylogenetic implications. Comp Biochem Physiol B 94(1):1-11.
    • (1989) Comp Biochem Physiol B , vol.94 , Issue.1 , pp. 1-11
    • Galand, G.1
  • 21
    • 0022463735 scopus 로고
    • Identification of an early expressed marker of the luminal membrane of rabbit small intestinal columnar cells. Presence of a homologous antigen in kidney proximal tubules and glomeruli
    • Gorvel JP, Rigal A, Olive D, Mawas C, Maroux S. 1986. Identification of an early expressed marker of the luminal membrane of rabbit small intestinal columnar cells. Presence of a homologous antigen in kidney proximal tubules and glomeruli. Biol Cell 56(2):121-126.
    • (1986) Biol Cell , vol.56 , Issue.2 , pp. 121-126
    • Gorvel, J.P.1    Rigal, A.2    Olive, D.3    Mawas, C.4    Maroux, S.5
  • 22
    • 0023731660 scopus 로고
    • Characterization of intestinal membrane vesicles with flow cytometry
    • Gorvel JP, Mishal Z, Maroux S. 1988. Characterization of intestinal membrane vesicles with flow cytometry. Prog Clin Biol Res 270:195-209.
    • (1988) Prog Clin Biol Res , vol.270 , pp. 195-209
    • Gorvel, J.P.1    Mishal, Z.2    Maroux, S.3
  • 23
    • 0019853256 scopus 로고
    • Passage of viral membrane proteins through the Golgi complex
    • Green J, Griffiths G, Louvard D, Quinn P, Warren G. 1981. Passage of viral membrane proteins through the Golgi complex. J Mol Biol 152(4):663-698.
    • (1981) J Mol Biol , vol.152 , Issue.4 , pp. 663-698
    • Green, J.1    Griffiths, G.2    Louvard, D.3    Quinn, P.4    Warren, G.5
  • 25
    • 0031773260 scopus 로고    scopus 로고
    • B30.2-like domain proteins: Update and new insights into a rapidly expanding family of proteins
    • Henry J, Mather IH, McDermott MF, Pontarotti P. 1998. B30.2-like domain proteins: Update and new insights into a rapidly expanding family of proteins. Mol Biol Evol 15(12):1696-1705.
    • (1998) Mol Biol Evol , vol.15 , Issue.12 , pp. 1696-1705
    • Henry, J.1    Mather, I.H.2    McDermott, M.F.3    Pontarotti, P.4
  • 26
    • 0043253165 scopus 로고    scopus 로고
    • The mammalian fatty acid-binding protein multigene family: Molecular and genetic insights into function
    • Hertzel AV, Bernlohr DA. 2000. The mammalian fatty acid-binding protein multigene family: Molecular and genetic insights into function. Trends Endocrinol Metab 11(5):175-180.
    • (2000) Trends Endocrinol Metab , vol.11 , Issue.5 , pp. 175-180
    • Hertzel, A.V.1    Bernlohr, D.A.2
  • 27
    • 0028973205 scopus 로고
    • Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically associates with a 150-kDa protein of mammary epithelial cells and milk fat globule membrane
    • Ishii T, Aoki N, Noda A, Adachi T, Nakamura R, Matsuda T. 1995. Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically associates with a 150-kDa protein of mammary epithelial cells and milk fat globule membrane. Biochim Biophys Acta 1245(3):285-292.
    • (1995) Biochim Biophys Acta , vol.1245 , Issue.3 , pp. 285-292
    • Ishii, T.1    Aoki, N.2    Noda, A.3    Adachi, T.4    Nakamura, R.5    Matsuda, T.6
  • 28
    • 0016287588 scopus 로고
    • Lipid components of two different regions of an intestinal epithelial cell membrane of mouse
    • Kawai K, Fujita M, Nakao M. 1974. Lipid components of two different regions of an intestinal epithelial cell membrane of mouse. Biochim Biophys Acta 369(2):222-233.
    • (1974) Biochim Biophys Acta , vol.369 , Issue.2 , pp. 222-233
    • Kawai, K.1    Fujita, M.2    Nakao, M.3
  • 29
    • 0020007911 scopus 로고
    • Topology of microvillar membrance hydrolases of kidney and intestine
    • Kenny AJ, Maroux S. 1982. Topology of microvillar membrance hydrolases of kidney and intestine. Physiol Rev 62(1):91-128.
    • (1982) Physiol Rev , vol.62 , Issue.1 , pp. 91-128
    • Kenny, A.J.1    Maroux, S.2
  • 30
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M. 2001. MEGA2: Molecular evolutionary genetics analysis software. Bioinformatics 17(12): 1244-1245.
    • (2001) Bioinformatics , vol.17 , Issue.12 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(259):680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. 1996. Coiled coils: New structures and new functions. Trends Biochem Sci 21(10):375-382.
    • (1996) Trends Biochem Sci , vol.21 , Issue.10 , pp. 375-382
    • Lupas, A.1
  • 33
    • 0036007425 scopus 로고    scopus 로고
    • The intestinal epithelial stem cell
    • Marshman E, Booth C, Potten CS. 2002. The intestinal epithelial stem cell. Bioessays 24(1):91-98.
    • (2002) Bioessays , vol.24 , Issue.1 , pp. 91-98
    • Marshman, E.1    Booth, C.2    Potten, C.S.3
  • 34
    • 0023234238 scopus 로고
    • Evidence for the transit of aminopeptidase N through the basolateral membrane before it reaches the brush border of enterocytes
    • Massey D, Feracci H, Gorvel JP, Rigal A, Soulie JM, Maroux S. 1987. Evidence for the transit of aminopeptidase N through the basolateral membrane before it reaches the brush border of enterocytes. J Membr Biol 96(1):19-25.
    • (1987) J Membr Biol , vol.96 , Issue.1 , pp. 19-25
    • Massey, D.1    Feracci, H.2    Gorvel, J.P.3    Rigal, A.4    Soulie, J.M.5    Maroux, S.6
  • 35
    • 0025759023 scopus 로고
    • Lipocortin IV is a basolateral cytoskeleton constituent of rabbit enterocytes
    • Massey D, Traverso V, Maroux S. 1991. Lipocortin IV is a basolateral cytoskeleton constituent of rabbit enterocytes. J Biol Chem 266(5): 3125-3130.
    • (1991) J Biol Chem , vol.266 , Issue.5 , pp. 3125-3130
    • Massey, D.1    Traverso, V.2    Maroux, S.3
  • 36
    • 0036902177 scopus 로고    scopus 로고
    • Functional regulation of xanthine oxidoreductase expression and localization in the mouse mammary gland: Evidence of a role in lipid secretion
    • McManaman JL, Palmer CA, Wright RM, Neville MC. 2002. Functional regulation of xanthine oxidoreductase expression and localization in the mouse mammary gland: Evidence of a role in lipid secretion. J Physiol 545(Pt 2):567-579.
    • (2002) J Physiol , vol.545 , Issue.PART 2 , pp. 567-579
    • McManaman, J.L.1    Palmer, C.A.2    Wright, R.M.3    Neville, M.C.4
  • 37
    • 0022643537 scopus 로고
    • Subcellular fractionation and subcellular localization of aminopeptidase N in the rabbit enterocytes
    • Moktari S, Feracci H, Gorvel JP, Mishal Z, Rigal A, Maroux S. 1986. Subcellular fractionation and subcellular localization of aminopeptidase N in the rabbit enterocytes. J Membr Biol 89(1):53-63.
    • (1986) J Membr Biol , vol.89 , Issue.1 , pp. 53-63
    • Moktari, S.1    Feracci, H.2    Gorvel, J.P.3    Mishal, Z.4    Rigal, A.5    Maroux, S.6
  • 38
    • 0035070246 scopus 로고    scopus 로고
    • Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase
    • Naim HY. 2001. Molecular and cellular aspects and regulation of intestinal lactase-phlorizin hydrolase. Histol Histopathol 16(2): 553-561.
    • (2001) Histol Histopathol , vol.16 , Issue.2 , pp. 553-561
    • Naim, H.Y.1
  • 39
    • 0035719198 scopus 로고    scopus 로고
    • Familial mediterranean fever - A review and update
    • Orbach H, Ben-Chetrit E. 2001. Familial mediterranean fever - A review and update. Minerva Med 92(6):421-430.
    • (2001) Minerva Med , vol.92 , Issue.6 , pp. 421-430
    • Orbach, H.1    Ben-Chetrit, E.2
  • 42
    • 0034524083 scopus 로고    scopus 로고
    • Characterization and molecular localization of anion transporters in colonic epithelial cells
    • Rajendran VM, Binder HJ. 2000. Characterization and molecular localization of anion transporters in colonic epithelial cells. Ann NY Acad Sci 915:15-29.
    • (2000) Ann NY Acad Sci , vol.915 , pp. 15-29
    • Rajendran, V.M.1    Binder, H.J.2
  • 43
    • 0036278558 scopus 로고    scopus 로고
    • The 52000 MW Ro/SS-A autoantigen in Sjogren's syndrome/systemic lupus erythematosus (Ro52) is an interferon-gamma inducible tripartite motif protein associated with membrane proximal structures
    • Rhodes DA, Ihrke G, Reinicke AT, Malcherek G, Towey M, Isenberg DA, Trowsdale J. 2002. The 52000 MW Ro/SS-A autoantigen in Sjogren's syndrome/systemic lupus erythematosus (Ro52) is an interferon-gamma inducible tripartite motif protein associated with membrane proximal structures. Immunology 106(2):246-256.
    • (2002) Immunology , vol.106 , Issue.2 , pp. 246-256
    • Rhodes, D.A.1    Ihrke, G.2    Reinicke, A.T.3    Malcherek, G.4    Towey, M.5    Isenberg, D.A.6    Trowsdale, J.7
  • 44
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. 1987. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol 4(4):406-425.
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 45
    • 0030991810 scopus 로고    scopus 로고
    • The apical submembrane cytoskeleton participates in the organization of the apical pole in epithelial cells
    • Salas PJ, Rodriguez ML, Viciana AL, Vega-Salas DE, Hauri HP. 1997. The apical submembrane cytoskeleton participates in the organization of the apical pole in epithelial cells. J Cell Biol 137(2):359-375.
    • (1997) J Cell Biol , vol.137 , Issue.2 , pp. 359-375
    • Salas, P.J.1    Rodriguez, M.L.2    Viciana, A.L.3    Vega-Salas, D.E.4    Hauri, H.P.5
  • 46
    • 0037205413 scopus 로고    scopus 로고
    • GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis
    • Skurat AV, Dietrich AD, Zhai L, Roach PJ. 2002. GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. J Biol Chem 277(22):19331-19338.
    • (2002) J Biol Chem , vol.277 , Issue.22 , pp. 19331-19338
    • Skurat, A.V.1    Dietrich, A.D.2    Zhai, L.3    Roach, P.J.4
  • 47
    • 0034717896 scopus 로고    scopus 로고
    • The fatty acid transport function of fatty acid-binding proteins
    • Storch J, Thumser AE. 2000. The fatty acid transport function of fatty acid-binding proteins. Biochim Biophys Acta 1486(1):28-44.
    • (2000) Biochim Biophys Acta , vol.1486 , Issue.1 , pp. 28-44
    • Storch, J.1    Thumser, A.E.2
  • 48
    • 0037458011 scopus 로고    scopus 로고
    • RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway
    • Suzumori N, Burns KH, Yan W, Matzuk MM. 2003. RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway. Proc Natl Acad Sci USA 100(2):550-555.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.2 , pp. 550-555
    • Suzumori, N.1    Burns, K.H.2    Yan, W.3    Matzuk, M.M.4
  • 49
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences
    • Tatusova TA, Madden TL. 1999. BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol Lett 174(2):247-250.
    • (1999) FEMS Microbiol Lett , vol.174 , Issue.2 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice. Nucleic Acids Res 22(22):4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0035083772 scopus 로고    scopus 로고
    • Two B or not two B? Overview of the rapidly expanding B-box family of proteins
    • Torok M, Etkin LD. 2001. Two B or not two B? Overview of the rapidly expanding B-box family of proteins. Differentiation 67(3): 63-71.
    • (2001) Differentiation , vol.67 , Issue.3 , pp. 63-71
    • Torok, M.1    Etkin, L.D.2
  • 53
    • 0033926472 scopus 로고    scopus 로고
    • Mass spectrometric analysis of proteins
    • Wilm M. 2000. Mass spectrometric analysis of proteins. Adv Protein Chem 54:1-30.
    • (2000) Adv Protein Chem , vol.54 , pp. 1-30
    • Wilm, M.1
  • 54
    • 0033740340 scopus 로고    scopus 로고
    • Genetic mosaic analysis based on Cre recombinase and navigated laser capture microdissection
    • Wong MH, Saam JR, Stappenbeck TS, Rexer CH, Gordon JI. 2000. Genetic mosaic analysis based on Cre recombinase and navigated laser capture microdissection. Proc Natl Acad Sci USA 97(23): 12601-12606.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.23 , pp. 12601-12606
    • Wong, M.H.1    Saam, J.R.2    Stappenbeck, T.S.3    Rexer, C.H.4    Gordon, J.I.5


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