메뉴 건너뛰기




Volumn 169, Issue 1, 2011, Pages

Peptide inhibitors of MK2 show promise for inhibition of abdominal adhesions

Author keywords

abdominal adhesion; IL 1 ; IL 6; MAPKAP Kinase 2; MK2; TNF

Indexed keywords

HYDROXYPROLINE; INTERLEUKIN 1BETA; INTERLEUKIN 6; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MMI 0100; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 79958239562     PISSN: 00224804     EISSN: 10958673     Source Type: Journal    
DOI: 10.1016/j.jss.2011.01.043     Document Type: Article
Times cited : (30)

References (69)
  • 1
    • 0031052907 scopus 로고    scopus 로고
    • The clinical significance of adhesions: Focus on intestinal obstruction
    • H. Ellis The clinical significance of adhesions: Focus on intestinal obstruction Eur J Surg Suppl 577 1997 5
    • (1997) Eur J Surg Suppl , vol.577 , pp. 5
    • Ellis, H.1
  • 2
    • 79958195932 scopus 로고    scopus 로고
    • Frost and Sullivan. U.S. Markets for jemostats, tissue sealants, tissue adhesives, and adhesion prevention products. December Available at
    • Frost and Sullivan. U.S. Markets for jemostats, tissue sealants, tissue adhesives, and adhesion prevention products. December 2004. Available at: http://www.frost.com/prod/servlet/frost-home.pag.
    • (2004)
  • 3
    • 0031915792 scopus 로고    scopus 로고
    • Abdominal adhesiolysis: Inpatient care and expenditures in the United States in 1994
    • N.F. Ray, W.G. Denton, and M. Thamer Abdominal adhesiolysis: Inpatient care and expenditures in the United States in 1994 J Am Coll Surg 186 1998 1
    • (1998) J Am Coll Surg , vol.186 , pp. 1
    • Ray, N.F.1    Denton, W.G.2    Thamer, M.3
  • 5
    • 0024360388 scopus 로고
    • The biology of interleukin-6
    • T. Kishimoto The biology of interleukin-6 Blood 74 1989 1
    • (1989) Blood , vol.74 , pp. 1
    • Kishimoto, T.1
  • 6
    • 0036159040 scopus 로고    scopus 로고
    • IL-1, IL-6 and TNF-α concentrations in the peritoneal fluid of women with pelvic adhesions
    • Y.C. Cheong, J.B. Shelton, and S.M. Laird IL-1, IL-6 and TNF-α concentrations in the peritoneal fluid of women with pelvic adhesions Hum Reprod 17 2002 69
    • (2002) Hum Reprod , vol.17 , pp. 69
    • Cheong, Y.C.1    Shelton, J.B.2    Laird, S.M.3
  • 7
    • 0036548611 scopus 로고    scopus 로고
    • Peritoneal molecular environment, adhesion formation and clinical implication
    • N. Chegini Peritoneal molecular environment, adhesion formation and clinical implication Front Biosci 7 2002 e91
    • (2002) Front Biosci , vol.7 , pp. 91
    • Chegini, N.1
  • 8
    • 0029888909 scopus 로고    scopus 로고
    • Effects of interleukin-6 and its neutralizing antibodies on peritoneal adhesion formation and wound healing
    • A.A. Saba, A.A. Kaidi, and V. Godziachvili Effects of interleukin-6 and its neutralizing antibodies on peritoneal adhesion formation and wound healing Am Surg 62 1996 569
    • (1996) Am Surg , vol.62 , pp. 569
    • Saba, A.A.1    Kaidi, A.A.2    Godziachvili, V.3
  • 9
    • 0036104339 scopus 로고    scopus 로고
    • The correlation of adhesions and peritoneal fluid cytokine concentrations: A pilot study
    • Y.C. Cheong, S.M. Laird, and J.B. Shelton The correlation of adhesions and peritoneal fluid cytokine concentrations: A pilot study Hum Reprod 17 2002 1039
    • (2002) Hum Reprod , vol.17 , pp. 1039
    • Cheong, Y.C.1    Laird, S.M.2    Shelton, J.B.3
  • 10
    • 0026751455 scopus 로고
    • Elevated interleukin-6 levels in peritoneal fluid of patients with pelvic pathology
    • R.P. Buyalos, V.A. Funari, and R. Azziz Elevated interleukin-6 levels in peritoneal fluid of patients with pelvic pathology Fertil Steril 58 1992 302
    • (1992) Fertil Steril , vol.58 , pp. 302
    • Buyalos, R.P.1    Funari, V.A.2    Azziz, R.3
  • 11
    • 0023942493 scopus 로고
    • Interleukin-6 in synovial fluid and serum of patients with rheumatoid arthritis and other inflammatory arthritides
    • F.A. Houssiau, J.P. Devogelaer, and J. Van Damme Interleukin-6 in synovial fluid and serum of patients with rheumatoid arthritis and other inflammatory arthritides Arthritis Rheum 31 1988 784
    • (1988) Arthritis Rheum , vol.31 , pp. 784
    • Houssiau, F.A.1    Devogelaer, J.P.2    Van Damme, J.3
  • 12
    • 33746214777 scopus 로고    scopus 로고
    • MAPKAP kinase 2-deficient mice are resistant to collagen-induced arthritis
    • M. Hegen, M. Gaestel, and C.L. Nickerson-Nutter MAPKAP kinase 2-deficient mice are resistant to collagen-induced arthritis J Immunol 177 2006 1913
    • (2006) J Immunol , vol.177 , pp. 1913
    • Hegen, M.1    Gaestel, M.2    Nickerson-Nutter, C.L.3
  • 13
    • 0023848694 scopus 로고
    • Elevated levels of the 26K human hybridoma growth factor (interleukin 6) in cerebrospinal fluid of patients with acute infection of the central nervous system
    • F.A. Houssiau, K. Bukasa, and C.J. Sindic Elevated levels of the 26K human hybridoma growth factor (interleukin 6) in cerebrospinal fluid of patients with acute infection of the central nervous system Clin Exp Immunol 71 1988 320
    • (1988) Clin Exp Immunol , vol.71 , pp. 320
    • Houssiau, F.A.1    Bukasa, K.2    Sindic, C.J.3
  • 14
    • 0023849455 scopus 로고
    • Autocrine generation and requirement of BSF-2/IL-6 for human multiple myelomas
    • M. Kawano, T. Hirano, and T. Matsuda Autocrine generation and requirement of BSF-2/IL-6 for human multiple myelomas Nature 332 1988 83
    • (1988) Nature , vol.332 , pp. 83
    • Kawano, M.1    Hirano, T.2    Matsuda, T.3
  • 15
    • 0024386426 scopus 로고
    • Interleukin-6 (IL-6) functions as an in vitro autocrine growth factor in renal cell carcinomas
    • S. Miki, M. Iwano, and Y. Miki Interleukin-6 (IL-6) functions as an in vitro autocrine growth factor in renal cell carcinomas FEBS Lett 250 1989 607
    • (1989) FEBS Lett , vol.250 , pp. 607
    • Miki, S.1    Iwano, M.2    Miki, Y.3
  • 16
    • 0029005689 scopus 로고
    • Circulating interleukin-6 levels in patients with bronchial asthma
    • A. Yokoyama, N. Kohno, and S. Fujino Circulating interleukin-6 levels in patients with bronchial asthma Am J Respir Crit Care Med 151 1995 1354
    • (1995) Am J Respir Crit Care Med , vol.151 , pp. 1354
    • Yokoyama, A.1    Kohno, N.2    Fujino, S.3
  • 17
    • 0024358854 scopus 로고
    • Interleukin 6 decreases cell-cell association and increases motility of ductal breast carcinoma cells
    • I. Tamm, I. Cardinale, and J. Krueger Interleukin 6 decreases cell-cell association and increases motility of ductal breast carcinoma cells J Exp Med 170 1989 1649
    • (1989) J Exp Med , vol.170 , pp. 1649
    • Tamm, I.1    Cardinale, I.2    Krueger, J.3
  • 18
    • 0343185888 scopus 로고
    • Human B-cell differentiation factor defined by an anti-peptide antibody and its possible role in autoantibody production
    • T. Hirano, T. Taga, and K. Yasukawa Human B-cell differentiation factor defined by an anti-peptide antibody and its possible role in autoantibody production Proc Natl Acad Sci USA 84 1987 228
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 228
    • Hirano, T.1    Taga, T.2    Yasukawa, K.3
  • 19
    • 0024316824 scopus 로고
    • IL-1 and IL-6 release by tumor-associated macrophages from human ovarian carcinoma
    • A. Erroi, M. Sironi, and F. Chiaffarino IL-1 and IL-6 release by tumor-associated macrophages from human ovarian carcinoma Int J Cancer 44 1989 795
    • (1989) Int J Cancer , vol.44 , pp. 795
    • Erroi, A.1    Sironi, M.2    Chiaffarino, F.3
  • 20
    • 0027534993 scopus 로고
    • High IL-6 levels in ascitic fluid correlate with reactive thrombocytosis in patients with epithelial ovarian cancer
    • G. Gastl, M. Plante, and C.L. Finstad High IL-6 levels in ascitic fluid correlate with reactive thrombocytosis in patients with epithelial ovarian cancer Br J Haematol 83 1993 433
    • (1993) Br J Haematol , vol.83 , pp. 433
    • Gastl, G.1    Plante, M.2    Finstad, C.L.3
  • 21
    • 0026622033 scopus 로고
    • Quantitation of tumor necrosis factor-α, interleukin-1 β, and interleukin-6 in the effusions of ovarian epithelial neoplasms
    • W.H. Kutteh, and C.C. Kutteh Quantitation of tumor necrosis factor-α, interleukin-1 β, and interleukin-6 in the effusions of ovarian epithelial neoplasms Am J Obstet Gynecol 167 1992 1864
    • (1992) Am J Obstet Gynecol , vol.167 , pp. 1864
    • Kutteh, W.H.1    Kutteh, C.C.2
  • 22
    • 0028321886 scopus 로고
    • Interleukin-6 serum levels in patients with gynecological tumors
    • G. Scambia, U. Testa, and P.B. Panici Interleukin-6 serum levels in patients with gynecological tumors Int J Cancer 57 1994 318
    • (1994) Int J Cancer , vol.57 , pp. 318
    • Scambia, G.1    Testa, U.2    Panici, P.B.3
  • 23
    • 33747632142 scopus 로고    scopus 로고
    • MAPK-activated protein kinase 2 deficiency in microglia inhibits pro-inflammatory mediator release and resultant neurotoxicity. Relevance to neuroinflammation in a transgenic mouse model of Alzheimer disease
    • A.A. Culbert, S.D. Skaper, and D.R. Howlett MAPK-activated protein kinase 2 deficiency in microglia inhibits pro-inflammatory mediator release and resultant neurotoxicity. Relevance to neuroinflammation in a transgenic mouse model of Alzheimer disease J Biol Chem 281 2006 23658
    • (2006) J Biol Chem , vol.281 , pp. 23658
    • Culbert, A.A.1    Skaper, S.D.2    Howlett, D.R.3
  • 24
    • 34447258367 scopus 로고    scopus 로고
    • MK2 controls the level of negative feedback in the NF-κB pathway and is essential for vascular permeability and airway inflammation
    • M.M. Gorska, Q. Liang, and S.J. Stafford MK2 controls the level of negative feedback in the NF-κB pathway and is essential for vascular permeability and airway inflammation J Exp Med 204 2007 1637
    • (2007) J Exp Med , vol.204 , pp. 1637
    • Gorska, M.M.1    Liang, Q.2    Stafford, S.J.3
  • 25
    • 36348954401 scopus 로고    scopus 로고
    • Systemic deficiency of the MAP kinase-activated protein kinase 2 reduces atherosclerosis in hypercholesterolemic mice
    • K. Jagavelu, U.J. Tietge, and M. Gaestel Systemic deficiency of the MAP kinase-activated protein kinase 2 reduces atherosclerosis in hypercholesterolemic mice Circ Res 101 2007 1104
    • (2007) Circ Res , vol.101 , pp. 1104
    • Jagavelu, K.1    Tietge, U.J.2    Gaestel, M.3
  • 26
    • 0037121941 scopus 로고    scopus 로고
    • Genetic dissection of the cellular pathways and signaling mechanisms in modeled tumor necrosis factor-induced Crohn's-like inflammatory bowel disease
    • D. Kontoyiannis, G. Boulougouris, and M. Manoloukos Genetic dissection of the cellular pathways and signaling mechanisms in modeled tumor necrosis factor-induced Crohn's-like inflammatory bowel disease J Exp Med 196 2002 1563
    • (2002) J Exp Med , vol.196 , pp. 1563
    • Kontoyiannis, D.1    Boulougouris, G.2    Manoloukos, M.3
  • 27
    • 0033145354 scopus 로고    scopus 로고
    • MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis
    • A. Kotlyarov, A. Neininger, and C. Schubert MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis Nat Cell Biol 1 1999 94
    • (1999) Nat Cell Biol , vol.1 , pp. 94
    • Kotlyarov, A.1    Neininger, A.2    Schubert, C.3
  • 28
    • 33846821915 scopus 로고    scopus 로고
    • P53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage
    • H.C. Reinhardt, A.S. Aslanian, and J.A. Lees p53-deficient cells rely on ATM- and ATR-mediated checkpoint signaling through the p38MAPK/MK2 pathway for survival after DNA damage Cancer Cell 11 2007 175
    • (2007) Cancer Cell , vol.11 , pp. 175
    • Reinhardt, H.C.1    Aslanian, A.S.2    Lees, J.A.3
  • 29
    • 49249089112 scopus 로고    scopus 로고
    • MAP-kinase-activated protein kinase 2 expression and activity is induced after neuronal depolarization
    • T. Thomas, E. Hitti, and A. Kotlyarov MAP-kinase-activated protein kinase 2 expression and activity is induced after neuronal depolarization Eur J Neurosci 28 2008 642
    • (2008) Eur J Neurosci , vol.28 , pp. 642
    • Thomas, T.1    Hitti, E.2    Kotlyarov, A.3
  • 30
    • 33646887783 scopus 로고    scopus 로고
    • Gene deletion of MK2 inhibits TNF-α and IL-6 and protects against cerulein-induced pancreatitis
    • A.B. Tietz, A. Malo, and J. Diebold Gene deletion of MK2 inhibits TNF-α and IL-6 and protects against cerulein-induced pancreatitis Am J Physiol Gastrointest Liver Physiol 290 2006 G1298
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.290 , pp. 1298
    • Tietz, A.B.1    Malo, A.2    Diebold, J.3
  • 31
    • 0036479125 scopus 로고    scopus 로고
    • MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels
    • A. Neininger, D. Kontoyiannis, and A. Kotlyarov MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels J Biol Chem 277 2002 3065
    • (2002) J Biol Chem , vol.277 , pp. 3065
    • Neininger, A.1    Kontoyiannis, D.2    Kotlyarov, A.3
  • 32
    • 43549083894 scopus 로고    scopus 로고
    • MAPKAP kinase 2-deficiency prevents neurons from cell death by reducing neuroinflammation-Relevance in a mouse model of Parkinson's disease
    • T. Thomas, M. Timmer, and K. Cesnulevicius MAPKAP kinase 2-deficiency prevents neurons from cell death by reducing neuroinflammation-Relevance in a mouse model of Parkinson's disease J Neurochem 105 2008 2039
    • (2008) J Neurochem , vol.105 , pp. 2039
    • Thomas, T.1    Timmer, M.2    Cesnulevicius, K.3
  • 33
    • 31144468296 scopus 로고    scopus 로고
    • Protein expression of TNF-α in psoriatic skin is regulated at a posttranscriptional level by MAPK-activated protein kinase 2
    • C. Johansen, A.T. Funding, and K. Otkjaer Protein expression of TNF-α in psoriatic skin is regulated at a posttranscriptional level by MAPK-activated protein kinase 2 J Immunol 176 2006 1431
    • (2006) J Immunol , vol.176 , pp. 1431
    • Johansen, C.1    Funding, A.T.2    Otkjaer, K.3
  • 34
    • 0037011121 scopus 로고    scopus 로고
    • Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs
    • S. Rousseau, N. Morrice, and M. Peggie Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs EMBO J 21 2002 6505
    • (2002) EMBO J , vol.21 , pp. 6505
    • Rousseau, S.1    Morrice, N.2    Peggie, M.3
  • 35
    • 0030739229 scopus 로고    scopus 로고
    • Effect of protein kinase inhibitors on activity of mammalian small heat-shock protein (HSP25) kinase
    • K. Hayess, and R. Benndorf Effect of protein kinase inhibitors on activity of mammalian small heat-shock protein (HSP25) kinase Biochem Pharmacol 53 1997 1239
    • (1997) Biochem Pharmacol , vol.53 , pp. 1239
    • Hayess, K.1    Benndorf, R.2
  • 36
    • 64049096535 scopus 로고    scopus 로고
    • Inhibition of HSP27 phosphorylation by a cell-permeant MAPKAP kinase 2 inhibitor
    • L.B. Lopes, C. Flynn, and P. Komalavilas Inhibition of HSP27 phosphorylation by a cell-permeant MAPKAP kinase 2 inhibitor Biochem Biophys Res Commun 382 2009 535
    • (2009) Biochem Biophys Res Commun , vol.382 , pp. 535
    • Lopes, L.B.1    Flynn, C.2    Komalavilas, P.3
  • 37
    • 70449686720 scopus 로고    scopus 로고
    • Design of a bioactive cell-penetrating, peptide: When a transduction domain does more than transduce
    • B.C. Ward, B.L. Seal, and C.M. Brophy Design of a bioactive cell-penetrating, peptide: When a transduction domain does more than transduce J Peptide Sci 2009
    • (2009) J Peptide Sci
    • Ward, B.C.1    Seal, B.L.2    Brophy, C.M.3
  • 38
    • 0035863391 scopus 로고    scopus 로고
    • Synthetic protein transduction domains: Enhanced transduction potential in vitro and in vivo
    • A. Ho, S.R. Schwarze, and S.J. Mermelstein Synthetic protein transduction domains: Enhanced transduction potential in vitro and in vivo Cancer Res 61 2001 474
    • (2001) Cancer Res , vol.61 , pp. 474
    • Ho, A.1    Schwarze, S.R.2    Mermelstein, S.J.3
  • 40
    • 0026551375 scopus 로고
    • Effect of phosphatidylcholine on postoperative adhesions after small bowel anastomosis in the rat
    • M. Snoj Effect of phosphatidylcholine on postoperative adhesions after small bowel anastomosis in the rat Br J Surg 79 1992 427
    • (1992) Br J Surg , vol.79 , pp. 427
    • Snoj, M.1
  • 41
    • 78651165459 scopus 로고
    • Prevention of adhesions with polyvinylpyrrolidone - Preliminary report
    • M. Mazuji, K. Kalambaheti, and B. Pawar Prevention of adhesions with polyvinylpyrrolidone - Preliminary report Arch Surg 89 1964 1011
    • (1964) Arch Surg , vol.89 , pp. 1011
    • Mazuji, M.1    Kalambaheti, K.2    Pawar, B.3
  • 42
    • 0029881336 scopus 로고    scopus 로고
    • A simplified method for the analysis of hydroxyproline in biological tissues
    • G.K. Reddy, and C.S. Enwemeka A simplified method for the analysis of hydroxyproline in biological tissues Clin Biochem 29 1996 225
    • (1996) Clin Biochem , vol.29 , pp. 225
    • Reddy, G.K.1    Enwemeka, C.S.2
  • 43
    • 0029082041 scopus 로고
    • Interleukin-8 production by human mesothelial cells after direct stimulation with staphylococci
    • C.E. Visser, J.J. Steenbergen, and M.G. Betjes Interleukin-8 production by human mesothelial cells after direct stimulation with staphylococci Infect Immun 63 1995 4206
    • (1995) Infect Immun , vol.63 , pp. 4206
    • Visser, C.E.1    Steenbergen, J.J.2    Betjes, M.G.3
  • 44
    • 0027298546 scopus 로고
    • Human peritoneal mesothelial cells synthesize interleukin-6: Induction by IL-1 β and TNF α
    • N. Topley, A. Jorres, and W. Luttmann Human peritoneal mesothelial cells synthesize interleukin-6: Induction by IL-1 β and TNF α Kidney Int 43 1993 226
    • (1993) Kidney Int , vol.43 , pp. 226
    • Topley, N.1    Jorres, A.2    Luttmann, W.3
  • 45
    • 0029112592 scopus 로고
    • IL-6 secretion by human peritoneal mesothelial and ovarian cancer cells
    • F.A. Offner, P. Obrist, and S. Stadlmann IL-6 secretion by human peritoneal mesothelial and ovarian cancer cells Cytokine 7 1995 542
    • (1995) Cytokine , vol.7 , pp. 542
    • Offner, F.A.1    Obrist, P.2    Stadlmann, S.3
  • 46
    • 0026475913 scopus 로고
    • Human peritoneal mesothelial cells produce many cytokines (granulocyte colony-stimulating factor [CSF], granulocyte-monocyte-CSF, macrophage-CSF, interleukin-1 [IL-1], and IL-6) and are activated and stimulated to grow by IL-1
    • L. Lanfrancone, D. Boraschi, and P. Ghiara Human peritoneal mesothelial cells produce many cytokines (granulocyte colony-stimulating factor [CSF], granulocyte-monocyte-CSF, macrophage-CSF, interleukin-1 [IL-1], and IL-6) and are activated and stimulated to grow by IL-1 Blood 80 1992 2835
    • (1992) Blood , vol.80 , pp. 2835
    • Lanfrancone, L.1    Boraschi, D.2    Ghiara, P.3
  • 47
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • S.P. Davies, H. Reddy, and M. Caivano Specificity and mechanism of action of some commonly used protein kinase inhibitors Biochem J 351 Pt 1 2000 95
    • (2000) Biochem J , vol.351 , Issue.PART 1 , pp. 95
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3
  • 48
    • 33644508365 scopus 로고    scopus 로고
    • MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration
    • M. Kobayashi, M. Nishita, and T. Mishima MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration Embo J 25 2006 713
    • (2006) Embo J , vol.25 , pp. 713
    • Kobayashi, M.1    Nishita, M.2    Mishima, T.3
  • 49
    • 34047102327 scopus 로고    scopus 로고
    • Smooth muscle α-actin expression and myofibroblast differentiation by TGFβ are dependent upon MK2
    • A.M. Sousa, T. Liu, and O. Guevara Smooth muscle α-actin expression and myofibroblast differentiation by TGFβ are dependent upon MK2 J Cell Biochem 100 2006 1581
    • (2006) J Cell Biochem , vol.100 , pp. 1581
    • Sousa, A.M.1    Liu, T.2    Guevara, O.3
  • 50
    • 15744394838 scopus 로고    scopus 로고
    • LIM-kinase 2 and cofilin phosphorylation mediate actin cytoskeleton reorganization induced by transforming growth factor-β
    • L. Vardouli, A. Moustakas, and C. Stournaras LIM-kinase 2 and cofilin phosphorylation mediate actin cytoskeleton reorganization induced by transforming growth factor-β J Biol Chem 280 2005 11448
    • (2005) J Biol Chem , vol.280 , pp. 11448
    • Vardouli, L.1    Moustakas, A.2    Stournaras, C.3
  • 51
    • 0031772351 scopus 로고    scopus 로고
    • In vivo evaluation of hsp27 as an inhibitor of actin polymerization: Hsp27 limits actin stress fiber and focal adhesion formation after heat shock
    • G.B. Schneider, H. Hamano, and L.F. Cooper In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp27 limits actin stress fiber and focal adhesion formation after heat shock J Cell Physiol 177 1998 575
    • (1998) J Cell Physiol , vol.177 , pp. 575
    • Schneider, G.B.1    Hamano, H.2    Cooper, L.F.3
  • 52
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • D. Stokoe, K. Engel, and D.G. Campbell Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins FEBS Lett 313 1992 307
    • (1992) FEBS Lett , vol.313 , pp. 307
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3
  • 53
    • 0026570931 scopus 로고
    • Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II
    • J. Landry, H. Lambert, and M. Zhou Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II J Biol Chem 267 1992 794
    • (1992) J Biol Chem , vol.267 , pp. 794
    • Landry, J.1    Lambert, H.2    Zhou, M.3
  • 54
    • 0030565457 scopus 로고    scopus 로고
    • A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress
    • A.D. Clifton, P.R. Young, and P. Cohen A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress FEBS Lett 392 1996 209
    • (1996) FEBS Lett , vol.392 , pp. 209
    • Clifton, A.D.1    Young, P.R.2    Cohen, P.3
  • 55
    • 0028815952 scopus 로고
    • MAPKAP kinase 2 is activated by heat shock and TNF-α: In vivo phosphorylation of small heat shock protein results from stimulation of the MAP kinase cascade
    • K. Engel, A. Ahlers, and M.A. Brach MAPKAP kinase 2 is activated by heat shock and TNF-α: In vivo phosphorylation of small heat shock protein results from stimulation of the MAP kinase cascade J Cell Biochem 57 1995 321
    • (1995) J Cell Biochem , vol.57 , pp. 321
    • Engel, K.1    Ahlers, A.2    Brach, M.A.3
  • 56
    • 0032508660 scopus 로고    scopus 로고
    • A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini
    • C. Schafer, S.E. Ross, and M.J. Bragado A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini J Biol Chem 273 1998 24173
    • (1998) J Biol Chem , vol.273 , pp. 24173
    • Schafer, C.1    Ross, S.E.2    Bragado, M.J.3
  • 57
    • 33845807361 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK
    • N. Ronkina, A. Kotlyarov, and O. Dittrich-Breiholz The mitogen-activated protein kinase (MAPK)-activated protein kinases MK2 and MK3 cooperate in stimulation of tumor necrosis factor biosynthesis and stabilization of p38 MAPK Mol Cell Biol 27 2007 170
    • (2007) Mol Cell Biol , vol.27 , pp. 170
    • Ronkina, N.1    Kotlyarov, A.2    Dittrich-Breiholz, O.3
  • 58
    • 77955421113 scopus 로고    scopus 로고
    • In vivo and in vitro SAR of tetracyclic MAPKAP-K2 (MK2) inhibitors. Part i
    • L. Revesz, A. Schlapbach, and R. Aichholz In vivo and in vitro SAR of tetracyclic MAPKAP-K2 (MK2) inhibitors. Part I Bioorg Med Chem Let 20 2010 4719
    • (2010) Bioorg Med Chem Let , vol.20 , pp. 4719
    • Revesz, L.1    Schlapbach, A.2    Aichholz, R.3
  • 59
    • 0032526694 scopus 로고    scopus 로고
    • PRAK, a novel protein kinase regulated by the p38 MAP kinase
    • L. New, Y. Jiang, and M. Zhao PRAK, a novel protein kinase regulated by the p38 MAP kinase Embo J 17 1998 3372
    • (1998) Embo J , vol.17 , pp. 3372
    • New, L.1    Jiang, Y.2    Zhao, M.3
  • 60
    • 33244471768 scopus 로고    scopus 로고
    • MAPKAP kinases - MKs - two's company, three's a crowd
    • M. Gaestel MAPKAP kinases - MKs - two's company, three's a crowd Nat Rev Mol Cell Biol 7 2006 120
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 120
    • Gaestel, M.1
  • 61
    • 0041344614 scopus 로고    scopus 로고
    • Heat shock protein 27 controls apoptosis by regulating Akt activation
    • M.J. Rane, Y. Pan, and S. Singh Heat shock protein 27 controls apoptosis by regulating Akt activation J Biol Chem 278 2003 27828
    • (2003) J Biol Chem , vol.278 , pp. 27828
    • Rane, M.J.1    Pan, Y.2    Singh, S.3
  • 62
    • 17644370387 scopus 로고    scopus 로고
    • A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D
    • H. Doppler, P. Storz, and J. Li A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D J Biol Chem 280 2005 15013
    • (2005) J Biol Chem , vol.280 , pp. 15013
    • Doppler, H.1    Storz, P.2    Li, J.3
  • 63
    • 24044485916 scopus 로고    scopus 로고
    • HSP25 inhibits protein kinase C delta-mediated cell death through direct interaction
    • Y.J. Lee, D.H. Lee, and C.K. Cho HSP25 inhibits protein kinase C delta-mediated cell death through direct interaction J Biol Chem 280 2005 18108
    • (2005) J Biol Chem , vol.280 , pp. 18108
    • Lee, Y.J.1    Lee, D.H.2    Cho, C.K.3
  • 64
    • 0032526192 scopus 로고    scopus 로고
    • Heat-shock protein-25/27 phosphorylation by the delta isoform of protein kinase C
    • E.T. Maizels, C.A. Peters, and M. Kline Heat-shock protein-25/27 phosphorylation by the delta isoform of protein kinase C Biochem J 332 Pt 3 1998 703
    • (1998) Biochem J , vol.332 , Issue.PART 3 , pp. 703
    • Maizels, E.T.1    Peters, C.A.2    Kline, M.3
  • 65
    • 0035793574 scopus 로고    scopus 로고
    • P38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • M.J. Rane, P.Y. Coxon, and D.W. Powell p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils J Biol Chem 276 2001 3517
    • (2001) J Biol Chem , vol.276 , pp. 3517
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3
  • 66
    • 33846000629 scopus 로고    scopus 로고
    • MAPK-activated protein kinase-2 (MK2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, MK2, Akt, and Hsp27
    • C. Zheng, Z. Lin, and Z.J. Zhao MAPK-activated protein kinase-2 (MK2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, MK2, Akt, and Hsp27 J Biol Chem 281 2006 37215
    • (2006) J Biol Chem , vol.281 , pp. 37215
    • Zheng, C.1    Lin, Z.2    Zhao, Z.J.3
  • 67
    • 79958210270 scopus 로고    scopus 로고
    • Available at AccessedApril
    • Available at: http://www.fda.gov/MedicalDevices/ ProductsandMedicalProcedures/DeviceApprovalsandClearances/Recently- ApprovedDevices/ucm077891.htm. Accessed April 2009.
    • (2009)
  • 69
    • 0038078565 scopus 로고    scopus 로고
    • A prospective, randomized, multicenter, controlled study of the safety of Seprafilm adhesion barrier in abdominopelvic surgery of the intestine
    • D.E. Beck, Z. Cohen, and J.W. Fleshman A prospective, randomized, multicenter, controlled study of the safety of Seprafilm adhesion barrier in abdominopelvic surgery of the intestine Dis Colon Rectum 46 2003 1310
    • (2003) Dis Colon Rectum , vol.46 , pp. 1310
    • Beck, D.E.1    Cohen, Z.2    Fleshman, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.