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Volumn 18, Issue 5, 2008, Pages 384-394

Different affinity of galectins for human serum glycoproteins: Galectin-3 binds many protease inhibitors and acute phase proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACUTE PHASE PROTEIN; ALPHA 2 MACROGLOBULIN; ECALECTIN; GALECTIN 2; GALECTIN 3; GALECTIN 8; GLYCOPROTEIN; HAPTOGLOBIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; N ACETYLLACTOSAMINE SYNTHASE; PROTEINASE INHIBITOR; TRANSFERRIN;

EID: 42449153703     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwn015     Document Type: Article
Times cited : (62)

References (55)
  • 1
    • 1542313823 scopus 로고    scopus 로고
    • Galectins as inflammatory mediators
    • Almkvist J and Karlsson A. 2004. Galectins as inflammatory mediators. Glycoconj J. 19:575-581.
    • (2004) Glycoconj J , vol.19 , pp. 575-581
    • Almkvist, J.1    Karlsson, A.2
  • 2
    • 33646379376 scopus 로고    scopus 로고
    • Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: A conserved feature of the thiol ester protein family?
    • Arnold JN, Wallis R, Willis AC, Harvey DJ, Royle L, Dwek RA, Rudd PM, Sim RB. 2006. Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: A conserved feature of the thiol ester protein family? J Biol Chem. 281:6955-6963.
    • (2006) J Biol Chem , vol.281 , pp. 6955-6963
    • Arnold, J.N.1    Wallis, R.2    Willis, A.C.3    Harvey, D.J.4    Royle, L.5    Dwek, R.A.6    Rudd, P.M.7    Sim, R.B.8
  • 3
    • 33846689832 scopus 로고    scopus 로고
    • Mechano-transduction mediated secretion and uptake of galectin-3 in breast carcinoma cells: Implications in the extracellular functions of the lectin
    • Baptiste TA, James A, Saria M, Ochieng J. 2007. Mechano-transduction mediated secretion and uptake of galectin-3 in breast carcinoma cells: Implications in the extracellular functions of the lectin. Exp Cell Res. 313:652-664.
    • (2007) Exp Cell Res , vol.313 , pp. 652-664
    • Baptiste, T.A.1    James, A.2    Saria, M.3    Ochieng, J.4
  • 4
    • 33947577842 scopus 로고    scopus 로고
    • Activated alpha(2)-macroglobulin induces cell proliferation and mitogen-activated protein kinase activation by LRP-1 in the J774 macrophage-derived cell line
    • Bonacci GR, Caceres LC, Sanchez MC, Chiabrando GA. 2007. Activated alpha(2)-macroglobulin induces cell proliferation and mitogen-activated protein kinase activation by LRP-1 in the J774 macrophage-derived cell line. Arch Biochem Biophys. 460:100-106.
    • (2007) Arch Biochem Biophys , vol.460 , pp. 100-106
    • Bonacci, G.R.1    Caceres, L.C.2    Sanchez, M.C.3    Chiabrando, G.A.4
  • 6
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • Brewer CF. 2002. Binding and cross-linking properties of galectins. Biochim Biophys Acta. 1572:255-262.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 255-262
    • Brewer, C.F.1
  • 7
    • 33749363387 scopus 로고    scopus 로고
    • Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death
    • Cabrera PV, Amano M, Mitoma J, Chan J, Said J, Fukuda M, Baum LG. 2006. Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death. Blood. 108:2399-2406.
    • (2006) Blood , vol.108 , pp. 2399-2406
    • Cabrera, P.V.1    Amano, M.2    Mitoma, J.3    Chan, J.4    Said, J.5    Fukuda, M.6    Baum, L.G.7
  • 10
    • 34548118303 scopus 로고    scopus 로고
    • Studies of arginine-arene interactions through synthesis and evaluation of a series of galectin-binding aromatic lactose esters
    • Cumpstey I, Salomonsson E, Sundin A, Leffler H, Nilsson UJ. 2007. Studies of arginine-arene interactions through synthesis and evaluation of a series of galectin-binding aromatic lactose esters. Chembiochem. 8:1389-1398.
    • (2007) Chembiochem , vol.8 , pp. 1389-1398
    • Cumpstey, I.1    Salomonsson, E.2    Sundin, A.3    Leffler, H.4    Nilsson, U.J.5
  • 11
    • 33645311204 scopus 로고    scopus 로고
    • Lipid raft organization and function in brush borders of epithelial cells (Review)
    • Danielsen EM and Hansen GH. 2006. Lipid raft organization and function in brush borders of epithelial cells (Review). Mol Membr Biol. 23:71-79.
    • (2006) Mol Membr Biol , vol.23 , pp. 71-79
    • Danielsen, E.M.1    Hansen, G.H.2
  • 14
    • 0035098486 scopus 로고    scopus 로고
    • Carbohydrate structures of haptoglobin in sera of healthy people and a patient with congenital disorder of glycosylation
    • Ferens-Sieczkowska M and Olczak M. 2001. Carbohydrate structures of haptoglobin in sera of healthy people and a patient with congenital disorder of glycosylation. Z Naturforsch [C]. 56:122-131.
    • (2001) Z Naturforsch , vol.56 , Issue.C , pp. 122-131
    • Ferens-Sieczkowska, M.1    Olczak, M.2
  • 15
    • 0024580871 scopus 로고
    • Novel polyfucosylated N-linked glycopeptides with blood group A, H, X, and Y determinants from human small intestinal epithelial cells
    • Finne J, Breimer ME, Hansson GC, Karlsson KA, Leffler H, Vliegenthart JF, van Halbeek H. 1989. Novel polyfucosylated N-linked glycopeptides with blood group A, H, X, and Y determinants from human small intestinal epithelial cells. J Biol Chem. 264:5720-5735.
    • (1989) J Biol Chem , vol.264 , pp. 5720-5735
    • Finne, J.1    Breimer, M.E.2    Hansson, G.C.3    Karlsson, K.A.4    Leffler, H.5    Vliegenthart, J.F.6    van Halbeek, H.7
  • 18
    • 0032533239 scopus 로고    scopus 로고
    • Binding of soluble myelin basic protein to various conformational forms of alpha-2-macroglobulin
    • Gunnarsson M, Jenssen PEH. 1998. Binding of soluble myelin basic protein to various conformational forms of alpha-2-macroglobulin. Arch Biochem Biophys. 359:192-198.
    • (1998) Arch Biochem Biophys , vol.359 , pp. 192-198
    • Gunnarsson, M.1    Jenssen, P.E.H.2
  • 22
    • 4143128862 scopus 로고    scopus 로고
    • Galectin-4 in normal tissues and cancer
    • Huflejt ME and Leffler H. 2004. Galectin-4 in normal tissues and cancer. Glycoconj J. 20:247-255.
    • (2004) Glycoconj J , vol.20 , pp. 247-255
    • Huflejt, M.E.1    Leffler, H.2
  • 23
    • 14244257721 scopus 로고    scopus 로고
    • Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells
    • Ideo H, Seko A, Yamashita K. 2005. Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J Biol Chem. 280:4730-4737.
    • (2005) J Biol Chem , vol.280 , pp. 4730-4737
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 24
  • 25
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S, Mimura Y, Jefferis R, Huber R. Sondermann P. 2003. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J Mol Biol. 325:979-989.
    • (2003) J Mol Biol , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 27
    • 33744974791 scopus 로고    scopus 로고
    • Specific haptoglobin expression in bronchoalveolar lavage during differentiation of circulating fibroblast progenitor cells in mild asthma
    • Larsen K. Macleod D, Nihlberg K. Gurcan E. Bjermer L. Marko-Varga G. Westergren-Thorsson G. 2006. Specific haptoglobin expression in bronchoalveolar lavage during differentiation of circulating fibroblast progenitor cells in mild asthma. J Proteome Res. 5:1479-1483.
    • (2006) J Proteome Res , vol.5 , pp. 1479-1483
    • Larsen, K.1    Macleod, D.2    Nihlberg, K.3    Gurcan, E.4    Bjermer, L.5    Marko-Varga, G.6    Westergren-Thorsson, G.7
  • 28
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A. Silvescu CI, Reinhold VN, Demetriou M, Dennis JW. 2007. Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell. 129:123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 29
    • 0013895324 scopus 로고
    • Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies
    • Laurell CB. 1966. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem. 15:45-52.
    • (1966) Anal Biochem , vol.15 , pp. 45-52
    • Laurell, C.B.1
  • 31
    • 14044272136 scopus 로고    scopus 로고
    • Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans
    • Leppanen A, Stowell S, Blixt O, Cummings RD. 2005. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. J Biol Chem. 280:5549-5562.
    • (2005) J Biol Chem , vol.280 , pp. 5549-5562
    • Leppanen, A.1    Stowell, S.2    Blixt, O.3    Cummings, R.D.4
  • 32
    • 4444233697 scopus 로고    scopus 로고
    • Automated methods for improved protein identification by peptide mass fingerprinting
    • Levander F, Rognvaldsson T, Samuelsson J, James P. 2004. Automated methods for improved protein identification by peptide mass fingerprinting. Proteomics. 4:2594-2601.
    • (2004) Proteomics , vol.4 , pp. 2594-2601
    • Levander, F.1    Rognvaldsson, T.2    Samuelsson, J.3    James, P.4
  • 33
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions
    • Mattu TS, Pleass RJ, Willis AC, Kilian M, Wormald MR, Lellouch AC, Rudd PM, Woof JM, Dwek RA. 1998. The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions. J Biol Chem. 273:2260-2272.
    • (1998) J Biol Chem , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3    Kilian, M.4    Wormald, M.R.5    Lellouch, A.C.6    Rudd, P.M.7    Woof, J.M.8    Dwek, R.A.9
  • 34
    • 0023760470 scopus 로고
    • Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin
    • Merkle RK and Cummings RD. 1988. Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin. J Biol Chem. 263:16143-16149.
    • (1988) J Biol Chem , vol.263 , pp. 16143-16149
    • Merkle, R.K.1    Cummings, R.D.2
  • 35
    • 36348976981 scopus 로고    scopus 로고
    • Structural analysis of the human galectin-9N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue
    • Nagae N, Nishi N, Nakamura-Tsuruta S. Hirabayashi J, Wakatsuki SKR 2008. Structural analysis of the human galectin-9N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue. J Mol Biol. 375:119-135.
    • (2008) J Mol Biol , vol.375 , pp. 119-135
    • Nagae, N.1    Nishi, N.2    Nakamura-Tsuruta, S.3    Hirabayashi, J.4    Wakatsuki, S.K.R.5
  • 36
    • 33847718338 scopus 로고    scopus 로고
    • Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer
    • Nieminen J, Kuno A, Hirabayashi J, Sato S. 2007. Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer. J Biol Chem. 282:1374-1383.
    • (2007) J Biol Chem , vol.282 , pp. 1374-1383
    • Nieminen, J.1    Kuno, A.2    Hirabayashi, J.3    Sato, S.4
  • 37
    • 33645102970 scopus 로고    scopus 로고
    • Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells
    • Patnaik SK, Potvin B, Carlsson S, Sturin D, Leffler H, Stanley P. 2006. Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells. Glycobiology. 16:305-317.
    • (2006) Glycobiology , vol.16 , pp. 305-317
    • Patnaik, S.K.1    Potvin, B.2    Carlsson, S.3    Sturin, D.4    Leffler, H.5    Stanley, P.6
  • 38
    • 0038842637 scopus 로고    scopus 로고
    • Roles of galectins in vivo
    • Poirier F. 2002. Roles of galectins in vivo. Biochem Soc Symp. 95-103.
    • (2002) Biochem Soc Symp , pp. 95-103
    • Poirier, F.1
  • 39
    • 34447301574 scopus 로고    scopus 로고
    • An emerging role for galectins in tuning the immune response: Lessons from experimental models of inflammatory disease, autoimmunity and cancer
    • Rabinovich GA, Liu FT, Hirashima M, Anderson A. 2007. An emerging role for galectins in tuning the immune response: Lessons from experimental models of inflammatory disease, autoimmunity and cancer. Scand J Immunol. 66: 143-158.
    • (2007) Scand J Immunol , vol.66 , pp. 143-158
    • Rabinovich, G.A.1    Liu, F.T.2    Hirashima, M.3    Anderson, A.4
  • 40
    • 0028147336 scopus 로고
    • Transport of macromolecules across microvascular walls: The two-pore theory
    • Rippe B and Haraldsson B. 1994. Transport of macromolecules across microvascular walls: The two-pore theory. Physiol Rev. 74:163-219.
    • (1994) Physiol Rev , vol.74 , pp. 163-219
    • Rippe, B.1    Haraldsson, B.2
  • 41
    • 30344486680 scopus 로고    scopus 로고
    • Thioureido N acetyllactosamine derivatives as potent galectin-7 and 9N inhibitors
    • Salameh BA, Sundin A, Leffler H, Nilsson UJ. 2006. Thioureido N acetyllactosamine derivatives as potent galectin-7 and 9N inhibitors. Bioorg Med Chem. 14:12415-1220.
    • (2006) Bioorg Med Chem , vol.14 , pp. 12415-21220
    • Salameh, B.A.1    Sundin, A.2    Leffler, H.3    Nilsson, U.J.4
  • 42
    • 10844221548 scopus 로고    scopus 로고
    • Site specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry
    • Satomi Y, Shimonishi Y, Hase T, Takao T. 2004. Site specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry. Rapid Commun Mass Spectrom. 18:2983-2988.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 2983-2988
    • Satomi, Y.1    Shimonishi, Y.2    Hase, T.3    Takao, T.4
  • 43
    • 37049015985 scopus 로고    scopus 로고
    • The determination of the levels of circulating galectin-1 and -3 in HNSCC patients could be used to monitor tumor progression and/or responses to therapy
    • Saussez S, Lotfevre F, Lequeux T, Laurent G, Chantrain G, Vertongen F; Toubeau G, Decaestecker C, Kiss R. 2008. The determination of the levels of circulating galectin-1 and -3 in HNSCC patients could be used to monitor tumor progression and/or responses to therapy. Oral Oncol. 44:86-93.
    • (2008) Oral Oncol , vol.44 , pp. 86-93
    • Saussez, S.1    Lotfevre, F.2    Lequeux, T.3    Laurent, G.4    Chantrain, G.5    Vertongen, F.6    Toubeau, G.7    Decaestecker, C.8    Kiss, R.9
  • 45
    • 4644260095 scopus 로고    scopus 로고
    • Fluorescence polarization as an analytical tool to evaluate galectin-ligand interactions
    • Sorme P, Kahl-Knutsson B, Huflejt M, Nilsson, UJ. Leffler H. 2004. Fluorescence polarization as an analytical tool to evaluate galectin-ligand interactions Anal Biochem. 334:36-47.
    • (2004) Anal Biochem , vol.334 , pp. 36-47
    • Sorme, P.1    Kahl-Knutsson, B.2    Huflejt, M.3    Nilsson, U.J.4    Leffler, H.5
  • 46
    • 30744445427 scopus 로고    scopus 로고
    • Galectin-3 and galectin- 1 bind distinct cell surface glycoproteiri receptors to induce T cell death
    • Stillman BN, Hsu DK, Pang M. Brewer CF. Johnson P. Liu FT. Baum LG. 2006. Galectin-3 and galectin- 1 bind distinct cell surface glycoproteiri receptors to induce T cell death. J Immunol. 176:778-789.
    • (2006) J Immunol , vol.176 , pp. 778-789
    • Stillman, B.N.1    Hsu, D.K.2    Pang, M.3    Brewer, C.F.4    Johnson, P.5    Liu, F.T.6    Baum, L.G.7
  • 48
    • 39549084700 scopus 로고    scopus 로고
    • The galectin profile of the endothelium: Altered expression and localization in activated and tumor endothelial cells
    • Thijssen VL, Hulsmans S, Griffioen AW. 2008. The galectin profile of the endothelium: Altered expression and localization in activated and tumor endothelial cells. Am J Pathol. 172:545-553.
    • (2008) Am J Pathol , vol.172 , pp. 545-553
    • Thijssen, V.L.1    Hulsmans, S.2    Griffioen, A.W.3
  • 49
    • 35549003245 scopus 로고    scopus 로고
    • Galectins in the tumor endothelium; oppoftunities for combined calicer therapy
    • Thijssen VL, Poirier F, Baum LG, Griffioen AW. 2007. Galectins in the tumor endothelium; oppoftunities for combined calicer therapy. Blood. 110:2819-2827.
    • (2007) Blood , vol.110 , pp. 2819-2827
    • Thijssen, V.L.1    Poirier, F.2    Baum, L.G.3    Griffioen, A.W.4
  • 51
    • 33947192955 scopus 로고    scopus 로고
    • Comparison of the methods for profiling glycoprotein glycans - HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study
    • Wada Y, Azadi P, Costello CF, Dell A, Dwek RA, Geyer H, Geyer R, Kakehi K, Karlsson NG, Kato K, et al. 2007. Comparison of the methods for profiling glycoprotein glycans - HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study. Glycobiology. 17:411-422.
    • (2007) Glycobiology , vol.17 , pp. 411-422
    • Wada, Y.1    Azadi, P.2    Costello, C.F.3    Dell, A.4    Dwek, R.A.5    Geyer, H.6    Geyer, R.7    Kakehi, K.8    Karlsson, N.G.9    Kato, K.10
  • 52
    • 0033693730 scopus 로고    scopus 로고
    • Haptoglobin: Function and polymorphism
    • Wassell J. 2000. Haptoglobin: Function and polymorphism. Clin Lab. 46:547-552.
    • (2000) Clin Lab , vol.46 , pp. 547-552
    • Wassell, J.1
  • 53
    • 0024562457 scopus 로고
    • Altered glycosylation of serum transferrin of patients with hepatocellular carcimona
    • Yamashita K, Koide N, Endo T, Iwaki Y, Kobata A. 1989. Altered glycosylation of serum transferrin of patients with hepatocellular carcimona. J Biol Chem. 264:2415-2423.
    • (1989) J Biol Chem , vol.264 , pp. 2415-2423
    • Yamashita, K.1    Koide, N.2    Endo, T.3    Iwaki, Y.4    Kobata, A.5
  • 55
    • 0027162467 scopus 로고
    • L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion
    • Zhou Q and Cummings RD. 1993. L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion. Arch Biochem Biophys. 300:6-17.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 6-17
    • Zhou, Q.1    Cummings, R.D.2


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