메뉴 건너뛰기




Volumn 1840, Issue 6, 2014, Pages 1892-1901

Direct cytocidal effect of galectin-9 localized on collagen matrices on human immune cell lines

Author keywords

Collagen; Collagen binding domain; Galectin; Immune suppression

Indexed keywords

COLLAGEN; COLLAGEN BINDING PEPTIDE; COLLAGENASE; ECALECTIN; GALECTIN 9 FUSION PROTEIN; HYBRID PROTEIN; OLIGOSACCHARIDE; PEPTIDE; UNCLASSIFIED DRUG; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 112 HIGHLY STABLE AND SOLUBLE FORM OF GALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 112 PROTEASE RESISTANT FORM OFGALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 115 HIGHLY STABLE AND SOLUBLE FORM OF GALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 115 PROTEASE RESISTANT FORM OF GALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 302 HIGHLY STABLE AND SOLUBLE FORM OF GALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 302 PROTEASE RESISTANT FORM OF GALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 305 HIGHLY STABLE AND SOLUBLE FORM OF GALECTIN 9 FUSION PROTEIN; CLOSTRIDIUM HISTOLYTICUM COLLAGENASE COLLAGEN BINDING DOMAIN 305 PROTEASE RESISTANT FORM OF GALECTIN 9 FUSION PROTEIN; COLLAGEN BINDING PEPTIDE HIGHLY STABLE AND SOLUBLE FORM OF GALECTIN 9 FUSION PROTEIN; COLLAGEN BINDING PEPTIDE PROTEASE RESISTANT FORM OF GALECTIN 9 FUSION PROTEIN; COLLAGEN BINDING PROTEIN; COLLAGEN TYPE 1; LACTOSE; RECOMBINANT PROTEIN;

EID: 84897099799     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.01.019     Document Type: Article
Times cited : (6)

References (45)
  • 2
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • J. Hirabayashi, and K. Kasai The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution Glycobiology 3 1993 297 304 (Pubitemid 23281277)
    • (1993) Glycobiology , vol.3 , Issue.4 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.-I.2
  • 3
    • 0042291641 scopus 로고    scopus 로고
    • Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease
    • DOI 10.1074/jbc.272.10.6416
    • O. Tureci, H. Schmitt, N. Fadle, M. Pfreundschuh, and U. Sahin Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease J. Biol. Chem. 272 1997 6416 6422 (Pubitemid 27118120)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6416-6422
    • Tureci, O.1    Schmitt, H.2    Fadle, N.3    Pfreundschuh, M.4    Sahin, U.5
  • 7
    • 84876066355 scopus 로고    scopus 로고
    • Galectin-9 ameliorates clinical severity of MRL/lpr lupus-prone mice by inducing plasma cell apoptosis independently of Tim-3
    • M. Moritoki, T. Kadowaki, T. Niki, D. Nakano, G. Soma, H. Mori, H. Kobara, T. Masaki, M. Kohno, and M. Hirashima Galectin-9 ameliorates clinical severity of MRL/lpr lupus-prone mice by inducing plasma cell apoptosis independently of Tim-3 PLoS One 8 2013 e60807
    • (2013) PLoS One , vol.8 , pp. 60807
    • Moritoki, M.1    Kadowaki, T.2    Niki, T.3    Nakano, D.4    Soma, G.5    Mori, H.6    Kobara, H.7    Masaki, T.8    Kohno, M.9    Hirashima, M.10
  • 8
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • DOI 10.1016/j.cell.2005.09.041, PII S0092867405011712
    • K. Ohtsubo, S. Takamatsu, M.T. Minowa, A. Yoshida, M. Takeuchi, and J.D. Marth Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes Cell 123 2005 1307 1321 (Pubitemid 41821787)
    • (2005) Cell , vol.123 , Issue.7 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6
  • 11
    • 45549107987 scopus 로고    scopus 로고
    • Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways
    • S. Bi, L.A. Earl, L. Jacobs, and L.G. Baum Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways J. Biol. Chem. 283 2008 12248 12258
    • (2008) J. Biol. Chem. , vol.283 , pp. 12248-12258
    • Bi, S.1    Earl, L.A.2    Jacobs, L.3    Baum, L.G.4
  • 12
    • 78049312395 scopus 로고    scopus 로고
    • Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells
    • R. Mishra, M. Grzybek, T. Niki, M. Hirashima, and K. Simons Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells Proc. Natl. Acad. Sci. U. S. A. 107 2010 17633 17638
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 17633-17638
    • Mishra, R.1    Grzybek, M.2    Niki, T.3    Hirashima, M.4    Simons, K.5
  • 13
    • 70450265476 scopus 로고    scopus 로고
    • Galectin-9 is a high affinity IgE-binding lectin with anti-allergic effect by blocking IgE-antigen complex formation
    • T. Niki, S. Tsutsui, S. Hirose, S. Aradono, Y. Sugimoto, K. Takeshita, N. Nishi, and M. Hirashima Galectin-9 is a high affinity IgE-binding lectin with anti-allergic effect by blocking IgE-antigen complex formation J. Biol. Chem. 284 2009 32344 32352
    • (2009) J. Biol. Chem. , vol.284 , pp. 32344-32352
    • Niki, T.1    Tsutsui, S.2    Hirose, S.3    Aradono, S.4    Sugimoto, Y.5    Takeshita, K.6    Nishi, N.7    Hirashima, M.8
  • 14
    • 80052673578 scopus 로고    scopus 로고
    • Galectin-9 regulates T helper cell function independently of Tim-3
    • E.W. Su, S. Bi, and L.P. Kane Galectin-9 regulates T helper cell function independently of Tim-3 Glycobiology 21 2011 1258 1265
    • (2011) Glycobiology , vol.21 , pp. 1258-1265
    • Su, E.W.1    Bi, S.2    Kane, L.P.3
  • 16
    • 70349245383 scopus 로고    scopus 로고
    • Attenuation of Th1 response through galectin-9 and T-cell Ig mucin 3 interaction inhibits autoimmune diabetes in NOD mice
    • F.C. Chou, S.J. Shieh, and H.K. Sytwu Attenuation of Th1 response through galectin-9 and T-cell Ig mucin 3 interaction inhibits autoimmune diabetes in NOD mice Eur. J. Immunol. 39 2009 2403 2411
    • (2009) Eur. J. Immunol. , vol.39 , pp. 2403-2411
    • Chou, F.C.1    Shieh, S.J.2    Sytwu, H.K.3
  • 18
    • 40849083349 scopus 로고    scopus 로고
    • Activation of Tim-3-Galectin-9 pathway improves survival of fully allogeneic skin grafts
    • F. Wang, W. He, J. Yuan, K. Wu, H. Zhou, W. Zhang, and Z.K. Chen Activation of Tim-3-Galectin-9 pathway improves survival of fully allogeneic skin grafts Transpl. Immunol. 19 2008 12 19
    • (2008) Transpl. Immunol. , vol.19 , pp. 12-19
    • Wang, F.1    He, W.2    Yuan, J.3    Wu, K.4    Zhou, H.5    Zhang, W.6    Chen, Z.K.7
  • 20
    • 84883460463 scopus 로고    scopus 로고
    • Galectin-9 in combination with rapamycin induces cardiac allograft tolerance in mice
    • L. Cai, H. Zhou, Z. Fang, J. Yuan, T. Niki, M. Hirashima, W. He, and Z.K. Chen Galectin-9 in combination with rapamycin induces cardiac allograft tolerance in mice Transplantation 96 2013 379 386
    • (2013) Transplantation , vol.96 , pp. 379-386
    • Cai, L.1    Zhou, H.2    Fang, Z.3    Yuan, J.4    Niki, T.5    Hirashima, M.6    He, W.7    Chen, Z.K.8
  • 23
    • 84897065658 scopus 로고    scopus 로고
    • Acceleration of periosteal bone formation by human basic fibroblast growth factor containing a collagen-binding domain from Clostridium histolyticum collagenase
    • (in press)
    • K. Uchida, O. Matsushita, K. Naruse, T. Mima, N. Nishi, S. Hattori, T. Ogura, G. Inoue, K. Tanaka, and M. Takaso Acceleration of periosteal bone formation by human basic fibroblast growth factor containing a collagen-binding domain from Clostridium histolyticum collagenase J. Biomed. Mater. Res. Part A 2014 (in press)
    • (2014) J. Biomed. Mater. Res. Part A
    • Uchida, K.1    Matsushita, O.2    Naruse, K.3    Mima, T.4    Nishi, N.5    Hattori, S.6    Ogura, T.7    Inoue, G.8    Tanaka, K.9    Takaso, M.10
  • 24
    • 34547881107 scopus 로고    scopus 로고
    • Vascularization and cellularization of collagen scaffolds incorporated with two different collagen-targeting human basic fibroblast growth factors
    • DOI 10.1002/jbm.a.31179
    • W. Zhao, B. Chen, X. Li, H. Lin, W. Sun, Y. Zhao, B. Wang, Q. Han, and J. Dai Vascularization and cellularization of collagen scaffolds incorporated with two different collagen-targeting human basic fibroblast growth factors J. Biomed. Mater. Res. Part A 82 2007 630 636 (Pubitemid 47258577)
    • (2007) Journal of Biomedical Materials Research - Part A , vol.82 , Issue.3 , pp. 630-636
    • Zhao, W.1    Chen, B.2    Li, X.3    Lin, H.4    Sun, W.5    Zhao, Y.6    Wang, B.7    Zhao, Y.8    Han, Q.9    Dai, J.10
  • 25
    • 84861706178 scopus 로고    scopus 로고
    • Design and synthesis of binding growth factors
    • S. Tada, T. Kitajima, and Y. Ito Design and synthesis of binding growth factors Int. J. Mol. Sci. 13 2012 6053 6072
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 6053-6072
    • Tada, S.1    Kitajima, T.2    Ito, Y.3
  • 26
    • 16344392326 scopus 로고    scopus 로고
    • Development of highly stable galectins: Truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins
    • DOI 10.1016/j.febslet.2005.02.054
    • N. Nishi, A. Itoh, A. Fujiyama, N. Yoshida, S. Araya, M. Hirashima, H. Shoji, and T. Nakamura Development of highly stable galectins: truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins FEBS Lett. 579 2005 2058 2064 (Pubitemid 40469670)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2058-2064
    • Nishi, N.1    Itoh, A.2    Fujiyama, A.3    Yoshida, N.4    Araya, S.-I.5    Hirashima, M.6    Shoji, H.7    Nakamura, T.8
  • 27
  • 28
    • 0032488998 scopus 로고    scopus 로고
    • A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase
    • DOI 10.1074/jbc.273.6.3643
    • O. Matsushita, C.M. Jung, J. Minami, S. Katayama, N. Nishi, and A. Okabe A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase J. Biol. Chem. 273 1998 3643 3648 (Pubitemid 28109790)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3643-3648
    • Matsushita, O.1    Jung, C.-M.2    Minami, J.3    Katayama, S.4    Nishi, N.5    Okabe, A.6
  • 31
    • 57049185150 scopus 로고    scopus 로고
    • Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1
    • DOI 10.1093/glycob/cwn089
    • N. Nishi, A. Abe, J. Iwaki, H. Yoshida, A. Itoh, H. Shoji, S. Kamitori, J. Hirabayashi, and T. Nakamura Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1 Glycobiology 18 2008 1065 1073 (Pubitemid 352762841)
    • (2008) Glycobiology , vol.18 , Issue.12 , pp. 1065-1073
    • Nishi, N.1    Abe, A.2    Iwaki, J.3    Yoshida, H.4    Itoh, A.5    Shoji, H.6    Kamitori, S.7    Hirabayashi, J.8    Nakamura, T.9
  • 33
    • 0344942600 scopus 로고    scopus 로고
    • A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation
    • DOI 10.1093/emboj/cdg172
    • J.J. Wilson, O. Matsushita, A. Okabe, and J. Sakon A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation EMBO J. 22 2003 1743 1752 (Pubitemid 36460131)
    • (2003) EMBO Journal , vol.22 , Issue.8 , pp. 1743-1752
    • Wilson, J.J.1    Matsushita, O.2    Okabe, A.3    Sakon, J.4
  • 35
    • 0035937822 scopus 로고    scopus 로고
    • Substrate recognition by the collagen-binding domain of Clostridium histolyticum class i collagenase
    • O. Matsushita, T. Koide, R. Kobayashi, K. Nagata, and A. Okabe Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase J. Biol. Chem. 276 2001 8761 8770
    • (2001) J. Biol. Chem. , vol.276 , pp. 8761-8770
    • Matsushita, O.1    Koide, T.2    Kobayashi, R.3    Nagata, K.4    Okabe, A.5
  • 37
    • 0018306812 scopus 로고
    • Characterization of a novel collagen chain in human placenta and its relation to AB collagen
    • H. Sage, and P. Bornstein Characterization of a novel collagen chain in human placenta and its relation to AB collagen Biochemistry 18 1979 3815 3822
    • (1979) Biochemistry , vol.18 , pp. 3815-3822
    • Sage, H.1    Bornstein, P.2
  • 40
    • 0014690194 scopus 로고
    • Characterization and quantitative determination of the hydroxylysine-linked carbohydrate units of several collagens
    • R.G. Spiro Characterization and quantitative determination of the hydroxylysine-linked carbohydrate units of several collagens J. Biol. Chem. 244 1969 602 612
    • (1969) J. Biol. Chem. , vol.244 , pp. 602-612
    • Spiro, R.G.1
  • 41
    • 72649101231 scopus 로고    scopus 로고
    • Collagen-binding human epidermal growth factor promotes cellularization of collagen scaffolds
    • Y. Yang, Y. Zhao, B. Chen, Q. Han, W. Sun, Z. Xiao, and J. Dai Collagen-binding human epidermal growth factor promotes cellularization of collagen scaffolds Tissue Eng. Part A 15 2009 3589 3596
    • (2009) Tissue Eng. Part A , vol.15 , pp. 3589-3596
    • Yang, Y.1    Zhao, Y.2    Chen, B.3    Han, Q.4    Sun, W.5    Xiao, Z.6    Dai, J.7
  • 42
    • 84862787773 scopus 로고    scopus 로고
    • Extrahepatic bile duct regeneration in pigs using collagen scaffolds loaded with human collagen-binding bFGF
    • Q. Li, L. Tao, B. Chen, H. Ren, X. Hou, S. Zhou, J. Zhou, X. Sun, J. Dai, and Y. Ding Extrahepatic bile duct regeneration in pigs using collagen scaffolds loaded with human collagen-binding bFGF Biomaterials 33 2012 4298 4308
    • (2012) Biomaterials , vol.33 , pp. 4298-4308
    • Li, Q.1    Tao, L.2    Chen, B.3    Ren, H.4    Hou, X.5    Zhou, S.6    Zhou, J.7    Sun, X.8    Dai, J.9    Ding, Y.10
  • 43
    • 83555178376 scopus 로고    scopus 로고
    • The effect of collagen-binding vascular endothelial growth factor on the remodeling of scarred rat uterus following full-thickness injury
    • N. Lin, X. Li, T. Song, J. Wang, K. Meng, J. Yang, X. Hou, J. Dai, and Y. Hu The effect of collagen-binding vascular endothelial growth factor on the remodeling of scarred rat uterus following full-thickness injury Biomaterials 33 2012 1801 1807
    • (2012) Biomaterials , vol.33 , pp. 1801-1807
    • Lin, N.1    Li, X.2    Song, T.3    Wang, J.4    Meng, K.5    Yang, J.6    Hou, X.7    Dai, J.8    Hu, Y.9
  • 44
    • 0026751189 scopus 로고
    • Collagen binding site in collagenase can be determined using the concept of sense-antisense peptide interactions
    • S.J. de Souza, and R. Brentani Collagen binding site in collagenase can be determined using the concept of sense-antisense peptide interactions J. Biol. Chem. 267 1992 13763 13767
    • (1992) J. Biol. Chem. , vol.267 , pp. 13763-13767
    • De Souza, S.J.1    Brentani, R.2
  • 45
    • 4444288628 scopus 로고    scopus 로고
    • Collagen vitrigel: A novel scaffold that can facilitate a three-dimensional culture for reconstructing organoids
    • T. Takezawa, K. Ozaki, A. Nitani, C. Takabayashi, and T. Shimo-Oka Collagen vitrigel: a novel scaffold that can facilitate a three-dimensional culture for reconstructing organoids Cell Transplant. 13 2004 463 473 (Pubitemid 39163091)
    • (2004) Cell Transplantation , vol.13 , Issue.4 , pp. 463-473
    • Takezawa, T.1    Ozaki, K.2    Nitani, A.3    Takabayashi, C.4    Shimo-Oka, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.