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Volumn 148, Issue 7, 2007, Pages 3176-3184

Increased phosphorylation of myosin light chain prevents in vitro decidualization

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SMOOTH MUSCLE ACTIN; BETA TUBULIN; BLEBBISTATIN; CYCLIC AMP; ESTRADIOL; FIBRONECTIN; FOCAL ADHESION KINASE; INTERLEUKIN 1BETA; MEDROXYPROGESTERONE ACETATE; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN KINASE; MYOSIN LIGHT CHAIN KINASE INHIBITOR; VINCULIN;

EID: 34347255711     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2006-1673     Document Type: Article
Times cited : (33)

References (58)
  • 1
    • 0033638444 scopus 로고    scopus 로고
    • Uteroplacental blood flow. The story of decidualization, menstruation and trophoblast invasion
    • Kliman HJ 2000 Uteroplacental blood flow. The story of decidualization, menstruation and trophoblast invasion. Am J Pathol 157:1759-1768
    • (2000) Am J Pathol , vol.157 , pp. 1759-1768
    • Kliman, H.J.1
  • 2
    • 0141614998 scopus 로고    scopus 로고
    • Complex regulation of decidualization: A role for cytokines and proteases
    • Salamonsen LA, Dimitriadis E, Jones RL, Nie G 2003 Complex regulation of decidualization: a role for cytokines and proteases. Placenta 24(Suppl A):S76-S85
    • (2003) Placenta , vol.24 , Issue.SUPPL. A
    • Salamonsen, L.A.1    Dimitriadis, E.2    Jones, R.L.3    Nie, G.4
  • 3
    • 0023835917 scopus 로고
    • Soluble 34K binding protein inhibits the binding of insulin-like growth factor I to its cell receptors in human secretory phase endometrium: Evidence for autocrine/paracrine regulation of growth factor action
    • Rutanen EM, Pekonen F, Makinen T 1988 Soluble 34K binding protein inhibits the binding of insulin-like growth factor I to its cell receptors in human secretory phase endometrium: evidence for autocrine/paracrine regulation of growth factor action. J Clin Endocrinol Metab 66:173-180
    • (1988) J Clin Endocrinol Metab , vol.66 , pp. 173-180
    • Rutanen, E.M.1    Pekonen, F.2    Makinen, T.3
  • 4
    • 0027267510 scopus 로고
    • Sequential appearance of relaxin, prolactin and IGFBP-1 during growth and differentiation of the human endometrium
    • Bryant-Greenwood GD, Rutanen EM, Partanen S, Coelho TK, Yamamoto SY 1993 Sequential appearance of relaxin, prolactin and IGFBP-1 during growth and differentiation of the human endometrium. Mol Cell Endocrinol 95:23-29
    • (1993) Mol Cell Endocrinol , vol.95 , pp. 23-29
    • Bryant-Greenwood, G.D.1    Rutanen, E.M.2    Partanen, S.3    Coelho, T.K.4    Yamamoto, S.Y.5
  • 6
    • 85047675242 scopus 로고    scopus 로고
    • Interleukin-1β induces the expression of insulin-like growth factor binding protein-1 during decidualization in the primate
    • Strakova Z, Srisuparp S, Fazleabas AT 2000 Interleukin-1β induces the expression of insulin-like growth factor binding protein-1 during decidualization in the primate. Endocrinology 141:4664-4670
    • (2000) Endocrinology , vol.141 , pp. 4664-4670
    • Strakova, Z.1    Srisuparp, S.2    Fazleabas, A.T.3
  • 7
    • 0344394270 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases prevents the synthesis of insulin-like growth factor binding protein-1 during decidualization in the baboon
    • Strakova Z, Szmidt M, Srisuparp S, Fazleabas AT 2003 Inhibition of matrix metalloproteinases prevents the synthesis of insulin-like growth factor binding protein-1 during decidualization in the baboon. Endocrinology 144:5339-5346
    • (2003) Endocrinology , vol.144 , pp. 5339-5346
    • Strakova, Z.1    Szmidt, M.2    Srisuparp, S.3    Fazleabas, A.T.4
  • 8
    • 84995853574 scopus 로고
    • Interleukin-1 system in the materno-trophoblast unit in human implantation: Immunohistochemical evidence for autocrine/paracrine function
    • Simon C, Frances A, Piquette G, Hendrickson M, Milki A, Polan ML 1994 Interleukin-1 system in the materno-trophoblast unit in human implantation: immunohistochemical evidence for autocrine/paracrine function. J Clin Endocrinol Metab 78:847-854
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 847-854
    • Simon, C.1    Frances, A.2    Piquette, G.3    Hendrickson, M.4    Milki, A.5    Polan, M.L.6
  • 10
    • 0031798349 scopus 로고    scopus 로고
    • Comparative studies on the in vitro decidualization process in the baboon (Papio anubis) and human
    • Kim JJ, Jaffe RC, Fazleabas AT 1998 Comparative studies on the in vitro decidualization process in the baboon (Papio anubis) and human. Biol Reprod 59:160-168
    • (1998) Biol Reprod , vol.59 , pp. 160-168
    • Kim, J.J.1    Jaffe, R.C.2    Fazleabas, A.T.3
  • 11
    • 0141842624 scopus 로고    scopus 로고
    • Cyclic AMP and progesterone receptor cross-talk in human endometrium: A decidualizing affair
    • Gellersen B, Brosens J 2003 Cyclic AMP and progesterone receptor cross-talk in human endometrium: a decidualizing affair. J Endocrinol 178:357-372
    • (2003) J Endocrinol , vol.178 , pp. 357-372
    • Gellersen, B.1    Brosens, J.2
  • 12
    • 0034456460 scopus 로고    scopus 로고
    • Discovery of new inducible genes in in vitro decidualized human endometrial stromal cells using microarray technology
    • Popovici RM, Kao LC, Giudice LC 2000 Discovery of new inducible genes in in vitro decidualized human endometrial stromal cells using microarray technology. Endocrinology 141:3510-3513
    • (2000) Endocrinology , vol.141 , pp. 3510-3513
    • Popovici, R.M.1    Kao, L.C.2    Giudice, L.C.3
  • 13
    • 0346109672 scopus 로고    scopus 로고
    • Gene induction and categorical reprogramming during in vitro human endometrial fibroblast decidualization
    • Brar AK, Handwerger S, Kessler CA, Aronow BJ 2001 Gene induction and categorical reprogramming during in vitro human endometrial fibroblast decidualization. Physiol Genomics 7:135-148
    • (2001) Physiol Genomics , vol.7 , pp. 135-148
    • Brar, A.K.1    Handwerger, S.2    Kessler, C.A.3    Aronow, B.J.4
  • 14
    • 1842587729 scopus 로고    scopus 로고
    • Activation of the protein kinase A pathway in human endometrial stromal cells reveals sequential categorical gene regulation
    • Tierney EP, Tulac S, Huang ST, Giudice LC 2003 Activation of the protein kinase A pathway in human endometrial stromal cells reveals sequential categorical gene regulation. Physiol Genom 16:47-66
    • (2003) Physiol Genom , vol.16 , pp. 47-66
    • Tierney, E.P.1    Tulac, S.2    Huang, S.T.3    Giudice, L.C.4
  • 15
    • 8844260444 scopus 로고    scopus 로고
    • Two billion years of actin. Meeting on cytoskeletal dynamics: From cell biology to developmental disease
    • Ayscough KR, Winder SJ 2004 Two billion years of actin. Meeting on cytoskeletal dynamics: from cell biology to developmental disease. EMBO Rep 5:947-952
    • (2004) EMBO Rep , vol.5 , pp. 947-952
    • Ayscough, K.R.1    Winder, S.J.2
  • 16
    • 0023785596 scopus 로고
    • Cellular mechanics as an indicator of cytoskeletal structure and function
    • Elson EL 1988 Cellular mechanics as an indicator of cytoskeletal structure and function. Annu Rev Biophys Biophys Chem 17:397-430
    • (1988) Annu Rev Biophys Biophys Chem , vol.17 , pp. 397-430
    • Elson, E.L.1
  • 17
    • 0026058812 scopus 로고
    • Myosin phosphorylation/ dephosphorylation and regulation of airway smooth muscle contractility
    • de Lanerolle P, Paul RJ 1991 Myosin phosphorylation/ dephosphorylation and regulation of airway smooth muscle contractility. Am J Physiol 261:L1-L14
    • (1991) Am J Physiol , vol.261
    • de Lanerolle, P.1    Paul, R.J.2
  • 18
    • 0026709998 scopus 로고
    • Control of nonmuscle myosins by phosphorylation
    • Tan JL, Ravid S, Spudich JA 1992 Control of nonmuscle myosins by phosphorylation. Annu Rev Biochem 61:721-759
    • (1992) Annu Rev Biochem , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 19
    • 0021057353 scopus 로고
    • Regulation of contractile proteins by phosphorylation
    • Adelstein RS 1983 Regulation of contractile proteins by phosphorylation. J Clin Invest 72:1863-1866
    • (1983) J Clin Invest , vol.72 , pp. 1863-1866
    • Adelstein, R.S.1
  • 20
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo AP, Somlyo AV 1994 Signal transduction and regulation in smooth muscle. Nature 372:231-236
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 21
    • 0032908870 scopus 로고    scopus 로고
    • Insulin-like growth factor binding protein-1 expression in baboon endometrial stromal cells: Regulation by filamentous actin and requirement for de novo protein synthesis
    • Kim JJ, Jaffe RC, Fazleabas AT 1999 Insulin-like growth factor binding protein-1 expression in baboon endometrial stromal cells: regulation by filamentous actin and requirement for de novo protein synthesis. Endocrinology 140:997-1004
    • (1999) Endocrinology , vol.140 , pp. 997-1004
    • Kim, J.J.1    Jaffe, R.C.2    Fazleabas, A.T.3
  • 22
    • 0019838042 scopus 로고
    • Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells
    • de Lanerolle P, Adelstein RS, Feramisco JR, Burridge K 1981 Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells. Proc Natl Acad Sci USA 78:4738-4742
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4738-4742
    • de Lanerolle, P.1    Adelstein, R.S.2    Feramisco, J.R.3    Burridge, K.4
  • 23
    • 0024333225 scopus 로고
    • Okadaic acid, a phosphatase inhibitor, produces a Ca2+ and calmodulin-independent contraction of smooth muscle
    • Obara K, Takai A, Ruegg JC, de Lanerolle P 1989 Okadaic acid, a phosphatase inhibitor, produces a Ca2+ and calmodulin-independent contraction of smooth muscle. Pflugers Arch 414:134-138
    • (1989) Pflugers Arch , vol.414 , pp. 134-138
    • Obara, K.1    Takai, A.2    Ruegg, J.C.3    de Lanerolle, P.4
  • 24
    • 0020586658 scopus 로고
    • Characterization of the synthesis and release of prolactin by an enriched fraction of human decidual cells
    • Markoff E, Zeitler P, Peleg S, Hardwerger S 1983 Characterization of the synthesis and release of prolactin by an enriched fraction of human decidual cells. J Clin Endocrinol Metab 56:962-968
    • (1983) J Clin Endocrinol Metab , vol.56 , pp. 962-968
    • Markoff, E.1    Zeitler, P.2    Peleg, S.3    Hardwerger, S.4
  • 25
    • 0028837998 scopus 로고
    • Fibroblast cells from term human decidua closely resemble endometrial stromal cells: Induction of prolactin and insulin-like growth factor binding protein-1 expression
    • Richards RG, Brar AK, Frank GR, Hartman SM, Jikihara H 1995 Fibroblast cells from term human decidua closely resemble endometrial stromal cells: induction of prolactin and insulin-like growth factor binding protein-1 expression. Biol Reprod 52:609-615
    • (1995) Biol Reprod , vol.52 , pp. 609-615
    • Richards, R.G.1    Brar, A.K.2    Frank, G.R.3    Hartman, S.M.4    Jikihara, H.5
  • 26
    • 0022869168 scopus 로고
    • Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA
    • Guerriero Jr V, Russo MA, Olson NJ, Putkey JA, Means AR 1986 Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. Biochemistry 25:8372-8381
    • (1986) Biochemistry , vol.25 , pp. 8372-8381
    • Guerriero Jr, V.1    Russo, M.A.2    Olson, N.J.3    Putkey, J.A.4    Means, A.R.5
  • 27
  • 28
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes CD, Hall A 1999 Rho GTPases control polarity, protrusion, and adhesion during cell movement. J Cell Biol 144:1235-1244
    • (1999) J Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 29
    • 0033846652 scopus 로고    scopus 로고
    • Modulation of the action of chorionic gonadotropin in the baboon (Papio anubis) uterus by a progesterone receptor antagonist (ZK 137.316)
    • Banaszak S, Brudney A, Donnelly K, Chai D, Chwalisz K, Fazleabas AT 2000 Modulation of the action of chorionic gonadotropin in the baboon (Papio anubis) uterus by a progesterone receptor antagonist (ZK 137.316). Biol Reprod 63:820-825
    • (2000) Biol Reprod , vol.63 , pp. 820-825
    • Banaszak, S.1    Brudney, A.2    Donnelly, K.3    Chai, D.4    Chwalisz, K.5    Fazleabas, A.T.6
  • 30
    • 0033279003 scopus 로고    scopus 로고
    • Expression of cyclooxygenase-1 and -2 in the baboon endometrium during the menstrual cycle and pregnancy
    • Kim JJ, Wang J, Bambra C, Das SK, Dey SK, Fazleabas AT 1999 Expression of cyclooxygenase-1 and -2 in the baboon endometrium during the menstrual cycle and pregnancy. Endocrinology 140:2672-2678
    • (1999) Endocrinology , vol.140 , pp. 2672-2678
    • Kim, J.J.1    Wang, J.2    Bambra, C.3    Das, S.K.4    Dey, S.K.5    Fazleabas, A.T.6
  • 32
    • 1942423274 scopus 로고    scopus 로고
    • Implantation: Embryonic signals and the modulation of the uterine environment
    • Fazleabas AT, Kim JJ, Strakova Z 2004 Implantation: embryonic signals and the modulation of the uterine environment. Placenta 25(Suppl A):S26-S31
    • (2004) Placenta , vol.25 , Issue.SUPPL. A
    • Fazleabas, A.T.1    Kim, J.J.2    Strakova, Z.3
  • 35
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • Parsons JT 2003 Focal adhesion kinase: the first ten years. J Cell Sci 116:1409-1416
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 37
    • 0028938421 scopus 로고
    • Interleukin-1-induced calcium flux in human fibroblasts is mediated through focal adhesions
    • Arora PD, Ma J, Min W, Cruz T, McCulloch AG 1995 Interleukin-1-induced calcium flux in human fibroblasts is mediated through focal adhesions. J Biol Chem 270:6042-6049
    • (1995) J Biol Chem , vol.270 , pp. 6042-6049
    • Arora, P.D.1    Ma, J.2    Min, W.3    Cruz, T.4    McCulloch, A.G.5
  • 38
    • 33746927145 scopus 로고    scopus 로고
    • IL-1β induces a MyD88-dependent and ceramide-mediated activation of Src in anterior hypothalamic neurons
    • Davis CN, Tabarean I, Gaidarova S, Behrens MM, Bartfai T 2006 IL-1β induces a MyD88-dependent and ceramide-mediated activation of Src in anterior hypothalamic neurons. J Neurochem 98:1379-1389
    • (2006) J Neurochem , vol.98 , pp. 1379-1389
    • Davis, C.N.1    Tabarean, I.2    Gaidarova, S.3    Behrens, M.M.4    Bartfai, T.5
  • 42
    • 0034604687 scopus 로고    scopus 로고
    • The recruitment of the interleukin-1 (IL-1) receptor-associated kinase (IRAK) into focal adhesion complexes is required for IL-1β-induced ERK activation
    • MacGillivray MK, Cruz TF, McCulloch CA 2000 The recruitment of the interleukin-1 (IL-1) receptor-associated kinase (IRAK) into focal adhesion complexes is required for IL-1β-induced ERK activation. J Biol Chem 275:23509-23515
    • (2000) J Biol Chem , vol.275 , pp. 23509-23515
    • MacGillivray, M.K.1    Cruz, T.F.2    McCulloch, C.A.3
  • 43
    • 0033305717 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and subcellular localization of focal adhesion proteins during in vitro decidualization of human endometrial stromal cells
    • Maruyama T, Yoshimura Y, Sabe H 1999 Tyrosine phosphorylation and subcellular localization of focal adhesion proteins during in vitro decidualization of human endometrial stromal cells. Endocrinology 140:5982-5990
    • (1999) Endocrinology , vol.140 , pp. 5982-5990
    • Maruyama, T.1    Yoshimura, Y.2    Sabe, H.3
  • 44
    • 33745050483 scopus 로고    scopus 로고
    • Altered S-phase kinase-associated protein-2 levels are a major mediator of cyclic nucleotide-induced inhibition of vascular smooth muscle cell proliferation
    • Wu YJ, Bond M, Sala-Newby GB, Newby AC 2006 Altered S-phase kinase-associated protein-2 levels are a major mediator of cyclic nucleotide-induced inhibition of vascular smooth muscle cell proliferation. Circ Res 98:1141-1150
    • (2006) Circ Res , vol.98 , pp. 1141-1150
    • Wu, Y.J.1    Bond, M.2    Sala-Newby, G.B.3    Newby, A.C.4
  • 45
    • 0029960996 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase (p125FAK): Regulation by cAMP and thrombin in mesangial cells
    • Troyer DA, Bouton A, Bedolla R, Padilla R 1996 Tyrosine phosphorylation of focal adhesion kinase (p125FAK): regulation by cAMP and thrombin in mesangial cells. J Am Soc Nephrol 7:415-423
    • (1996) J Am Soc Nephrol , vol.7 , pp. 415-423
    • Troyer, D.A.1    Bouton, A.2    Bedolla, R.3    Padilla, R.4
  • 46
    • 0033526541 scopus 로고    scopus 로고
    • Dibutyryl cyclic AMP-induced process formation in astrocytes is associated with a decrease in tyrosine phosphorylation of focal adhesion kinase and paxillin
    • Padmanabhan J, Clayton D, Shelanski ML 1999 Dibutyryl cyclic AMP-induced process formation in astrocytes is associated with a decrease in tyrosine phosphorylation of focal adhesion kinase and paxillin. J Neurobiol 39:407-422
    • (1999) J Neurobiol , vol.39 , pp. 407-422
    • Padmanabhan, J.1    Clayton, D.2    Shelanski, M.L.3
  • 47
    • 0025834881 scopus 로고
    • An increase or a decrease in myosin II phosphorylation inhibits macrophage motility
    • Wilson AK, Gorgas G, Claypool WD, de Lanerolle P 1991 An increase or a decrease in myosin II phosphorylation inhibits macrophage motility. J Cell Biol 114:277-283
    • (1991) J Cell Biol , vol.114 , pp. 277-283
    • Wilson, A.K.1    Gorgas, G.2    Claypool, W.D.3    de Lanerolle, P.4
  • 49
    • 0030824245 scopus 로고    scopus 로고
    • Expression of a mutant myosin light chain that cannot be phosphorylated increases paracellular permeability
    • Gandhi S, Lorimer DD, de Lanerolle P 1997 Expression of a mutant myosin light chain that cannot be phosphorylated increases paracellular permeability. Am J Physiol 272:F214-F221
    • (1997) Am J Physiol , vol.272
    • Gandhi, S.1    Lorimer, D.D.2    de Lanerolle, P.3
  • 50
    • 0034735542 scopus 로고    scopus 로고
    • Localization and activity of myosin light chain kinase isoforms during the cell cycle
    • Poperechnaya A, Varlamova O, Lin PJ, Stull JT, Bresnick AR 2000 Localization and activity of myosin light chain kinase isoforms during the cell cycle. J Cell Biol 151:697-708
    • (2000) J Cell Biol , vol.151 , pp. 697-708
    • Poperechnaya, A.1    Varlamova, O.2    Lin, P.J.3    Stull, J.T.4    Bresnick, A.R.5
  • 51
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders LC, Matsumura F, Bokoch GM, de Lanerolle P 1999 Inhibition of myosin light chain kinase by p21-activated kinase. Science 283:2083-2085
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    de Lanerolle, P.4
  • 54
    • 33748314466 scopus 로고    scopus 로고
    • Increased myosin light chain kinase expression in hypertension: Regulation by serum response factor via an insertion mutation in the promoter
    • Han YJ, Hu WY, Chernaya O, Antic N, Gu L, Gupta M, Piano M, de Lanerolle P 2006 Increased myosin light chain kinase expression in hypertension: regulation by serum response factor via an insertion mutation in the promoter. Mol Biol Cell 17:4039-4050
    • (2006) Mol Biol Cell , vol.17 , pp. 4039-4050
    • Han, Y.J.1    Hu, W.Y.2    Chernaya, O.3    Antic, N.4    Gu, L.5    Gupta, M.6    Piano, M.7    de Lanerolle, P.8
  • 56
    • 33748747620 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced long myosin light chain kinase transcription is regulated by differentiation-dependent signaling events. Characterization of the human long myosin light chain kinase promoter
    • Graham WV, Wang F, Clayburgh DR, Cheng JX, Yoon B, Wang Y, Lin A, Turner JR 2006 Tumor necrosis factor-induced long myosin light chain kinase transcription is regulated by differentiation-dependent signaling events. Characterization of the human long myosin light chain kinase promoter. J Biol Chem 281:26205-26215
    • (2006) J Biol Chem , vol.281 , pp. 26205-26215
    • Graham, W.V.1    Wang, F.2    Clayburgh, D.R.3    Cheng, J.X.4    Yoon, B.5    Wang, Y.6    Lin, A.7    Turner, J.R.8


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