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Volumn 28, Issue 11, 2007, Pages 2137-2145

Interaction of antiflammin-1 with uteroglobin-binding protein induces phosphorylation of ERK1/2 in NIH 3T3 cells

Author keywords

Antiflammin 1; Extracellular signal regulated kinase; Uteroglobin; Uteroglobin binding protein

Indexed keywords

ANTIFLAMMIN; ANTIFLAMMIN 1; BINDING PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; UNCLASSIFIED DRUG; UTEROGLOBIN;

EID: 35348939009     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2007.08.027     Document Type: Article
Times cited : (2)

References (33)
  • 1
    • 0025823448 scopus 로고
    • ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
    • Boulton T.G., Nye S.H., Robbins D.J., Ip N.Y., Radziejewska E., Morgenbesser S.D., et al. ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Cell 65 (1991) 663-675
    • (1991) Cell , vol.65 , pp. 663-675
    • Boulton, T.G.1    Nye, S.H.2    Robbins, D.J.3    Ip, N.Y.4    Radziejewska, E.5    Morgenbesser, S.D.6
  • 3
    • 0034502494 scopus 로고    scopus 로고
    • Therapeutic applications of antiflammin peptides in experimental ocular inflammation
    • Chan C.C., Tuaillon N., Li Q., and Shen D.F. Therapeutic applications of antiflammin peptides in experimental ocular inflammation. Ann NY Acad Sci 923 (2000) 141-146
    • (2000) Ann NY Acad Sci , vol.923 , pp. 141-146
    • Chan, C.C.1    Tuaillon, N.2    Li, Q.3    Shen, D.F.4
  • 4
    • 0028926893 scopus 로고
    • Binding of uteroglobin to microsomes and plasmatic membranes
    • Diaz Gonzalez K., and Nieto A. Binding of uteroglobin to microsomes and plasmatic membranes. FEBS Lett 361 2-3 (1995) 255-258
    • (1995) FEBS Lett , vol.361 , Issue.2-3 , pp. 255-258
    • Diaz Gonzalez, K.1    Nieto, A.2
  • 5
    • 4444276797 scopus 로고    scopus 로고
    • Effect of uteroglobin on cPLA2, COX-2 expression and erk activation in nsclc cells
    • Kim W.J., Yoon J.M., Lee K.H., Han S.J., Shin W.H., Yim J.J., et al. Effect of uteroglobin on cPLA2, COX-2 expression and erk activation in nsclc cells. Tuberc Respir Dis 56 6 (2004) 638-645
    • (2004) Tuberc Respir Dis , vol.56 , Issue.6 , pp. 638-645
    • Kim, W.J.1    Yoon, J.M.2    Lee, K.H.3    Han, S.J.4    Shin, W.H.5    Yim, J.J.6
  • 7
    • 0032575644 scopus 로고    scopus 로고
    • Uteroglobin (UG) suppresses extracellular matrix invasion by normal and cancer cells that express the high affinity UG-binding proteins
    • Kundu G.C., Mandal A.K., Zhang Z., Mantile-Selvaggi G., and Mukherjee A.B. Uteroglobin (UG) suppresses extracellular matrix invasion by normal and cancer cells that express the high affinity UG-binding proteins. J Biol Chem 273 35 (1998) 22819-22824
    • (1998) J Biol Chem , vol.273 , Issue.35 , pp. 22819-22824
    • Kundu, G.C.1    Mandal, A.K.2    Zhang, Z.3    Mantile-Selvaggi, G.4    Mukherjee, A.B.5
  • 8
    • 0029865426 scopus 로고    scopus 로고
    • Recombinant human uteroglobin suppresses cellular invasiveness via a novel class of high-affinity cell surface binding site
    • Kundu G.C., Mantile G., Miele L., Cordella-Miele E., and Mukherjee A.B. Recombinant human uteroglobin suppresses cellular invasiveness via a novel class of high-affinity cell surface binding site. Proc Natl Acad Sci 93 (1996) 2915-2919
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 2915-2919
    • Kundu, G.C.1    Mantile, G.2    Miele, L.3    Cordella-Miele, E.4    Mukherjee, A.B.5
  • 9
    • 0031900740 scopus 로고    scopus 로고
    • Signal transduction through MAP kinase cascades
    • Lewis T.S., Shapiro P.S., and Ahn N.G. Signal transduction through MAP kinase cascades. Adv Cancer Res 74 (1998) 49-139
    • (1998) Adv Cancer Res , vol.74 , pp. 49-139
    • Lewis, T.S.1    Shapiro, P.S.2    Ahn, N.G.3
  • 10
    • 0029084436 scopus 로고
    • Effect of an anti-inflammatory peptide (antiflammin-1) on cell influx, eicosanoid biosynthesis, and edema formation by arachidonic acid and tetradecanoyl phorbol dermal application
    • Lloret S., and Moreno J.J. Effect of an anti-inflammatory peptide (antiflammin-1) on cell influx, eicosanoid biosynthesis, and edema formation by arachidonic acid and tetradecanoyl phorbol dermal application. Biochem Pharmacol 50 (1995) 347-353
    • (1995) Biochem Pharmacol , vol.50 , pp. 347-353
    • Lloret, S.1    Moreno, J.J.2
  • 11
    • 0026786327 scopus 로고
    • In vitro and in vivo effects of the anti-inflammatory peptides, antiflammins
    • Lloret S., and Moreno J.J. In vitro and in vivo effects of the anti-inflammatory peptides, antiflammins. Biochem Pharmacol 44 7 (1992) 1437-1441
    • (1992) Biochem Pharmacol , vol.44 , Issue.7 , pp. 1437-1441
    • Lloret, S.1    Moreno, J.J.2
  • 12
    • 0037093999 scopus 로고    scopus 로고
    • IFN-gamma-inducible protein 10 (CXCL10) contributes to airway hyperreactivity and airway inflammation in a mouse model of asthma
    • Medoff B.D., Sauty A., Tager A.M., Maclean J.A., Smith R.N., Mathew A., et al. IFN-gamma-inducible protein 10 (CXCL10) contributes to airway hyperreactivity and airway inflammation in a mouse model of asthma. J Immunol 168 10 (2002) 5278-5286
    • (2002) J Immunol , vol.168 , Issue.10 , pp. 5278-5286
    • Medoff, B.D.1    Sauty, A.2    Tager, A.M.3    Maclean, J.A.4    Smith, R.N.5    Mathew, A.6
  • 13
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I: the synthesis of a tetrapeptide
    • Merrifield R.B. Solid phase peptide synthesis. I: the synthesis of a tetrapeptide. J Am Chem Soc 85 (1963) 2149-2154
    • (1963) J Am Chem Soc , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 14
    • 0023683668 scopus 로고
    • Novel anti-inflammatory peptides from the region of highest similarity between uteroglobin and lipocortin I
    • Miele L., Cordella-Miele E., Facchiano A., and Mukherjee A.B. Novel anti-inflammatory peptides from the region of highest similarity between uteroglobin and lipocortin I. Nature 335 (1988) 726-730
    • (1988) Nature , vol.335 , pp. 726-730
    • Miele, L.1    Cordella-Miele, E.2    Facchiano, A.3    Mukherjee, A.B.4
  • 15
    • 0034501374 scopus 로고    scopus 로고
    • Antiflammin peptides in the regulation of inflammatory response
    • Moreno J.J. Antiflammin peptides in the regulation of inflammatory response. Ann NY Acad Sci 923 (2000) 147-153
    • (2000) Ann NY Acad Sci , vol.923 , pp. 147-153
    • Moreno, J.J.1
  • 17
    • 0020692464 scopus 로고
    • Suppression of epididymal sperm antigenicity in the rabbit by uteroglobin and transglutaminase in vitro
    • Mukherjee D.C., Agrawal A.K., Manjunath R., and Mukherjee A.B. Suppression of epididymal sperm antigenicity in the rabbit by uteroglobin and transglutaminase in vitro. Science 219 4587 (1983) 989-991
    • (1983) Science , vol.219 , Issue.4587 , pp. 989-991
    • Mukherjee, D.C.1    Agrawal, A.K.2    Manjunath, R.3    Mukherjee, A.B.4
  • 19
    • 0642334379 scopus 로고    scopus 로고
    • Multiple mechanisms for oxygen-induced regulation of the Clara cell secretory protein gene
    • Ramsay P.L., Luo Z., Major A., Park M.S., Finegold M., Welty S.E., et al. Multiple mechanisms for oxygen-induced regulation of the Clara cell secretory protein gene. FASEB J 17 14 (2003) 2142-2144
    • (2003) FASEB J , vol.17 , Issue.14 , pp. 2142-2144
    • Ramsay, P.L.1    Luo, Z.2    Major, A.3    Park, M.S.4    Finegold, M.5    Welty, S.E.6
  • 20
    • 33750993188 scopus 로고    scopus 로고
    • 2 differentiation by down-regulating the expression of serum amyloid A and SOCS-3 genes
    • 2 differentiation by down-regulating the expression of serum amyloid A and SOCS-3 genes. FEBS Lett 580 25 (2006) 6022-6026
    • (2006) FEBS Lett , vol.580 , Issue.25 , pp. 6022-6026
    • Ray, R.1    Zhang, Z.2    Lee, Y.C.3    Gao, J.L.4    Mukherjee, A.B.5
  • 21
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions
    • Roux P.P., and Blenis J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol Mol Biol Rev 68 2 (2004) 320-344
    • (2004) Microbiol Mol Biol Rev , vol.68 , Issue.2 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 22
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signaling on the surface of living cells
    • Sako Y., Minoghchi S., and Yanagida T. Single-molecule imaging of EGFR signaling on the surface of living cells. Nat Cell Biol 2 3 (2000) 168-172
    • (2000) Nat Cell Biol , vol.2 , Issue.3 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 23
    • 0024380087 scopus 로고
    • Rapid detection of octamer-binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E., Matthias P., Muller M.M., and Schaffner W. Rapid detection of octamer-binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res 17 15 (1989) 6419
    • (1989) Nucleic Acids Res , vol.17 , Issue.15 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 24
    • 0037269113 scopus 로고    scopus 로고
    • Clinical aspects of Clara cell 10 kDa protein/uteroglobin (secretoglobin 1A1)
    • Review
    • Shijubo N., Kawabata I., Sato N., and Itoh Y. Clinical aspects of Clara cell 10 kDa protein/uteroglobin (secretoglobin 1A1). Curr Pharm Des 9 14 (2003) 1139-1149 Review
    • (2003) Curr Pharm Des , vol.9 , Issue.14 , pp. 1139-1149
    • Shijubo, N.1    Kawabata, I.2    Sato, N.3    Itoh, Y.4
  • 27
    • 0035477153 scopus 로고    scopus 로고
    • Validation of flow cytometric competitive binding protocols and characterization of fluorescently labeled ligands
    • Waller A., Pipkorn D., Sutton K.L., Linderman J.J., and Omann G.M. Validation of flow cytometric competitive binding protocols and characterization of fluorescently labeled ligands. Cytometry 45 2 (2001) 102-114
    • (2001) Cytometry , vol.45 , Issue.2 , pp. 102-114
    • Waller, A.1    Pipkorn, D.2    Sutton, K.L.3    Linderman, J.J.4    Omann, G.M.5
  • 28
    • 0038521291 scopus 로고    scopus 로고
    • Antisense down-regulation of lipocalin-interacting membrane receptor expression inhibits cellular internalization of lipocalin-1 in human NT2 cells
    • Wojnar P., Lechner M., and Redl B. Antisense down-regulation of lipocalin-interacting membrane receptor expression inhibits cellular internalization of lipocalin-1 in human NT2 cells. J Biol Chem 278 18 (2003) 16209-16215
    • (2003) J Biol Chem , vol.278 , Issue.18 , pp. 16209-16215
    • Wojnar, P.1    Lechner, M.2    Redl B3
  • 29
    • 3142707507 scopus 로고    scopus 로고
    • Increased susceptibility of mice lacking Clara cell 10 kDa protein to lung tumorigenesis by 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, a potent carcinogen in cigarette smoke
    • Yang Y., Zhang Z., Mukherjee A.B., and Linnoila R.I. Increased susceptibility of mice lacking Clara cell 10 kDa protein to lung tumorigenesis by 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, a potent carcinogen in cigarette smoke. J Biol Chem 279 28 (2004) 29336-29340
    • (2004) J Biol Chem , vol.279 , Issue.28 , pp. 29336-29340
    • Yang, Y.1    Zhang, Z.2    Mukherjee, A.B.3    Linnoila, R.I.4
  • 30
    • 0035845503 scopus 로고    scopus 로고
    • Single-cell analysis of signal transduction in CD4 T cells stimulated by antigen in vivo
    • Zell T., Khoruts A., Ingulli E., Bonnevier J.L., Mueller D.L., and Jenkins M.K. Single-cell analysis of signal transduction in CD4 T cells stimulated by antigen in vivo. Proc Natl Acad Sci 98 19 (2001) 10805-10810
    • (2001) Proc Natl Acad Sci , vol.98 , Issue.19 , pp. 10805-10810
    • Zell, T.1    Khoruts, A.2    Ingulli, E.3    Bonnevier, J.L.4    Mueller, D.L.5    Jenkins, M.K.6
  • 31
    • 33644641965 scopus 로고    scopus 로고
    • Interaction of uteroglobin with lipocalin-1 receptor suppresses cancer cell motility and invasion
    • Zhang Z., Kim S.J., Chowdhury B., Wang J., Lee Y.C., Tsai P.C., et al. Interaction of uteroglobin with lipocalin-1 receptor suppresses cancer cell motility and invasion. Gene 369 (2006) 66-71
    • (2006) Gene , vol.369 , pp. 66-71
    • Zhang, Z.1    Kim, S.J.2    Chowdhury, B.3    Wang, J.4    Lee, Y.C.5    Tsai, P.C.6
  • 32
    • 0033616673 scopus 로고    scopus 로고
    • Loss of transformed phenotype in cancer cells by overexpression of the uteroglobin gene
    • Zhang Z., Kundu G.C., Panda D., Mandal A.K., Mantile-Selvaggi G., Peri A., et al. Loss of transformed phenotype in cancer cells by overexpression of the uteroglobin gene. Proc Natl Acad Sci 96 7 (1999) 3963-3968
    • (1999) Proc Natl Acad Sci , vol.96 , Issue.7 , pp. 3963-3968
    • Zhang, Z.1    Kundu, G.C.2    Panda, D.3    Mandal, A.K.4    Mantile-Selvaggi, G.5    Peri, A.6
  • 33
    • 0034106834 scopus 로고    scopus 로고
    • The anti-inflammatory peptides, antiflammins, regulate the expression of adhesion molecules on human leukocytes and prevent neutrophil adhesion to endothelial cells
    • Zouki C., Ouellet S., and Filep J.G. The anti-inflammatory peptides, antiflammins, regulate the expression of adhesion molecules on human leukocytes and prevent neutrophil adhesion to endothelial cells. FASEB J 14 (2000) 572-580
    • (2000) FASEB J , vol.14 , pp. 572-580
    • Zouki, C.1    Ouellet, S.2    Filep, J.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.