메뉴 건너뛰기




Volumn 435, Issue , 1998, Pages 133-143

Cytokine and protease glycosylation as a regulatory mechanism in inflammation and autoimmunity

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; PROTEINASE;

EID: 0031602226     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-5383-0_13     Document Type: Article
Times cited : (33)

References (47)
  • 2
    • 0025264198 scopus 로고
    • Granulocyte-macrophage colony stimulating factor from human lymphocytes. The effect of glycosylation on receptor binding and biological activity
    • Cebon, J., Nicola, N., Ward, M., Gardner, I., Dempsey, P., Layton, J., Durhrsen, U., Burgess, A.W., Nice, E., and Morstyn, G., 1990, Granulocyte-macrophage colony stimulating factor from human lymphocytes. The effect of glycosylation on receptor binding and biological activity, J. Biol. Chem. 265:4483-4491.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4483-4491
    • Cebon, J.1    Nicola, N.2    Ward, M.3    Gardner, I.4    Dempsey, P.5    Layton, J.6    Durhrsen, U.7    Burgess, A.W.8    Nice, E.9    Morstyn, G.10
  • 4
    • 0027413493 scopus 로고
    • Role of the glycosaminoglycan component of thrombomodulin in its acceleration of the inactivation of single-chain urokinase-type plasminogen activator by thrombin
    • de Munk, G.A., Parkinson, J.F., Groeneveld, E., Bang, N.U., and Rijken, D.C., 1993, Role of the glycosaminoglycan component of thrombomodulin in its acceleration of the inactivation of single-chain urokinase-type plasminogen activator by thrombin, Biochem. J. 290:655-659.
    • (1993) Biochem. J. , vol.290 , pp. 655-659
    • De Munk, G.A.1    Parkinson, J.F.2    Groeneveld, E.3    Bang, N.U.4    Rijken, D.C.5
  • 5
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • K.
    • K., 1991, Clearing up glycoprotein hormones, Cell 67:1029-1032.
    • (1991) Cell , vol.67 , pp. 1029-1032
  • 6
    • 0023227390 scopus 로고
    • Heterogeneity of chinese hamster ovary cell-produced recombinant interferon-g
    • Dijkmans, R., Heremans, H., and Billiau, A., 1987, Heterogeneity of chinese hamster ovary cell-produced recombinant interferon-g, J. Biol. Chem. 262:2528-2535.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2528-2535
    • Dijkmans, R.1    Heremans, H.2    Billiau, A.3
  • 7
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • Drickamer, K., 1991, Clearing up glycoprotein hormones, Cell 67:1029-1032.
    • (1991) Cell , vol.67 , pp. 1029-1032
    • Drickamer, K.1
  • 9
    • 43949151961 scopus 로고
    • Surface-bound cytokines -a possible effector mechanism in bacterial immunity?
    • George, A.J.T., 1994, Surface-bound cytokines -a possible effector mechanism in bacterial immunity?, Immunol. Today 15:88-89.
    • (1994) Immunol. Today , vol.15 , pp. 88-89
    • George, A.J.T.1
  • 10
    • 0027718044 scopus 로고
    • A thermodynamic model for denaturation of granulocyte colony-stimulating factor: O-linked sugar chain suppresses not the triggering deprotonation but the succeeding denaturation
    • Hasegawa, M., 1993, A thermodynamic model for denaturation of granulocyte colony-stimulating factor: O-linked sugar chain suppresses not the triggering deprotonation but the succeeding denaturation, Biochim. Biophys. Acta. 1203:295-297.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 295-297
    • Hasegawa, M.1
  • 11
    • 0028809115 scopus 로고
    • Full active baculovirus-expressed human monocyte chemoattractant protein I with the intact N-terminus
    • Ishii, K., Yamagami, S., Tanaka, H., Motoki, M., Suwa, Y. and Endo, N., 1995, Full active baculovirus-expressed human monocyte chemoattractant protein I with the intact N-terminus, Biochem. Biophys. Res. Comm. 206:955-961.
    • (1995) Biochem. Biophys. Res. Comm. , vol.206 , pp. 955-961
    • Ishii, K.1    Yamagami, S.2    Tanaka, H.3    Motoki, M.4    Suwa, Y.5    Endo, N.6
  • 12
    • 0027414938 scopus 로고
    • Role of sugar chains in the in-vitro activity of recombinant human interleukin 5
    • Kodama, S., Tsujimoto, M., Tsuruoka, N., Sugo, T., Endo, T., and Kobata, A., 1993, Role of sugar chains in the in-vitro activity of recombinant human interleukin 5, Eur. J. Biochem. 211:903-908.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 903-908
    • Kodama, S.1    Tsujimoto, M.2    Tsuruoka, N.3    Sugo, T.4    Endo, T.5    Kobata, A.6
  • 13
    • 0026161362 scopus 로고
    • High-level production of murine interleukin-5 (IL-5) utilising recombinant baculovirus expression. Purification of the rill-5 and its use in assessing the biologic role of IL-5 glycosylation
    • Kunimoto, D.Y., Allison, K.C., Watson, C., Fuerst, T., Armstrong, G.D., Paul, W., and Strober, W., 1991, High-level production of murine interleukin-5 (IL-5) utilising recombinant baculovirus expression. Purification of the rill-5 and its use in assessing the biologic role of IL-5 glycosylation, Cytokine 3:224-230.
    • (1991) Cytokine , vol.3 , pp. 224-230
    • Kunimoto, D.Y.1    Allison, K.C.2    Watson, C.3    Fuerst, T.4    Armstrong, G.D.5    Paul, W.6    Strober, W.7
  • 14
    • 0025370911 scopus 로고
    • Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae
    • Livi, G.P., Ferrara, A.A., Roskin, R., Simon, Pl., and Young, Pr., 1990, Secretion of N-glycosylated human recombinant interleukin-1 alpha in Saccharomyces cerevisiae. Gene 88:297-301.
    • (1990) Gene , vol.88 , pp. 297-301
    • Livi, G.P.1    Ferrara, A.A.2    Roskin, R.3    Simon, Pl.4    Young, Pr.5
  • 15
    • 0025883650 scopus 로고
    • Secretion of N-glycosylated interleukin-1 beta in Saccharomyces cerevisiae using a leader peptide from Candida albicans. Effect of N-glycosylation on biological activity
    • Livi, G.P., Lillquist, J.S., Miles, L.M., Ferrara, A., Sathe, G.M., Simon, Pl., Meyers, C.A., Gorman, J.A., Young, Pr., 1991, Secretion of N-glycosylated interleukin-1 beta in Saccharomyces cerevisiae using a leader peptide from Candida albicans. Effect of N-glycosylation on biological activity, J. Biol. Chem. 266:15348-15355.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15348-15355
    • Livi, G.P.1    Lillquist, J.S.2    Miles, L.M.3    Ferrara, A.4    Sathe, G.M.5    Simon, Pl.6    Meyers, C.A.7    Gorman, J.A.8    Young, Pr.9
  • 17
    • 0025232766 scopus 로고
    • Separation by cation-exchange high-performance liquid chromatography of three forms of Chinese hamster ovary cell-derived recombinant human interleukin-2
    • Marchese, E., Vita, N., Maureaud, T., Ferrara, P., 1990, Separation by cation-exchange high-performance liquid chromatography of three forms of Chinese hamster ovary cell-derived recombinant human interleukin-2, J. Chromatogr. 504:351-358.
    • (1990) J. Chromatogr. , vol.504 , pp. 351-358
    • Marchese, E.1    Vita, N.2    Maureaud, T.3    Ferrara, P.4
  • 18
    • 0027426024 scopus 로고
    • Mouse gelatinase B: CDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation
    • Masure, S., Nys, G., Fiten, P., Van Damme, J., and Opdenakker, G., 1993, Mouse gelatinase B: cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation, Eur. J. Biochem. 218:129-141.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 129-141
    • Masure, S.1    Nys, G.2    Fiten, P.3    Van Damme, J.4    Opdenakker, G.5
  • 19
    • 0024346064 scopus 로고
    • Cytokine-mediated proteolysis in tissue remodelling
    • Masure, S., and Opdenakker, G. 1989, Cytokine-mediated proteolysis in tissue remodelling, Experientia 45:542-549.
    • (1989) Experientia , vol.45 , pp. 542-549
    • Masure, S.1    Opdenakker, G.2
  • 21
    • 0028832978 scopus 로고
    • The activation of type 1 and type 2 plasminogen by type 1 and type 2 tissue plasminogen activator
    • Mori, K., Dwek, R.A., Downing, A.K., Opdenakker, G., and Rudd, P.M., 1995, The activation of type 1 and type 2 plasminogen by type 1 and type 2 tissue plasminogen activator, J. Biol. Chem. 270:3261-3267.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3261-3267
    • Mori, K.1    Dwek, R.A.2    Downing, A.K.3    Opdenakker, G.4    Rudd, P.M.5
  • 23
    • 0026491215 scopus 로고
    • Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition
    • Naim, H.Y., and Lentze, M.J., 1992, Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition, J. Biol. Chem. 267:25494-25504.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25494-25504
    • Naim, H.Y.1    Lentze, M.J.2
  • 24
    • 0028289809 scopus 로고
    • In vitro comparison of the biological potency of glycosylated versus nonglycosylated rG-CSF
    • Nissen, C., Dalle Carbonare, V., and Moser, Y., 1994, In vitro comparison of the biological potency of glycosylated versus nonglycosylated rG-CSF, Drug invest. 7:346-352.
    • (1994) Drug Invest. , vol.7 , pp. 346-352
    • Nissen, C.1    Dalle Carbonare, V.2    Moser, Y.3
  • 25
    • 0025284968 scopus 로고
    • O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity
    • Oh-eda, M., Hasegawa, M., Hattori, K., Kuboniwa, H., Kojima, T., Orita, T., Tomonou, K., Yamazaki, T., and Ochi, N., 1990, O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity, J. Biol. Chem. 265:11432-11435.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11432-11435
    • Oh-eda, M.1    Hasegawa, M.2    Hattori, K.3    Kuboniwa, H.4    Kojima, T.5    Orita, T.6    Tomonou, K.7    Yamazaki, T.8    Ochi, N.9
  • 28
  • 29
    • 0026890915 scopus 로고
    • Cytokines and proteases in invasive processes: Molecular similarities between inflammation and cancer
    • Opdenakker, G., and Van Damme, J., 1992, Cytokines and proteases in invasive processes: molecular similarities between inflammation and cancer, Cytokine 4:251-258.
    • (1992) Cytokine , vol.4 , pp. 251-258
    • Opdenakker, G.1    Van Damme, J.2
  • 30
    • 0028328881 scopus 로고
    • Cytokine-induced proteolysis in autoimmune diseases
    • Opdenakker, G., and Van Damme J., 1994, Cytokine-induced proteolysis in autoimmune diseases, Immunol. Today 15:104-107.
    • (1994) Immunol. Today , vol.15 , pp. 104-107
    • Opdenakker, G.1    Van Damme, J.2
  • 34
    • 0026506310 scopus 로고
    • Recombinant human thrombomodulin. Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain
    • Parkinson, J.F., Vlahos, C.J., Yan, S.C., and Bang, N.U., 1992, Recombinant human thrombomodulin. Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain, Biochem. J. 283:151-157.
    • (1992) Biochem. J. , vol.283 , pp. 151-157
    • Parkinson, J.F.1    Vlahos, C.J.2    Yan, S.C.3    Bang, N.U.4
  • 35
    • 0025201215 scopus 로고
    • Changes in the serum concentration and the glycosylation of human alpha 1-acid glycoprotein and alpha 1-protease inhibitor in severely burned persons: Relation to interleukin-6 levels
    • Pos, O., van der stelt, M.E., Wolbink, G.J., Nijsten, M.W., van der Tempel, G.L., and van Dijk, W., 1990, Changes in the serum concentration and the glycosylation of human alpha 1-acid glycoprotein and alpha 1-protease inhibitor in severely burned persons: relation to interleukin-6 levels, Clin. Exp. Immunol. 82:579-582.
    • (1990) Clin. Exp. Immunol. , vol.82 , pp. 579-582
    • Pos, O.1    Van Der Stelt, M.E.2    Wolbink, G.J.3    Nijsten, M.W.4    Van Der Tempel, G.L.5    Van Dijk, W.6
  • 37
    • 0025807832 scopus 로고
    • Characterisation of human interferon-gamma and human interleukin-2 from recombinant mammalian cell lines and peripheral blood lymphocytes
    • Riske, F.J., Cullen, B.R., Chizzonite, R., 1991, Characterisation of human interferon-gamma and human interleukin-2 from recombinant mammalian cell lines and peripheral blood lymphocytes, Lymphokine and Cytokine Res. 10:213-218.
    • (1991) Lymphokine and Cytokine Res. , vol.10 , pp. 213-218
    • Riske, F.J.1    Cullen, B.R.2    Chizzonite, R.3
  • 39
    • 0028921674 scopus 로고
    • The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator
    • Rudd, P.M., Woods, R.J., Wormald, M.R., Opdenakker, G., Downing, A.K., Campbell, I.D., and Dwek, R.A., 1995, The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator, Biochim. Biophys. Acta 1248:1-10.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 1-10
    • Rudd, P.M.1    Woods, R.J.2    Wormald, M.R.3    Opdenakker, G.4    Downing, A.K.5    Campbell, I.D.6    Dwek, R.A.7
  • 40
  • 41
    • 0025490235 scopus 로고
    • Biochemical and biological analysis of human interleukin 6 expressed in rodent and primate cells
    • Tanner, J.E., Goldman, N.D., and Tosato, G., 1990, Biochemical and biological analysis of human interleukin 6 expressed in rodent and primate cells, Cytokine 2:363-374.
    • (1990) Cytokine , vol.2 , pp. 363-374
    • Tanner, J.E.1    Goldman, N.D.2    Tosato, G.3
  • 42
    • 0026602231 scopus 로고
    • Glycosylation variants of murine interleukin-4: Evidence for different functional properties
    • Thor, G., Brian, A.A., 1992, Glycosylation variants of murine interleukin-4: evidence for different functional properties, Immunology 75:143-149.
    • (1992) Immunology , vol.75 , pp. 143-149
    • Thor, G.1    Brian, A.A.2
  • 44
    • 0025055641 scopus 로고
    • Role of carbohydrate moiety of IL-5. Effect of tunicamycin on the glycosylation of IL-5 and the biologic activity of deglycosylated IL-5
    • Tominaga, A., Takahashi, T., Kikuchi, Y., Mita, S., Naomi, S., Harada, N., Yamaguchi, N., and Takatsu, K., 1990, Role of carbohydrate moiety of IL-5. Effect of tunicamycin on the glycosylation of IL-5 and the biologic activity of deglycosylated IL-5, J. Immunol. 144:1345-1352.
    • (1990) J. Immunol. , vol.144 , pp. 1345-1352
    • Tominaga, A.1    Takahashi, T.2    Kikuchi, Y.3    Mita, S.4    Naomi, S.5    Harada, N.6    Yamaguchi, N.7    Takatsu, K.8
  • 45
    • 0021837926 scopus 로고
    • Homogeneous interferon-inducing 22K factor is related to endogenous pyrogen and interleukin-1
    • Van Damme, J., De Ley, M., Opdenakker, G., Billiau, A., De Somer, P., and Van Beeumen, J., 1985, Homogeneous interferon-inducing 22K factor is related to endogenous pyrogen and interleukin-1, Nature 314:266-268.
    • (1985) Nature , vol.314 , pp. 266-268
    • Van Damme, J.1    De Ley, M.2    Opdenakker, G.3    Billiau, A.4    De Somer, P.5    Van Beeumen, J.6
  • 46
    • 0024467392 scopus 로고
    • Effects of N-glycosylation on in vitro activity of Bowes melanoma and human colon fibroblast derived tissue plasminogen activator
    • Wittwer, A.J., Howard, S.C., Carr, L.S., Harakas, N.K., Feder, J., Parekh, R.B., Rudd, P.M., Dwek, R.A., Rademacher, T.W., 1989, Effects of N-glycosylation on in vitro activity of Bowes melanoma and human colon fibroblast derived tissue plasminogen activator, Biochemistry 28:7662-7669.
    • (1989) Biochemistry , vol.28 , pp. 7662-7669
    • Wittwer, A.J.1    Howard, S.C.2    Carr, L.S.3    Harakas, N.K.4    Feder, J.5    Parekh, R.B.6    Rudd, P.M.7    Dwek, R.A.8    Rademacher, T.W.9
  • 47
    • 0027438684 scopus 로고
    • Glycosylation does not affect in vitro biological activity of interleukin-3
    • Ziltener, H.J., 1993, Glycosylation does not affect in vitro biological activity of interleukin-3, Cytokine 5:291-297.
    • (1993) Cytokine , vol.5 , pp. 291-297
    • Ziltener, H.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.