메뉴 건너뛰기




Volumn 111, Issue 20, 1998, Pages 3007-3015

Polarized localizations of annexins I, II, VI and XIII in epithelial cells of intestinal, hepatic and pancreatic tissues

Author keywords

Annexin; Basolateral domain; Traffic

Indexed keywords

ANNEXIN; CALPHOBINDIN II; LIPOCORTIN 1; LIPOCORTIN 2;

EID: 0031739687     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (54)

References (45)
  • 1
    • 0024583598 scopus 로고
    • Enhancement of calcium sensitivity of lipocortin 1 in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography
    • Ando, Y., Imamura, S., Hong, Y. M., Owada, M. K., Kakunaga, T. and Kannagi, R. (1989). Enhancement of calcium sensitivity of lipocortin 1 in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography. J. Biol. Chem. 264, 6948-6955.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6948-6955
    • Ando, Y.1    Imamura, S.2    Hong, Y.M.3    Owada, M.K.4    Kakunaga, T.5    Kannagi, R.6
  • 2
    • 0029990362 scopus 로고    scopus 로고
    • Reconstitution of transcytosis in SLO-permeabilized MDCK cells: Existence of an NSF-dependent fusion mechanism with the apical surface of MDCK cells
    • Apodaca, G., Cardone, M. H., Whiteheart, S. W., DasGupta, B. R. and Mostov, K. E. (1996). Reconstitution of transcytosis in SLO-permeabilized MDCK cells: existence of an NSF-dependent fusion mechanism with the apical surface of MDCK cells. EMBO J. 15, 1471-1481.
    • (1996) EMBO J. , vol.15 , pp. 1471-1481
    • Apodaca, G.1    Cardone, M.H.2    Whiteheart, S.W.3    DasGupta, B.R.4    Mostov, K.E.5
  • 3
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., Katz, L. A. and Mostov, K. E. (1994). Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125, 67-86.
    • (1994) J. Cell Biol. , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 4
    • 0023608934 scopus 로고
    • Biogenesis of the rat hepatocyte plasma membrane in vivo: Comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation
    • Bartles, J. R., Feracci, H. M., Stieger, B. and Hubbard, A. L. (1987). Biogenesis of the rat hepatocyte plasma membrane in vivo: comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation. J. Cell. Biol. 105, 1241-1251.
    • (1987) J. Cell. Biol. , vol.105 , pp. 1241-1251
    • Bartles, J.R.1    Feracci, H.M.2    Stieger, B.3    Hubbard, A.L.4
  • 5
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. (1981). Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256, 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 6
    • 0016358918 scopus 로고
    • Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. I. Columnar cells
    • Cheng, H. and Leblond, C. P. (1974a). Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. I. Columnar cells. Am. J. Anat. 141, 461-480.
    • (1974) Am. J. Anat. , vol.141 , pp. 461-480
    • Cheng, H.1    Leblond, C.P.2
  • 7
    • 0016327360 scopus 로고
    • Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. II. Mucous cells
    • Cheng, H. and Leblond, C. P. (1974b). Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. II. Mucous cells. Am. J. Anat. 141, 481-502.
    • (1974) Am. J. Anat. , vol.141 , pp. 481-502
    • Cheng, H.1    Leblond, C.P.2
  • 8
    • 0026048811 scopus 로고
    • Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: Evidence for developmental regulation in B- and T-lymphocytes
    • Clark, D. M. Moss, S. E., Wright, N. A. and Crumpton, M. J. (1991). Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: evidence for developmental regulation in B- and T-lymphocytes. Histochem. 96, 405-412.
    • (1991) Histochem. , vol.96 , pp. 405-412
    • Clark, D.M.1    Moss, S.E.2    Wright, N.A.3    Crumpton, M.J.4
  • 9
    • 0030853566 scopus 로고    scopus 로고
    • Annexins in the secretory pathway
    • Donnelly, S. R. and Moss, S. E. (1997). Annexins in the secretory pathway. Cell. Mol. Life Sci. 53, 539-545.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 539-545
    • Donnelly, S.R.1    Moss, S.E.2
  • 11
    • 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, J. P. and Maroux, S. (1982). Localization by immunofluorescence and histochemical labeling of aminopeptidase N in relation to its biosynthesis in rabbit and pig enterocytes. Gastroenterology 82, 317-324.
    • (1982) Gastroenterology , vol.82 , pp. 317-324
    • Feracci, H.1    Bernadac, A.2    Gorvel, J.P.3    Maroux, S.4
  • 12
    • 0028921025 scopus 로고
    • Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane
    • Fiedler, K., Lafont, F., Parton, R. G. and Simons, K. (1995). Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J. Cell Biol. 128, 1043-1053.
    • (1995) J. Cell Biol. , vol.128 , pp. 1043-1053
    • Fiedler, K.1    Lafont, F.2    Parton, R.G.3    Simons, K.4
  • 14
    • 0028241854 scopus 로고
    • Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion
    • Gaisano, H. Y., Sheu, L., Foskett, J. K. and Trimble, W. S. (1994). Tetanus toxin light chain cleaves a vesicle-associated membrane protein (VAMP) isoform 2 in rat pancreatic zymogen granules and inhibits enzyme secretion. J. Biol. Chem. 269, 17062-17066.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17062-17066
    • Gaisano, H.Y.1    Sheu, L.2    Foskett, J.K.3    Trimble, W.S.4
  • 15
    • 0030998465 scopus 로고    scopus 로고
    • Annexins and membrane dynamics
    • Gerke, V. and Moss, S. E. (1997). Annexins and membrane dynamics. Biochim. Biophys. Acta 1357, 129-154.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 129-154
    • Gerke, V.1    Moss, S.E.2
  • 16
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V. and Weber, K. (1984). Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3, 227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 17
    • 0024312336 scopus 로고
    • Conformational change of rabbit aminopeptidase N into enterocyte plasma membrane domains analysed by flow cytometry fluorescence energy transfer
    • Gorvel, J. P., Mishal, Z., Liegey, F., Rigal, A. and Maroux, S. (1989) Conformational change of rabbit aminopeptidase N into enterocyte plasma membrane domains analysed by flow cytometry fluorescence energy transfer. J. Cell Biol. 108, 2193-2200.
    • (1989) J. Cell Biol. , vol.108 , pp. 2193-2200
    • Gorvel, J.P.1    Mishal, Z.2    Liegey, F.3    Rigal, A.4    Maroux, S.5
  • 18
    • 0021995554 scopus 로고
    • Aminopeptidase N and human blood group A-antigenicity along the digestive tract and associated glands in rabbit
    • Gorvel, J. P., Rigal, A., Sarles, J. and Maroux, S. (1985). Aminopeptidase N and human blood group A-antigenicity along the digestive tract and associated glands in rabbit. Cell Tissue Res. 239, 241-248.
    • (1985) Cell Tissue Res. , vol.239 , pp. 241-248
    • Gorvel, J.P.1    Rigal, A.2    Sarles, J.3    Maroux, S.4
  • 19
    • 0021733218 scopus 로고
    • Cellular localization of class I (HLA-A, B, C) and class II (HLA-DR and DQ) MHC antigens on the epithelial cells of normal human jejunum
    • Gorvel, J. P., Sarles, J., Maroux, S., Olive, D. and Mawas, C. (1984). Cellular localization of class I (HLA-A, B, C) and class II (HLA-DR and DQ) MHC antigens on the epithelial cells of normal human jejunum. Biol. Cell 52, 249-252.
    • (1984) Biol. Cell , vol.52 , pp. 249-252
    • Gorvel, J.P.1    Sarles, J.2    Maroux, S.3    Olive, D.4    Mawas, C.5
  • 20
    • 0021362113 scopus 로고
    • The 46,000-dalton tyrosine protrein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues
    • Gould, K. L., Cooper, J. A. and Hunter, T. (1984). The 46,000-dalton tyrosine protrein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues. J. Cell Biol. 98, 487-497.
    • (1984) J. Cell Biol. , vol.98 , pp. 487-497
    • Gould, K.L.1    Cooper, J.A.2    Hunter, T.3
  • 21
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • Harder, T., Kellner, R., Parton, R. G. and Gruenberg, J. (1997). Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol. Biol. Cell 8, 533-545.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 22
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rub proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., Tagaya, M., Ullrich, O., Montecucco, C. and Simons, K. (1995). Different requirements for NSF, SNAP, and Rub proteins in apical and basolateral transport in MDCK cells. Cell 81, 571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 25
    • 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, J. P., Rigal, A., Soulié J. M. and Maroux S. (1987). Evidence for the transit of aminopeptidase N through the basolateral membrane before it reaches the brush border of enterocytes. J. Membrane Biol. 96, 19-25.
    • (1987) J. Membrane Biol. , vol.96 , pp. 19-25
    • Massey, D.1    Feracci, H.2    Gorvel, J.P.3    Rigal, A.4    Soulié, J.M.5    Maroux, S.6
  • 26
    • 0025759023 scopus 로고
    • Lipocortin IV is a basolateral cytoskeleton constituent of rabbit enterocytes
    • Massey, D., Traverso, V. and Maroux, S. (1991). Lipocortin IV is a basolateral cytoskeleton constituent of rabbit enterocytes. J. Biol. Chem. 266, 3125-3130.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3125-3130
    • Massey, D.1    Traverso, V.2    Maroux, S.3
  • 27
    • 0028886299 scopus 로고
    • Changes in expression and subcellular localization of annexin IV in rabbit kidney proximal tubule cells during primary culture
    • Massey-Harroche, D., Traverso, V., Mayran, N., Francou, V., Vandewalle, A. and Maroux, S. (1995). Changes in expression and subcellular localization of annexin IV in rabbit kidney proximal tubule cells during primary culture. J. Cell Physiol. 165, 313-322.
    • (1995) J. Cell Physiol. , vol.165 , pp. 313-322
    • Massey-Harroche, D.1    Traverso, V.2    Mayran, N.3    Francou, V.4    Vandewalle, A.5    Maroux, S.6
  • 28
    • 0029898796 scopus 로고    scopus 로고
    • Cellular and subcellular localizations of annexins I, IV and VI in lung epithelia
    • Mayran, N., Traverso, V., Maroux, S. and Massey-Harroche, D. (1996). Cellular and subcellular localizations of annexins I, IV and VI in lung epithelia. Am. J. Physiol. 270, L863-L871.
    • (1996) Am. J. Physiol. , vol.270
    • Mayran, N.1    Traverso, V.2    Maroux, S.3    Massey-Harroche, D.4
  • 29
    • 0022643537 scopus 로고
    • Subcellular fractionation and subcellular localization of aminopeptidase N in the rabbit enterocytes
    • Moktari, S., Feracci, H., Gorvel, J. P., Mishal, Z., Rigal, A., and Maroux, S. (1986). Subcellular fractionation and subcellular localization of aminopeptidase N in the rabbit enterocytes. J. Membrane Biol. 89, 53-63.
    • (1986) J. Membrane Biol. , vol.89 , pp. 53-63
    • Moktari, S.1    Feracci, H.2    Gorvel, J.P.3    Mishal, Z.4    Rigal, A.5    Maroux, S.6
  • 32
    • 0031931006 scopus 로고    scopus 로고
    • Annexin VI defines an apical endocytic compartment in rat liver hepatocytes
    • Ortega, D., Pol A., Biermer, M, Jäckle, S. and Enrich, C. (1998). Annexin VI defines an apical endocytic compartment in rat liver hepatocytes. J. Cell Sci. 111, 261-269.
    • (1998) J. Cell Sci. , vol.111 , pp. 261-269
    • Ortega, D.1    Pol, A.2    Biermer, M.3    Jäckle, S.4    Enrich, C.5
  • 34
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal, P. and Pollard, H. B. (1994). Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta 1197, 63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 35
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo, M., Sudol, M., Tang, Z. and Lisanti, MP. (1993). Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Sci. 122, 789-807.
    • (1993) J. Cell Sci. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 40
    • 0000840999 scopus 로고
    • Simultaneous observations of immunolabeled frozen section in LM and EM
    • Tokuyasu, K. T., Slot, J. W. and Singer, S. J. (1978). Simultaneous observations of immunolabeled frozen section in LM and EM. Ninth Int. Congr. Electron Microsc. 2, 164-165.
    • (1978) Ninth Int. Congr. Electron Microsc. , vol.2 , pp. 164-165
    • Tokuyasu, K.T.1    Slot, J.W.2    Singer, S.J.3
  • 41
    • 0028008991 scopus 로고
    • The effects of PMA and TFP and alterations in intracellular pH and calcium concentration on the membrane associations of phospholipid-binding proteins fodrin, protein kinase C and annexin II in cultured MDCK cells
    • Vääräniemi, J., Huotari, V., Lehto, V. P. and Eskelinen, S. (1994). The effects of PMA and TFP and alterations in intracellular pH and calcium concentration on the membrane associations of phospholipid-binding proteins fodrin, protein kinase C and annexin II in cultured MDCK cells. Biochim. Biophys. Acta 1189, 21-30.
    • (1994) Biochim. Biophys. Acta , vol.1189 , pp. 21-30
    • Vääräniemi, J.1    Huotari, V.2    Lehto, V.P.3    Eskelinen, S.4
  • 43
    • 0029153608 scopus 로고
    • Annexin I is overexpressed and specifically secreted during experimentally induced colitis in rats
    • Vergnolle, N., Coméra, C. and Buéno, L. (1995). Annexin I is overexpressed and specifically secreted during experimentally induced colitis in rats. Eur. J. Biochem. 232, 603-610.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 603-610
    • Vergnolle, N.1    Coméra, C.2    Buéno, L.3
  • 44
    • 0026575153 scopus 로고
    • A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: Characterization of a novel gut-specific N-myristoylated annexin
    • Wice, B. M. and Gordon, J. I. (1992). A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. J. Cell Biol. 116, 405-422.
    • (1992) J. Cell Biol. , vol.116 , pp. 405-422
    • Wice, B.M.1    Gordon, J.I.2
  • 45
    • 0028019458 scopus 로고
    • Fluorescent choleretic and cholestatic bile salts take different paths across the hepatocyte: Transcytosis of glycolithocholate leads to an extensive redistribution of annexin II
    • Wilton, J. C., Matthews, G. M., Burgoyne, R. D., Mills, C. O., Chipman, J. K. and Coleman, R. (1994). Fluorescent choleretic and cholestatic bile salts take different paths across the hepatocyte: transcytosis of glycolithocholate leads to an extensive redistribution of annexin II. J. Cell Biol. 127, 401-410.
    • (1994) J. Cell Biol. , vol.127 , pp. 401-410
    • Wilton, J.C.1    Matthews, G.M.2    Burgoyne, R.D.3    Mills, C.O.4    Chipman, J.K.5    Coleman, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.