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Volumn 141, Issue 1, 2007, Pages 47-55

Ligand-binding activity and expression profile of annexins in Caenorhabditis elegans

Author keywords

Annexin; C. elegans; Glycosaminoglycan; Lectin; Phospholipid

Indexed keywords

CALCIUM BINDING PROTEIN; CARBOHYDRATE BINDING PROTEIN; CHONDROITIN; GLYCEROPHOSPHOINOSITOL INOSITOLPHOSPHODIESTERASE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; LECTIN; LIPOCORTIN 1; LIPOCORTIN 2; LIPOCORTIN 4; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID;

EID: 34147210169     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm009     Document Type: Article
Times cited : (10)

References (46)
  • 2
    • 0037398446 scopus 로고    scopus 로고
    • Annexin 1: An endogenous anti-inflammatory protein
    • Perretti, M. and Gavins, F.N. (2003) Annexin 1: an endogenous anti-inflammatory protein. News Physiol. Sci. 18, 60-64
    • (2003) News Physiol. Sci , vol.18 , pp. 60-64
    • Perretti, M.1    Gavins, F.N.2
  • 3
    • 1942486365 scopus 로고    scopus 로고
    • Annexin 1: More than an anti-phospholipase protein
    • Parente, L. and Solito, E. (2004) Annexin 1: more than an anti-phospholipase protein. Inflamm. Res. 53, 125-132
    • (2004) Inflamm. Res , vol.53 , pp. 125-132
    • Parente, L.1    Solito, E.2
  • 4
    • 0033826136 scopus 로고    scopus 로고
    • Antiphospholipid antibody-mediated disruption of the annexin-V antithrombotic shield: A thrombogenic mechanism for the antiphospholipid syndrome
    • Rand, J.H. (2000) Antiphospholipid antibody-mediated disruption of the annexin-V antithrombotic shield: a thrombogenic mechanism for the antiphospholipid syndrome. J. Autoimmun. 15, 107-111
    • (2000) J. Autoimmun , vol.15 , pp. 107-111
    • Rand, J.H.1
  • 5
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz, C.E. (1992) The annexins and exocytosis. Science 258, 924-931
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 6
    • 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
  • 7
    • 0037315827 scopus 로고    scopus 로고
    • Aberrant inflammation and resistance to glucocorticoids in annexin 1-/- mouse
    • Hannon, R., Croxtall, J.D., Getting, S.J. et al. (2003) Aberrant inflammation and resistance to glucocorticoids in annexin 1-/- mouse. FASEB J. 17, 253-255
    • (2003) FASEB J , vol.17 , pp. 253-255
    • Hannon, R.1    Croxtall, J.D.2    Getting, S.J.3
  • 8
    • 1542466792 scopus 로고    scopus 로고
    • Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo
    • Ling, Q., Jacovina, A.T., Deora, A. et al. (2004) Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo. J. Clin. Invest. 113, 38-48
    • (2004) J. Clin. Invest , vol.113 , pp. 38-48
    • Ling, Q.1    Jacovina, A.T.2    Deora, A.3
  • 9
    • 0033598680 scopus 로고    scopus 로고
    • Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse
    • Srivastava, M., Atwater, I., Glasman, M. et al. (1999) Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse. Proc. Natl. Acad. Sci. USA 96, 13783-13788
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13783-13788
    • Srivastava, M.1    Atwater, I.2    Glasman, M.3
  • 10
    • 0034967999 scopus 로고    scopus 로고
    • Loss of annexin A7 leads to alterations in frequency-induced shortening of isolated murine cardiomyocytes
    • Herr, C., Smyth, N., Ullrich, S. et al. (2001) Loss of annexin A7 leads to alterations in frequency-induced shortening of isolated murine cardiomyocytes. Mol. Cell Biol. 21, 4119-1128
    • (2001) Mol. Cell Biol , vol.21 , pp. 4119-1128
    • Herr, C.1    Smyth, N.2    Ullrich, S.3
  • 11
    • 0026539294 scopus 로고
    • Affinity purification and affinity characterization of carbohydrate-binding proteins in bovine kidney
    • Kojima, K., Ogawa, H.K., Seno, N. et al. (1992) Affinity purification and affinity characterization of carbohydrate-binding proteins in bovine kidney. J. Chromatogr. 597, 323-330
    • (1992) J. Chromatogr , vol.597 , pp. 323-330
    • Kojima, K.1    Ogawa, H.K.2    Seno, N.3
  • 12
    • 0026705785 scopus 로고
    • Carbohydrate-binding proteins in bovine kidney have consensus amino acid sequences of annexin family proteins
    • Kojima, K., Ogawa, H.K., Seno, N. et al. (1992) Carbohydrate-binding proteins in bovine kidney have consensus amino acid sequences of annexin family proteins. J. Biol. Chem. 267, 20536-20539
    • (1992) J. Biol. Chem , vol.267 , pp. 20536-20539
    • Kojima, K.1    Ogawa, H.K.2    Seno, N.3
  • 13
    • 0037033081 scopus 로고    scopus 로고
    • A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes
    • Tsujii-Hayashi, Y., Kitahara, M., Yamagaki, T. et al. (2002) A potential endogenous ligand of annexin IV in the exocrine pancreas. Carbohydrate structure of GP-2, a glycosylphosphatidylinositol-anchored glycoprotein of zymogen granule membranes. J. Biol. Chem. 277, 47493-47499
    • (2002) J. Biol. Chem , vol.277 , pp. 47493-47499
    • Tsujii-Hayashi, Y.1    Kitahara, M.2    Yamagaki, T.3
  • 14
    • 0032540321 scopus 로고    scopus 로고
    • Glycosaminoglycan binding properties of annexin IV, V, and VI
    • Ishitsuka, R., Kojima, K., Utsumi, H. et al. (1998) Glycosaminoglycan binding properties of annexin IV, V, and VI. J. Biol. Chem. 273, 9935-9941
    • (1998) J. Biol. Chem , vol.273 , pp. 9935-9941
    • Ishitsuka, R.1    Kojima, K.2    Utsumi, H.3
  • 15
    • 3042800376 scopus 로고    scopus 로고
    • Human annexin V binds to sulfatide: Contribution to regulation of blood coagulation
    • Ida, M., Satoh, A., Matsumoto, I. et al. (2004) Human annexin V binds to sulfatide: contribution to regulation of blood coagulation. J. Biochem. (Tokyo) 135, 583-588
    • (2004) J. Biochem. (Tokyo) , vol.135 , pp. 583-588
    • Ida, M.1    Satoh, A.2    Matsumoto, I.3
  • 16
    • 0037101954 scopus 로고    scopus 로고
    • Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains
    • Takagi, H., Asano, Y., Yamakawa, N. et al. (2002) Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains. J. Cell Sci. 115, 3309-3318
    • (2002) J. Cell Sci , vol.115 , pp. 3309-3318
    • Takagi, H.1    Asano, Y.2    Yamakawa, N.3
  • 17
    • 0035313549 scopus 로고    scopus 로고
    • Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells
    • Srikrishna, G., Panneerselvam, K., Westphal, V. et al. (2001) Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells. J. Immunol. 166, 4678-4688
    • (2001) J. Immunol , vol.166 , pp. 4678-4688
    • Srikrishna, G.1    Panneerselvam, K.2    Westphal, V.3
  • 18
    • 0035148547 scopus 로고    scopus 로고
    • Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces
    • Capila, I., Hernaiz, M.J., Mo, Y.D. et al. (2001) Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces. Structure 10, 57-64
    • (2001) Structure , vol.10 , pp. 57-64
    • Capila, I.1    Hernaiz, M.J.2    Mo, Y.D.3
  • 19
    • 0033662251 scopus 로고    scopus 로고
    • A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine
    • Gao-Uozumi, C.X., Uozumi, N., Miyoshi, E. et al. (2000) A novel carbohydrate binding activity of annexin V toward a bisecting N-acetylglucosamine. Glycobiology 10, 1209-1216
    • (2000) Glycobiology , vol.10 , pp. 1209-1216
    • Gao-Uozumi, C.X.1    Uozumi, N.2    Miyoshi, E.3
  • 20
    • 27944437501 scopus 로고    scopus 로고
    • Bisecting GlcNAc mediates the binding of annexin V to Hsp47
    • Gao, C.X., Miyoshi, E., Uozumi, N. et al. (2005) Bisecting GlcNAc mediates the binding of annexin V to Hsp47. Glycobiology 15, 1067-1075
    • (2005) Glycobiology , vol.15 , pp. 1067-1075
    • Gao, C.X.1    Miyoshi, E.2    Uozumi, N.3
  • 21
    • 0032835201 scopus 로고    scopus 로고
    • Yamada, S.Van Die, I. et al. (1999) Demonstration of glycosaminoglycans in Caenorhabditis elegans. FEBS Lett. 459, 327-331
    • Yamada, S.Van Die, I. et al. (1999) Demonstration of glycosaminoglycans in Caenorhabditis elegans. FEBS Lett. 459, 327-331
  • 22
    • 0034723308 scopus 로고    scopus 로고
    • Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo
    • Toyoda, H., Kinoshita-Toyoda, A., and Selleck, S.B. (2000) Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo. J. Biol. Chem. 275, 2269-2275
    • (2000) J. Biol. Chem , vol.275 , pp. 2269-2275
    • Toyoda, H.1    Kinoshita-Toyoda, A.2    Selleck, S.B.3
  • 23
    • 0035396643 scopus 로고    scopus 로고
    • The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: Identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides
    • Guerardel, Y., Balanzino, L., Maes, E. et al. (2001) The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides. Biochem. J. 357, 167-182
    • (2001) Biochem. J , vol.357 , pp. 167-182
    • Guerardel, Y.1    Balanzino, L.2    Maes, E.3
  • 24
    • 0034838433 scopus 로고    scopus 로고
    • Genetic model organisms in the study of N-glycans
    • Altmann, F., Fabini, G., Ahorn, H. et al. (2001) Genetic model organisms in the study of N-glycans. Biochimie. 83, 703-712
    • (2001) Biochimie , vol.83 , pp. 703-712
    • Altmann, F.1    Fabini, G.2    Ahorn, H.3
  • 25
    • 0036293332 scopus 로고    scopus 로고
    • Structural analysis of N-linked glycans in Caenorhabditis elegans
    • Natsuka, S., Adachi, J., Kawaguchi, M. et al. (2002) Structural analysis of N-linked glycans in Caenorhabditis elegans. J. Biochem. (Tokyo) 131, 807-813
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 807-813
    • Natsuka, S.1    Adachi, J.2    Kawaguchi, M.3
  • 26
    • 0348209615 scopus 로고    scopus 로고
    • The fine structure of Caenorhabditis elegans N-glycans
    • Cipollo, J.F., Costello, C.E., and Hirschberg, C.B. (2002) The fine structure of Caenorhabditis elegans N-glycans. J. Biol. Chem. 277, 49143-49157
    • (2002) J. Biol. Chem , vol.277 , pp. 49143-49157
    • Cipollo, J.F.1    Costello, C.E.2    Hirschberg, C.B.3
  • 27
    • 0038823611 scopus 로고    scopus 로고
    • Caenorhabditis elegans early embryogenesis and vulval morphogenesis require chondroitin biosynthesis
    • Hwang, H.Y., Olson, S.K., Esko, J.D. et al. (2003) Caenorhabditis elegans early embryogenesis and vulval morphogenesis require chondroitin biosynthesis. Nature 423, 439-443
    • (2003) Nature , vol.423 , pp. 439-443
    • Hwang, H.Y.1    Olson, S.K.2    Esko, J.D.3
  • 28
    • 0038485622 scopus 로고    scopus 로고
    • Chondroitin proteoglycans are involved in cell division of Caenorhabditis elegans
    • Mizuguchi, S., Uyama, T., Kitagawa, H. et al. (2003) Chondroitin proteoglycans are involved in cell division of Caenorhabditis elegans. Nature 423, 443-448
    • (2003) Nature , vol.423 , pp. 443-448
    • Mizuguchi, S.1    Uyama, T.2    Kitagawa, H.3
  • 29
    • 2642542826 scopus 로고    scopus 로고
    • Differential sulfations and epimerization define heparan sulfate specificity in nervous system development
    • Bulow, H.E. and Hobert, O. (2004) Differential sulfations and epimerization define heparan sulfate specificity in nervous system development. Neuron 41, 723-736
    • (2004) Neuron , vol.41 , pp. 723-736
    • Bulow, H.E.1    Hobert, O.2
  • 30
    • 13444294245 scopus 로고    scopus 로고
    • Heparan 2-O-sulfotransferase, hst-2, is essential for normal cell migration in Caenorhabditis elegans
    • Kinnunen, T., Huang, Z., Townsend, J. et al. (2005) Heparan 2-O-sulfotransferase, hst-2, is essential for normal cell migration in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 102, 1507-1512
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1507-1512
    • Kinnunen, T.1    Huang, Z.2    Townsend, J.3
  • 31
    • 0032775815 scopus 로고    scopus 로고
    • Transcription, biochemistry and localization of nematode annexins
    • Daigle, S.N. and Creutz, C.E. (1999) Transcription, biochemistry and localization of nematode annexins. J. Cell Sci. 112, 1901-1913
    • (1999) J. Cell Sci , vol.112 , pp. 1901-1913
    • Daigle, S.N.1    Creutz, C.E.2
  • 32
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974) The genetics of Caenorhabditis elegans. Genetics 77, 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 33
    • 0029898363 scopus 로고    scopus 로고
    • Temporal reiteration of a precise gene expression pattern during nematode development
    • Johnstone, I.L. and Barry, J.D. (1996) Temporal reiteration of a precise gene expression pattern during nematode development. EMBO J. 15, 3633-3639
    • (1996) EMBO J , vol.15 , pp. 3633-3639
    • Johnstone, I.L.1    Barry, J.D.2
  • 34
    • 0033809287 scopus 로고    scopus 로고
    • Ligand-binding properties of annexin from Caenorhabditis elegans (annexin XVI, Nex-1)
    • Satoh, A., Miwa, H.E., Kojima, K. et al. (2000) Ligand-binding properties of annexin from Caenorhabditis elegans (annexin XVI, Nex-1). J. Biochem. (Tokyo) 128, 377-381
    • (2000) J. Biochem. (Tokyo) , vol.128 , pp. 377-381
    • Satoh, A.1    Miwa, H.E.2    Kojima, K.3
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber, R., Romisch, J., and Paques, E.P. (1990) The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 9, 3867-3874
    • (1990) EMBO J , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, J.2    Paques, E.P.3
  • 37
    • 0344010176 scopus 로고    scopus 로고
    • The lack of annexin A7 affects functions of primary astrocytes
    • Clemen, C.S., Herr, C., Hovelmeyer, N. et al. (2003) The lack of annexin A7 affects functions of primary astrocytes. Exp. Cell Res. 291, 406-414
    • (2003) Exp. Cell Res , vol.291 , pp. 406-414
    • Clemen, C.S.1    Herr, C.2    Hovelmeyer, N.3
  • 38
    • 0030875859 scopus 로고    scopus 로고
    • Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII)
    • Brownawell, A.M. and Creutz, C.E. (1997) Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII). J. Biol. Chem. 272, 22182-22190
    • (1997) J. Biol. Chem , vol.272 , pp. 22182-22190
    • Brownawell, A.M.1    Creutz, C.E.2
  • 39
    • 0036296413 scopus 로고    scopus 로고
    • ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner
    • Satoh, H., Shibata, H., Nakano, Y. et al. (2002) ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner. Biochem. Biophys. Res. Commun. 291, 1166-1172
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 1166-1172
    • Satoh, H.1    Shibata, H.2    Nakano, Y.3
  • 40
    • 0037020677 scopus 로고    scopus 로고
    • The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner
    • Satoh, H., Nakano, Y., Shibata, H. et al. (2002) The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner. Biochim. Biophys. Acta. 1600, 61-67
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 61-67
    • Satoh, H.1    Nakano, Y.2    Shibata, H.3
  • 41
    • 0038167010 scopus 로고    scopus 로고
    • The story of cell fusion: Big lessons from little worms
    • Shemer, G. and Podbilewicz, B. (2003) The story of cell fusion: big lessons from little worms. Bioessays 25, 672-682
    • (2003) Bioessays , vol.25 , pp. 672-682
    • Shemer, G.1    Podbilewicz, B.2
  • 42
    • 1542618335 scopus 로고    scopus 로고
    • Annexin 2-caveolin 1 complex is a target of ezetimibe and regulates intestinal cholesterol transport
    • Smart, E.J., De Rose, R.A., and Farber, S.A. (2004) Annexin 2-caveolin 1 complex is a target of ezetimibe and regulates intestinal cholesterol transport. Proc. Natl. Acad. Sci. USA 101, 3450-3455
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3450-3455
    • Smart, E.J.1    De Rose, R.A.2    Farber, S.A.3
  • 43
    • 4744361552 scopus 로고    scopus 로고
    • Protein glycosylation lessons from Caenorhabditis elegans
    • Schachter, H. (2004) Protein glycosylation lessons from Caenorhabditis elegans. Curr. Opin. Struct. Biol. 14, 607-616
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 607-616
    • Schachter, H.1
  • 44
    • 0032008243 scopus 로고    scopus 로고
    • Overproduction of beta-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES
    • Machida, S., Yu, Y., Singh, S.P. et al. (1998) Overproduction of beta-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES. FEMS Microbiol. Lett. 159, 41-46
    • (1998) FEMS Microbiol. Lett , vol.159 , pp. 41-46
    • Machida, S.1    Yu, Y.2    Singh, S.P.3
  • 45
    • 0038193706 scopus 로고    scopus 로고
    • Chaperone-assisted expression, purification, and characterization of recombinant nitrile hydratase NI1 from Comamonas testosteroni
    • Stevens, J.M., Rao Saroja, N., Jaouen, M. et al. (2003) Chaperone-assisted expression, purification, and characterization of recombinant nitrile hydratase NI1 from Comamonas testosteroni. Protein Expr. Purif. 29, 70-76
    • (2003) Protein Expr. Purif , vol.29 , pp. 70-76
    • Stevens, J.M.1    Rao Saroja, N.2    Jaouen, M.3
  • 46
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin, A.D. and Weintraub, H.J. (1989) Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9, 21-32
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2


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