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Volumn 17, Issue 5, 2006, Pages 367-380

Interleukin-22: A novel T- and NK-cell derived cytokine that regulates the biology of tissue cells

Author keywords

CRF2; Cytokine receptors; Cytokines; IL 10 family; IL 22 binding protein

Indexed keywords

BINDING PROTEIN; CYTOKINE; INTERLEUKIN 22; INTERLEUKIN 22 BINDING PROTEIN; INTERLEUKIN 22 RECEPTOR; INTERLEUKIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 33749983749     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2006.09.001     Document Type: Review
Times cited : (262)

References (62)
  • 1
    • 0034651583 scopus 로고    scopus 로고
    • Cloning and characterization of IL-10-related T cell-derived inducible factor (IL-TIF), a novel cytokine structurally related to IL-10 and inducible by IL-9
    • Dumoutier L., Louahed J., and Renauld J.C. Cloning and characterization of IL-10-related T cell-derived inducible factor (IL-TIF), a novel cytokine structurally related to IL-10 and inducible by IL-9. J Immunol 164 (2000) 1814-1819
    • (2000) J Immunol , vol.164 , pp. 1814-1819
    • Dumoutier, L.1    Louahed, J.2    Renauld, J.C.3
  • 2
    • 0034730141 scopus 로고    scopus 로고
    • Human interleukin-10-related T cell-derived inducible factor: molecular cloning and functional characterization as an hepatocyte-stimulating factor
    • Dumoutier L., Van Roost E., Colau D., and Renauld J.C. Human interleukin-10-related T cell-derived inducible factor: molecular cloning and functional characterization as an hepatocyte-stimulating factor. Proc Natl Acad Sci USA 97 (2000) 10144-10149
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10144-10149
    • Dumoutier, L.1    Van Roost, E.2    Colau, D.3    Renauld, J.C.4
  • 3
    • 0034613201 scopus 로고    scopus 로고
    • Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R
    • Xie M.H., Aggarwal S., Ho W.H., et al. Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R. J Biol Chem 275 (2000) 31335-31339
    • (2000) J Biol Chem , vol.275 , pp. 31335-31339
    • Xie, M.H.1    Aggarwal, S.2    Ho, W.H.3
  • 4
    • 17744373448 scopus 로고    scopus 로고
    • Interleukin 20: discovery, receptor identification, and role in epidermal function
    • Blumberg H., Conklin D., Xu W.F., et al. Interleukin 20: discovery, receptor identification, and role in epidermal function. Cell 104 (2001) 9-19
    • (2001) Cell , vol.104 , pp. 9-19
    • Blumberg, H.1    Conklin, D.2    Xu, W.F.3
  • 5
    • 0034303102 scopus 로고    scopus 로고
    • Cloning, expression and initial characterization of interleukin-19 (IL-19), a novel homologue of human interleukin-10 (IL-10)
    • Gallagher G., Dickensheets H., Eskdale J., et al. Cloning, expression and initial characterization of interleukin-19 (IL-19), a novel homologue of human interleukin-10 (IL-10). Genes Immun 1 (2000) 442-450
    • (2000) Genes Immun , vol.1 , pp. 442-450
    • Gallagher, G.1    Dickensheets, H.2    Eskdale, J.3
  • 6
    • 0342803595 scopus 로고    scopus 로고
    • Induction of a novel cellular homolog of interleukin-10, AK155, by transformation of T lymphocytes with herpesvirus saimiri
    • Knappe A., Hor S., Wittmann S., and Fickenscher H. Induction of a novel cellular homolog of interleukin-10, AK155, by transformation of T lymphocytes with herpesvirus saimiri. J Virol 74 (2000) 3881-3887
    • (2000) J Virol , vol.74 , pp. 3881-3887
    • Knappe, A.1    Hor, S.2    Wittmann, S.3    Fickenscher, H.4
  • 7
    • 0029558740 scopus 로고
    • Subtraction hybridization identifies a novel melanoma differentiation associated gene, mda-7, modulated during human melanoma differentiation, growth and progression
    • Jiang H., Lin J.J., Su Z.Z., Goldstein N.I., and Fisher P.B. Subtraction hybridization identifies a novel melanoma differentiation associated gene, mda-7, modulated during human melanoma differentiation, growth and progression. Oncogene 11 (1995) 2477-2486
    • (1995) Oncogene , vol.11 , pp. 2477-2486
    • Jiang, H.1    Lin, J.J.2    Su, Z.Z.3    Goldstein, N.I.4    Fisher, P.B.5
  • 8
    • 0035424124 scopus 로고    scopus 로고
    • IL-10 and its homologs: important immune mediators and emerging immunotherapeutic targets
    • Volk H., Asadullah K., Gallagher G., Sabat R., and Grutz G. IL-10 and its homologs: important immune mediators and emerging immunotherapeutic targets. Trends Immunol 22 (2001) 414-417
    • (2001) Trends Immunol , vol.22 , pp. 414-417
    • Volk, H.1    Asadullah, K.2    Gallagher, G.3    Sabat, R.4    Grutz, G.5
  • 9
    • 0037243222 scopus 로고    scopus 로고
    • IFN-lambdas mediate antiviral protection through a distinct class II cytokine receptor complex
    • Kotenko S.V., Gallagher G., Baurin V.V., et al. IFN-lambdas mediate antiviral protection through a distinct class II cytokine receptor complex. Nat Immunol 4 (2003) 69-77
    • (2003) Nat Immunol , vol.4 , pp. 69-77
    • Kotenko, S.V.1    Gallagher, G.2    Baurin, V.V.3
  • 10
    • 0037236826 scopus 로고    scopus 로고
    • IL-28, IL-29 and their class II cytokine receptor IL-28R
    • Sheppard P., Kindsvogel W., Xu W., et al. IL-28, IL-29 and their class II cytokine receptor IL-28R. Nat Immunol 4 (2003) 63-68
    • (2003) Nat Immunol , vol.4 , pp. 63-68
    • Sheppard, P.1    Kindsvogel, W.2    Xu, W.3
  • 11
    • 3442888513 scopus 로고    scopus 로고
    • The expanded family of class II cytokines that share the IL-10 receptor-2 (IL-10R2) chain
    • Donnelly R.P., Sheikh F., Kotenko S.V., and Dickensheets H. The expanded family of class II cytokines that share the IL-10 receptor-2 (IL-10R2) chain. J Leukoc Biol 76 (2004) 314-321
    • (2004) J Leukoc Biol , vol.76 , pp. 314-321
    • Donnelly, R.P.1    Sheikh, F.2    Kotenko, S.V.3    Dickensheets, H.4
  • 12
    • 1642432084 scopus 로고    scopus 로고
    • The Class II cytokine receptor (CRF2) family: overview and patterns of receptor-ligand interactions
    • Langer J.A., Cutrone E.C., and Kotenko S. The Class II cytokine receptor (CRF2) family: overview and patterns of receptor-ligand interactions. Cytokine Growth Factor Rev 15 (2004) 33-48
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 33-48
    • Langer, J.A.1    Cutrone, E.C.2    Kotenko, S.3
  • 15
    • 0033166966 scopus 로고    scopus 로고
    • Evidence for conformationally different states of interleukin-10: binding of a neutralizing antibody enhances accessibility of a hidden epitope
    • Reineke U., Schneider-Mergener J., Glaser R.W., et al. Evidence for conformationally different states of interleukin-10: binding of a neutralizing antibody enhances accessibility of a hidden epitope. J Mol Recognit 12 (1999) 242-248
    • (1999) J Mol Recognit , vol.12 , pp. 242-248
    • Reineke, U.1    Schneider-Mergener, J.2    Glaser, R.W.3
  • 16
    • 0034565220 scopus 로고    scopus 로고
    • IL-TIF/IL-22: genomic organization and mapping of the human and mouse genes
    • Dumoutier L., Van Roost E., Ameye G., Michaux L., and Renauld J.C. IL-TIF/IL-22: genomic organization and mapping of the human and mouse genes. Genes Immun 1 (2000) 488-494
    • (2000) Genes Immun , vol.1 , pp. 488-494
    • Dumoutier, L.1    Van Roost, E.2    Ameye, G.3    Michaux, L.4    Renauld, J.C.5
  • 17
    • 0035992506 scopus 로고    scopus 로고
    • The family of IL-10-related cytokines and their receptors: related, but to what extent?
    • Kotenko S.V. The family of IL-10-related cytokines and their receptors: related, but to what extent?. Cytokine Growth Factor Rev 13 (2002) 223-240
    • (2002) Cytokine Growth Factor Rev , vol.13 , pp. 223-240
    • Kotenko, S.V.1
  • 20
    • 0037474286 scopus 로고    scopus 로고
    • Crystal structure of interleukin-19 defines a new subfamily of helical cytokines
    • Chang C., Magracheva E., Kozlov S., et al. Crystal structure of interleukin-19 defines a new subfamily of helical cytokines. J Biol Chem 278 (2003) 3308-3313
    • (2003) J Biol Chem , vol.278 , pp. 3308-3313
    • Chang, C.1    Magracheva, E.2    Kozlov, S.3
  • 21
    • 0029148581 scopus 로고
    • Crystal structure of interleukin 10 reveals an interferon gamma-like fold
    • Walter M.R., and Nagabhushan T.L. Crystal structure of interleukin 10 reveals an interferon gamma-like fold. Biochemistry 34 (1995) 12118-12125
    • (1995) Biochemistry , vol.34 , pp. 12118-12125
    • Walter, M.R.1    Nagabhushan, T.L.2
  • 22
    • 0029644946 scopus 로고
    • Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma
    • Zdanov A., Schalk-Hihi C., Gustchina A., Tsang M., Weatherbee J., and Wlodawer A. Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma. Structure 3 (1995) 591-601
    • (1995) Structure , vol.3 , pp. 591-601
    • Zdanov, A.1    Schalk-Hihi, C.2    Gustchina, A.3    Tsang, M.4    Weatherbee, J.5    Wlodawer, A.6
  • 23
    • 0035951795 scopus 로고    scopus 로고
    • Identification of the functional interleukin-22 (IL-22) receptor complex: the IL-10R2 chain (IL-10Rbeta) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes
    • Kotenko S.V., Izotova L.S., Mirochnitchenko O.V., et al. Identification of the functional interleukin-22 (IL-22) receptor complex: the IL-10R2 chain (IL-10Rbeta) is a common chain of both the IL-10 and IL-22 (IL-10-related T cell-derived inducible factor, IL-TIF) receptor complexes. J Biol Chem 276 (2001) 2725-2732
    • (2001) J Biol Chem , vol.276 , pp. 2725-2732
    • Kotenko, S.V.1    Izotova, L.S.2    Mirochnitchenko, O.V.3
  • 24
    • 4344581122 scopus 로고    scopus 로고
    • The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation
    • Logsdon N.J., Jones B.C., Allman J.C., et al. The IL-10R2 binding hot spot on IL-22 is located on the N-terminal helix and is dependent on N-linked glycosylation. J Mol Biol 342 (2004) 503-514
    • (2004) J Mol Biol , vol.342 , pp. 503-514
    • Logsdon, N.J.1    Jones, B.C.2    Allman, J.C.3
  • 25
    • 0036604122 scopus 로고    scopus 로고
    • Cutting edge: immune cells as sources and targets of the IL-10 family members?
    • Wolk K., Kunz S., Asadullah K., and Sabat R. Cutting edge: immune cells as sources and targets of the IL-10 family members?. J Immunol 168 (2002) 5397-5402
    • (2002) J Immunol , vol.168 , pp. 5397-5402
    • Wolk, K.1    Kunz, S.2    Asadullah, K.3    Sabat, R.4
  • 27
    • 33646552450 scopus 로고    scopus 로고
    • IL-22 regulates the expression of genes responsible for antimicrobial defense, cellular differentiation, and mobility in keratinocytes: a potential role in psoriasis
    • Wolk K., Witte E., Wallace E., et al. IL-22 regulates the expression of genes responsible for antimicrobial defense, cellular differentiation, and mobility in keratinocytes: a potential role in psoriasis. Eur J Immunol 36 (2006) 1309-1323
    • (2006) Eur J Immunol , vol.36 , pp. 1309-1323
    • Wolk, K.1    Witte, E.2    Wallace, E.3
  • 28
    • 13844306351 scopus 로고    scopus 로고
    • Is there an interaction between interleukin-10 and interleukin-22?
    • Wolk K., Witte E., Reineke U., et al. Is there an interaction between interleukin-10 and interleukin-22?. Genes Immun 6 (2005) 8-18
    • (2005) Genes Immun , vol.6 , pp. 8-18
    • Wolk, K.1    Witte, E.2    Reineke, U.3
  • 29
    • 0037431756 scopus 로고    scopus 로고
    • Atopic dermatitis
    • Leung D.Y., and Bieber T. Atopic dermatitis. Lancet 361 (2003) 151-160
    • (2003) Lancet , vol.361 , pp. 151-160
    • Leung, D.Y.1    Bieber, T.2
  • 30
    • 24144477540 scopus 로고    scopus 로고
    • Interleukin-22, a member of the IL-10 subfamily, induces inflammatory responses in colonic subepithelial myofibroblasts
    • Andoh A., Zhang Z., Inatomi O., et al. Interleukin-22, a member of the IL-10 subfamily, induces inflammatory responses in colonic subepithelial myofibroblasts. Gastroenterology 129 (2005) 969-984
    • (2005) Gastroenterology , vol.129 , pp. 969-984
    • Andoh, A.1    Zhang, Z.2    Inatomi, O.3
  • 31
    • 17244381180 scopus 로고    scopus 로고
    • Expression of interleukin-22 in rheumatoid arthritis: potential role as a proinflammatory cytokine
    • Ikeuchi H., Kuroiwa T., Hiramatsu N., et al. Expression of interleukin-22 in rheumatoid arthritis: potential role as a proinflammatory cytokine. Arthritis Rheum 52 (2005) 1037-1046
    • (2005) Arthritis Rheum , vol.52 , pp. 1037-1046
    • Ikeuchi, H.1    Kuroiwa, T.2    Hiramatsu, N.3
  • 33
    • 0030799157 scopus 로고    scopus 로고
    • Identification and functional characterization of a second chain of the interleukin-10 receptor complex
    • Kotenko S.V., Krause C.D., Izotova L.S., Pollack B.P., Wu W., and Pestka S. Identification and functional characterization of a second chain of the interleukin-10 receptor complex. EMBO J 16 (1997) 5894-5903
    • (1997) EMBO J , vol.16 , pp. 5894-5903
    • Kotenko, S.V.1    Krause, C.D.2    Izotova, L.S.3    Pollack, B.P.4    Wu, W.5    Pestka, S.6
  • 34
    • 33750018619 scopus 로고    scopus 로고
    • Adams RL, Farrah TM, Jelmberg AC, Lok S, Whitemore TE, Patent WO9907848-A1 and U.S. Patent 5,965,704; 1999.
  • 35
    • 0642278521 scopus 로고    scopus 로고
    • Genomic structure and inducible expression of the IL-22 receptor alpha chain in mice
    • Tachiiri A., Imamura R., Wang Y., Fukui M., Umemura M., and Suda T. Genomic structure and inducible expression of the IL-22 receptor alpha chain in mice. Genes Immun 4 (2003) 153-159
    • (2003) Genes Immun , vol.4 , pp. 153-159
    • Tachiiri, A.1    Imamura, R.2    Wang, Y.3    Fukui, M.4    Umemura, M.5    Suda, T.6
  • 36
    • 11144354300 scopus 로고    scopus 로고
    • Temporal associations between interleukin 22 and the extracellular domains of IL-22R and IL-10R2
    • Li J., Tomkinson K.N., Tan X.Y., et al. Temporal associations between interleukin 22 and the extracellular domains of IL-22R and IL-10R2. Int Immunopharmacol 4 (2004) 693-708
    • (2004) Int Immunopharmacol , vol.4 , pp. 693-708
    • Li, J.1    Tomkinson, K.N.2    Tan, X.Y.3
  • 37
    • 0034897552 scopus 로고    scopus 로고
    • Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site
    • Josephson K., Logsdon N.J., and Walter M.R. Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site. Immunity 15 (2001) 35-46
    • (2001) Immunity , vol.15 , pp. 35-46
    • Josephson, K.1    Logsdon, N.J.2    Walter, M.R.3
  • 38
    • 0031955920 scopus 로고    scopus 로고
    • Mapping of the interleukin-10/interleukin-10 receptor combining site
    • Reineke U., Sabat R., Volk H.D., and Schneider-Mergener J. Mapping of the interleukin-10/interleukin-10 receptor combining site. Protein Sci 7 (1998) 951-960
    • (1998) Protein Sci , vol.7 , pp. 951-960
    • Reineke, U.1    Sabat, R.2    Volk, H.D.3    Schneider-Mergener, J.4
  • 39
    • 14844342604 scopus 로고    scopus 로고
    • IL-22 inhibits epidermal differentiation and induces proinflammatory gene expression and migration of human keratinocytes
    • Boniface K., Bernard F.X., Garcia M., Gurney A.L., Lecron J.C., and Morel F. IL-22 inhibits epidermal differentiation and induces proinflammatory gene expression and migration of human keratinocytes. J Immunol 174 (2005) 3695-3702
    • (2005) J Immunol , vol.174 , pp. 3695-3702
    • Boniface, K.1    Bernard, F.X.2    Garcia, M.3    Gurney, A.L.4    Lecron, J.C.5    Morel, F.6
  • 40
    • 1842841846 scopus 로고    scopus 로고
    • IL-22, in contrast to IL-10, does not induce Ig production, due to absence of a functional IL-22 receptor on activated human B cells
    • Lecart S., Morel F., Noraz N., et al. IL-22, in contrast to IL-10, does not induce Ig production, due to absence of a functional IL-22 receptor on activated human B cells. Int Immunol 14 (2002) 1351-1356
    • (2002) Int Immunol , vol.14 , pp. 1351-1356
    • Lecart, S.1    Morel, F.2    Noraz, N.3
  • 42
    • 0037033092 scopus 로고    scopus 로고
    • Interleukins 19, 20, and 24 signal through two distinct receptor complexes. Differences in receptor-ligand interactions mediate unique biological functions
    • Parrish-Novak J., Xu W., Brender T., et al. Interleukins 19, 20, and 24 signal through two distinct receptor complexes. Differences in receptor-ligand interactions mediate unique biological functions. J Biol Chem 277 (2002) 47517-47523
    • (2002) J Biol Chem , vol.277 , pp. 47517-47523
    • Parrish-Novak, J.1    Xu, W.2    Brender, T.3
  • 43
    • 0035877222 scopus 로고    scopus 로고
    • Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22
    • Dumoutier L., Lejeune D., Colau D., and Renauld J.C. Cloning and characterization of IL-22 binding protein, a natural antagonist of IL-10-related T cell-derived inducible factor/IL-22. J Immunol 166 (2001) 7090-7095
    • (2001) J Immunol , vol.166 , pp. 7090-7095
    • Dumoutier, L.1    Lejeune, D.2    Colau, D.3    Renauld, J.C.4
  • 44
    • 0035487081 scopus 로고    scopus 로고
    • A novel, soluble homologue of the human IL-10 receptor with preferential expression in placenta
    • Gruenberg B.H., Schoenemeyer A., Weiss B., et al. A novel, soluble homologue of the human IL-10 receptor with preferential expression in placenta. Genes Immun 2 (2001) 329-334
    • (2001) Genes Immun , vol.2 , pp. 329-334
    • Gruenberg, B.H.1    Schoenemeyer, A.2    Weiss, B.3
  • 45
    • 0035877120 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of a novel soluble receptor that binds IL-22 and neutralizes its activity
    • Kotenko S.V., Izotova L.S., Mirochnitchenko O.V., et al. Identification, cloning, and characterization of a novel soluble receptor that binds IL-22 and neutralizes its activity. J Immunol 166 (2001) 7096-7103
    • (2001) J Immunol , vol.166 , pp. 7096-7103
    • Kotenko, S.V.1    Izotova, L.S.2    Mirochnitchenko, O.V.3
  • 46
    • 0242473337 scopus 로고    scopus 로고
    • Cloning and characterization of mouse IL-22 binding protein
    • Wei C.C., Ho T.W., Liang W.G., Chen G.Y., and Chang M.S. Cloning and characterization of mouse IL-22 binding protein. Genes Immun 4 (2003) 204-211
    • (2003) Genes Immun , vol.4 , pp. 204-211
    • Wei, C.C.1    Ho, T.W.2    Liang, W.G.3    Chen, G.Y.4    Chang, M.S.5
  • 47
    • 4344584114 scopus 로고    scopus 로고
    • Cloning of murine IL-22 receptor alpha 2 and comparison with its human counterpart
    • Weiss B., Wolk K., Grunberg B.H., et al. Cloning of murine IL-22 receptor alpha 2 and comparison with its human counterpart. Genes Immun 5 (2004) 330-336
    • (2004) Genes Immun , vol.5 , pp. 330-336
    • Weiss, B.1    Wolk, K.2    Grunberg, B.H.3
  • 48
    • 0035859898 scopus 로고    scopus 로고
    • A soluble class II cytokine receptor, IL-22RA2, is a naturally occurring IL-22 antagonist
    • Xu W., Presnell S.R., Parrish-Novak J., et al. A soluble class II cytokine receptor, IL-22RA2, is a naturally occurring IL-22 antagonist. Proc Natl Acad Sci USA 98 (2001) 9511-9516
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9511-9516
    • Xu, W.1    Presnell, S.R.2    Parrish-Novak, J.3
  • 49
    • 0035478639 scopus 로고    scopus 로고
    • Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor complexes of two types
    • Dumoutier L., Leemans C., Lejeune D., Kotenko S.V., and Renauld J.C. Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor complexes of two types. J Immunol 167 (2001) 3545-3549
    • (2001) J Immunol , vol.167 , pp. 3545-3549
    • Dumoutier, L.1    Leemans, C.2    Lejeune, D.3    Kotenko, S.V.4    Renauld, J.C.5
  • 50
    • 0037072796 scopus 로고    scopus 로고
    • Interleukin-22 (IL-22) activates the JAK/STAT, ERK, JNK, and p38 MAP kinase pathways in a rat hepatoma cell line. Pathways that are shared with and distinct from IL-10
    • Lejeune D., Dumoutier L., Constantinescu S., Kruijer W., Schuringa J.J., and Renauld J.C. Interleukin-22 (IL-22) activates the JAK/STAT, ERK, JNK, and p38 MAP kinase pathways in a rat hepatoma cell line. Pathways that are shared with and distinct from IL-10. J Biol Chem 277 (2002) 33676-33682
    • (2002) J Biol Chem , vol.277 , pp. 33676-33682
    • Lejeune, D.1    Dumoutier, L.2    Constantinescu, S.3    Kruijer, W.4    Schuringa, J.J.5    Renauld, J.C.6
  • 51
    • 32944473854 scopus 로고    scopus 로고
    • Regulation of T cells and cytokines by the interleukin-10 (IL-10)-family cytokines IL-19, IL-20, IL-22, IL-24 and IL-26
    • Oral H.B., Kotenko S.V., Yilmaz M., et al. Regulation of T cells and cytokines by the interleukin-10 (IL-10)-family cytokines IL-19, IL-20, IL-22, IL-24 and IL-26. Eur J Immunol 36 (2006) 380-388
    • (2006) Eur J Immunol , vol.36 , pp. 380-388
    • Oral, H.B.1    Kotenko, S.V.2    Yilmaz, M.3
  • 52
    • 0035791743 scopus 로고    scopus 로고
    • Serum amyloid A and high-density lipoprotein cholesterol: serum markers of inflammation in sarcoidosis and other systemic disorders
    • Salazar A., Pinto X., and Mana J. Serum amyloid A and high-density lipoprotein cholesterol: serum markers of inflammation in sarcoidosis and other systemic disorders. Eur J Clin Invest 31 (2001) 1070-1077
    • (2001) Eur J Clin Invest , vol.31 , pp. 1070-1077
    • Salazar, A.1    Pinto, X.2    Mana, J.3
  • 53
    • 2342462460 scopus 로고    scopus 로고
    • Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation
    • Radaeva S., Sun R., Pan H.N., Hong F., and Gao B. Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation. Hepatology 39 (2004) 1332-1342
    • (2004) Hepatology , vol.39 , pp. 1332-1342
    • Radaeva, S.1    Sun, R.2    Pan, H.N.3    Hong, F.4    Gao, B.5
  • 54
    • 2342458559 scopus 로고    scopus 로고
    • Hydrodynamic gene delivery of interleukin-22 protects the mouse liver from concanavalin A-, carbon tetrachloride-, and Fas ligand-induced injury via activation of STAT3
    • Pan H., Hong F., Radaeva S., and Gao B. Hydrodynamic gene delivery of interleukin-22 protects the mouse liver from concanavalin A-, carbon tetrachloride-, and Fas ligand-induced injury via activation of STAT3. Cell Mol Immunol 1 (2004) 43-49
    • (2004) Cell Mol Immunol , vol.1 , pp. 43-49
    • Pan, H.1    Hong, F.2    Radaeva, S.3    Gao, B.4
  • 55
    • 33645051715 scopus 로고    scopus 로고
    • Antimicrobial skin peptides and proteins
    • Schroder J.M., and Harder J. Antimicrobial skin peptides and proteins. Cell Mol Life Sci 63 (2006) 469-486
    • (2006) Cell Mol Life Sci , vol.63 , pp. 469-486
    • Schroder, J.M.1    Harder, J.2
  • 57
    • 14944365560 scopus 로고    scopus 로고
    • Therapeutic potential of follistatin for colonic inflammation in mice
    • Dohi T., Ejima C., Kato R., et al. Therapeutic potential of follistatin for colonic inflammation in mice. Gastroenterology 128 (2005) 411-423
    • (2005) Gastroenterology , vol.128 , pp. 411-423
    • Dohi, T.1    Ejima, C.2    Kato, R.3
  • 58
    • 0343145719 scopus 로고    scopus 로고
    • Activin A: a novel player and inflammatory marker in inflammatory bowel disease?
    • Hubner G., Brauchle M., Gregor M., and Werner S. Activin A: a novel player and inflammatory marker in inflammatory bowel disease?. Lab Invest 77 (1997) 311-318
    • (1997) Lab Invest , vol.77 , pp. 311-318
    • Hubner, G.1    Brauchle, M.2    Gregor, M.3    Werner, S.4
  • 60
    • 0032188840 scopus 로고    scopus 로고
    • Growth factors and the gastrointestinal tract
    • Murphy M.S. Growth factors and the gastrointestinal tract. Nutrition 14 (1998) 771-774
    • (1998) Nutrition , vol.14 , pp. 771-774
    • Murphy, M.S.1
  • 61
    • 0038718739 scopus 로고    scopus 로고
    • Stimulation of human colonic epithelial cells by leukemia inhibitory factor is dependent on collagen-embedded fibroblasts in organotypic culture
    • Kalabis J., Patterson M.J., Enders G.H., et al. Stimulation of human colonic epithelial cells by leukemia inhibitory factor is dependent on collagen-embedded fibroblasts in organotypic culture. FASEB J 17 (2003) 1115-1117
    • (2003) FASEB J , vol.17 , pp. 1115-1117
    • Kalabis, J.1    Patterson, M.J.2    Enders, G.H.3
  • 62
    • 8444223078 scopus 로고    scopus 로고
    • Expression of interleukin-22 in murine carcinoma cells did not influence tumour growth in vivo but did improve survival of the inoculated hosts
    • Nagakawa H., Shimozato O., Yu L., et al. Expression of interleukin-22 in murine carcinoma cells did not influence tumour growth in vivo but did improve survival of the inoculated hosts. Scand J Immunol 60 (2004) 449-454
    • (2004) Scand J Immunol , vol.60 , pp. 449-454
    • Nagakawa, H.1    Shimozato, O.2    Yu, L.3


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