메뉴 건너뛰기




Volumn 286, Issue 5 55-5, 2004, Pages

ERK-mediated uterine artery contraction: Role of thick and thin filament regulatory pathways

Author keywords

Intracellular free calcium concentration; Isometric tension; Myosin light chain phosphorylation; PD 098059; Phenylephrine; Phorbol 12,13 dibutyrate

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; CALCIUM; CALDESMON; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MYOSIN LIGHT CHAIN; PHENYLEPHRINE; PHORBOL DIBUTYRATE; PROTEIN P44;

EID: 1942501683     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.00981.2003     Document Type: Article
Times cited : (28)

References (57)
  • 1
    • 0029069706 scopus 로고
    • Role of tyrosine kinases in norepinephrine-induced contraction of vascular smooth muscle
    • Abebe W and Agrawal DK. Role of tyrosine kinases in norepinephrine-induced contraction of vascular smooth muscle. J Cardiovasc Pharmacol 26: 153-159, 1995.
    • (1995) J Cardiovasc Pharmacol , vol.26 , pp. 153-159
    • Abebe, W.1    Agrawal, D.K.2
  • 2
    • 0028906470 scopus 로고
    • Activation of mitogen-activated protein kinases in porcine carotid arteries
    • Adam LP, Franklin MT, Raff GJ, and Hathaway DR. Activation of mitogen-activated protein kinases in porcine carotid arteries. Circ Res 76: 183-190, 1995.
    • (1995) Circ Res , vol.76 , pp. 183-190
    • Adam, L.P.1    Franklin, M.T.2    Raff, G.J.3    Hathaway, D.R.4
  • 3
    • 0026519840 scopus 로고
    • Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas
    • Adam LP, Gapinski CJ, and Hathaway DR. Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas. FEBS Lett 302: 223-226, 1992.
    • (1992) FEBS Lett , vol.302 , pp. 223-226
    • Adam, L.P.1    Gapinski, C.J.2    Hathaway, D.R.3
  • 4
    • 0024514394 scopus 로고
    • Phosphorylation of caldesmon in arterial smooth muscle
    • Adam LP, Haeberle JR, and Hathaway DR. Phosphorylation of caldesmon in arterial smooth muscle. J Biol Chem 264: 7698-7703, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 7698-7703
    • Adam, L.P.1    Haeberle, J.R.2    Hathaway, D.R.3
  • 5
    • 0027460805 scopus 로고
    • Identification of mitogen-activated protein kinase phosphorylation sequences in mammalian h-caldesmon
    • Adam LP and Hathaway DR. Identification of mitogen-activated protein kinase phosphorylation sequences in mammalian h-caldesmon. FEBS Lett 322: 56-60, 1993.
    • (1993) FEBS Lett , vol.322 , pp. 56-60
    • Adam, L.P.1    Hathaway, D.R.2
  • 7
    • 0022466153 scopus 로고
    • Phorbol ester-induced contraction in chemically skinned vascular smooth muscle
    • Chatterjee M and Tejada M. Phorbol ester-induced contraction in chemically skinned vascular smooth muscle. Am J Physiol Cell Physiol 251: C356-C361, 1986.
    • (1986) Am J Physiol Cell Physiol , vol.251
    • Chatterjee, M.1    Tejada, M.2
  • 8
    • 0036088773 scopus 로고    scopus 로고
    • Inhibition of ERK attenuates force development by lowering myosin light chain phosphorylation
    • D'Angelo G and Adam LP. Inhibition of ERK attenuates force development by lowering myosin light chain phosphorylation. Am J Physiol Heart Circ Physiol 282: H602-H610, 2002.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282
    • D'Angelo, G.1    Adam, L.P.2
  • 9
    • 0033570095 scopus 로고    scopus 로고
    • Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle. Quantitation using novel anti-phosphopeptide antibodies
    • D'Angelo G, Graceffa P, Wang CA, Wrangle J, and Adam LP. Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle. Quantitation using novel anti-phosphopeptide antibodies. J Biol Chem 274: 30115-30121, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 30115-30121
    • D'Angelo, G.1    Graceffa, P.2    Wang, C.A.3    Wrangle, J.4    Adam, L.P.5
  • 10
    • 0021743705 scopus 로고
    • Phorbol ester-induced contraction of arterial smooth muscle and inhibition of α-adrenergic response
    • Danthuluri NR and Deth RC. Phorbol ester-induced contraction of arterial smooth muscle and inhibition of α-adrenergic response. Biochem Biophys Res Commun 125: 1103-1109, 1984.
    • (1984) Biochem Biophys Res Commun , vol.125 , pp. 1103-1109
    • Danthuluri, N.R.1    Deth, R.C.2
  • 11
    • 0031722643 scopus 로고    scopus 로고
    • A role for MAP kinase in differentiated smooth muscle contraction evoked by ot-adrenoceptor stimulation
    • Dessy C, Kim I, Sougnez CL, Laporte R, and Morgan KG. A role for MAP kinase in differentiated smooth muscle contraction evoked by ot-adrenoceptor stimulation. Am J Physiol Cell Physiol 275: C1081-C1086, 1998.
    • (1998) Am J Physiol Cell Physiol , vol.275
    • Dessy, C.1    Kim, I.2    Sougnez, C.L.3    Laporte, R.4    Morgan, K.G.5
  • 12
    • 0019433353 scopus 로고
    • Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle
    • Dillon PF, Aksoy MO, Driska SP, and Murphy RA. Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. Science 211: 495-497, 1981.
    • (1981) Science , vol.211 , pp. 495-497
    • Dillon, P.F.1    Aksoy, M.O.2    Driska, S.P.3    Murphy, R.A.4
  • 13
    • 0032555992 scopus 로고    scopus 로고
    • Caldesmon inhibits active cross-bridges in unstimulated vascular smooth muscle: An antisense oligodeoxynucleotide approach
    • Earley JJ, Su X, and Moreland RS. Caldesmon inhibits active cross-bridges in unstimulated vascular smooth muscle: an antisense oligodeoxynucleotide approach. Circ Res 83: 661-667, 1998.
    • (1998) Circ Res , vol.83 , pp. 661-667
    • Earley, J.J.1    Su, X.2    Moreland, R.S.3
  • 14
    • 0023757545 scopus 로고
    • Actions of a phorbol ester on factors regulating contraction in rabbit mesenteric artery
    • Fujiwara T, Itoh T, Kubota Y, and Kuriyama H. Actions of a phorbol ester on factors regulating contraction in rabbit mesenteric artery. Circ Res 63: 893-902, 1988.
    • (1988) Circ Res , vol.63 , pp. 893-902
    • Fujiwara, T.1    Itoh, T.2    Kubota, Y.3    Kuriyama, H.4
  • 15
    • 0028626160 scopus 로고
    • Caldesmon and calponin phosphorylation in regulation of smooth muscle contraction
    • Gerthoffer WT and Pohl J. Caldesmon and calponin phosphorylation in regulation of smooth muscle contraction. Can J Physiol Pharmacol 72: 1410-1414, 1994.
    • (1994) Can J Physiol Pharmacol , vol.72 , pp. 1410-1414
    • Gerthoffer, W.T.1    Pohl, J.2
  • 18
    • 0028258477 scopus 로고
    • Regulation of isotonic shortening velocity by second messengers in tracheal smooth muscle
    • Gunst SJ, al-Hassani MH, and Adam LP. Regulation of isotonic shortening velocity by second messengers in tracheal smooth muscle. Am J Physiol Cell Physiol 266: C684-C691, 1994.
    • (1994) Am J Physiol Cell Physiol , vol.266
    • Gunst, S.J.1    Al-Hassani, M.H.2    Adam, L.P.3
  • 20
    • 0021920052 scopus 로고
    • Regulation of isometric force and isotonic shortening velocity by phosphorylation of the 20,000-dalton myosin light of rat uterine smooth muscle
    • Haeberle JR, Hott JW, and Hathaway DR. Regulation of isometric force and isotonic shortening velocity by phosphorylation of the 20,000-dalton myosin light of rat uterine smooth muscle. Pflügers Arch 403: 215-219, 1985.
    • (1985) Pflügers Arch , vol.403 , pp. 215-219
    • Haeberle, J.R.1    Hott, J.W.2    Hathaway, D.R.3
  • 23
    • 0023607764 scopus 로고
    • Intracellular calcium levels in phorbol ester-induced contractions of vascular muscle
    • Jiang MJ and Morgan KG. Intracellular calcium levels in phorbol ester-induced contractions of vascular muscle. Am J Physiol Heart Circ Physiol 253: H1365-H1371, 1987.
    • (1987) Am J Physiol Heart Circ Physiol , vol.253
    • Jiang, M.J.1    Morgan, K.G.2
  • 24
    • 0024554764 scopus 로고
    • Agonist-specific myosin phosphorylation and intracellular calcium during isometric contractions of arterial smooth muscle
    • Jiang MJ and Morgan KG. Agonist-specific myosin phosphorylation and intracellular calcium during isometric contractions of arterial smooth muscle. Pflügers Arch 413: 637-643, 1989.
    • (1989) Pflügers Arch , vol.413 , pp. 637-643
    • Jiang, M.J.1    Morgan, K.G.2
  • 25
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm KE and Stull JT. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu Rev Pharmacol Toxicol 25: 593-620, 1985.
    • (1985) Annu Rev Pharmacol Toxicol , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 26
    • 0028855043 scopus 로고
    • Agonist and membrane depolarization induced activation of MAP kinase in the swine carotid artery
    • Katoch SS and Moreland RS. Agonist and membrane depolarization induced activation of MAP kinase in the swine carotid artery. Am J Physiol Heart Circ Physiol 269: H222-H229, 1995.
    • (1995) Am J Physiol Heart Circ Physiol , vol.269
    • Katoch, S.S.1    Moreland, R.S.2
  • 27
    • 0026695761 scopus 로고
    • Regulation of vascular smooth muscle tone by caldesmon
    • Katsuyama H, Wang CL, and Morgan KG. Regulation of vascular smooth muscle tone by caldesmon. J Biol Chem 267: 14555-14558, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 14555-14558
    • Katsuyama, H.1    Wang, C.L.2    Morgan, K.G.3
  • 30
    • 0033044419 scopus 로고    scopus 로고
    • erk mitogen-activated protein kinase in vitro and demonstration of another caldesmon kinase in intact gizzard smooth muscle
    • erk mitogen-activated protein kinase in vitro and demonstration of another caldesmon kinase in intact gizzard smooth muscle. FEBS Lett 452: 254-258, 1999.
    • (1999) FEBS Lett , vol.452 , pp. 254-258
    • Krymsky, M.A.1    Chibalina, M.V.2    Shirinsky, V.P.3    Marston, S.B.4    Vorotnikov, A.V.5
  • 32
    • 0030868556 scopus 로고    scopus 로고
    • Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle
    • Menice CB, Hulvershorn J, Adam LP, Wang CA, and Morgan KG. Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle. J Biol Chem 272: 25157-25161, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 25157-25161
    • Menice, C.B.1    Hulvershorn, J.2    Adam, L.P.3    Wang, C.A.4    Morgan, K.G.5
  • 33
    • 0034921574 scopus 로고    scopus 로고
    • Cross-bridge regulation by thin filament-associated proteins
    • Morgan KG and Gangopadhyay SS. Cross-bridge regulation by thin filament-associated proteins. J Appl Physiol 91: 953-962, 2001.
    • (2001) J Appl Physiol , vol.91 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 35
    • 0028350569 scopus 로고
    • What is special about smooth muscle? The significance of covalent crossbridge regulation
    • Murphy RA. What is special about smooth muscle? The significance of covalent crossbridge regulation. FASEB J 8: 311-318, 1994.
    • (1994) FASEB J , vol.8 , pp. 311-318
    • Murphy, R.A.1
  • 36
    • 0021718452 scopus 로고
    • 2+-ATPase activity by caldesmon
    • 2+-ATPase activity by caldesmon. J Biol Chem 259: 13656-13659, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 13656-13659
    • Ngai, P.K.1    Walsh, M.P.2
  • 39
    • 0034976775 scopus 로고    scopus 로고
    • Regulation of myosin phosphorylation in smooth muscle
    • Pfitzer G. Regulation of myosin phosphorylation in smooth muscle. J Appl Physiol 91: 497-503, 2001.
    • (2001) J Appl Physiol , vol.91 , pp. 497-503
    • Pfitzer, G.1
  • 41
    • 0024226712 scopus 로고
    • 2+]-dependent myosin phosphorylation in phorbol diester-stimulated smooth muscle contraction
    • 2+]-dependent myosin phosphorylation in phorbol diester-stimulated smooth muscle contraction. Am J Physiol Cell Physiol 255: C719-C723, 1988.
    • (1988) Am J Physiol Cell Physiol , vol.255
    • Rembold, C.M.1    Murphy, R.A.2
  • 44
    • 0023572362 scopus 로고
    • Calcium dependence of phorbol 12,13-dibutyrate-induced force and myosin light chain phosphorylation in arterial smooth muscle
    • Singer HA and Baker KM. Calcium dependence of phorbol 12,13-dibutyrate-induced force and myosin light chain phosphorylation in arterial smooth muscle. J Pharmacol Exp Ther 243: 814-821, 1987.
    • (1987) J Pharmacol Exp Ther , vol.243 , pp. 814-821
    • Singer, H.A.1    Baker, K.M.2
  • 45
    • 0025900837 scopus 로고
    • Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
    • Sobue K and Sellers JR. Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J Biol Chem 266: 12115-12118, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 12115-12118
    • Sobue, K.1    Sellers, J.R.2
  • 46
    • 0033538641 scopus 로고    scopus 로고
    • Two distinct mechanisms mediate a differential regulation of protein kinase C isozymes in acute and prolonged myocardial ischemia
    • Strasser RH, Simonis G, Schon SP, Braun MU, Ihl-Vahl R, Weinbrenner C, Marquetant R, and Kubler W. Two distinct mechanisms mediate a differential regulation of protein kinase C isozymes in acute and prolonged myocardial ischemia. Circ Res 85: 77-87, 1999.
    • (1999) Circ Res , vol.85 , pp. 77-87
    • Strasser, R.H.1    Simonis, G.2    Schon, S.P.3    Braun, M.U.4    Ihl-Vahl, R.5    Weinbrenner, C.6    Marquetant, R.7    Kubler, W.8
  • 47
    • 0025274050 scopus 로고
    • Phosphorylation by protein kinase C of the 20,000-dalton light chain of myosin in intact and chemically skinned vascular smooth muscle
    • Sutton TA and Haeberle JR. Phosphorylation by protein kinase C of the 20,000-dalton light chain of myosin in intact and chemically skinned vascular smooth muscle. J Biol Chem 265: 2749-2754, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 2749-2754
    • Sutton, T.A.1    Haeberle, J.R.2
  • 48
    • 0025195356 scopus 로고
    • r caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction between actin and myosin
    • r caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction between actin and myosin. Eur J Biochem 188: 495-500, 1990.
    • (1990) Eur J Biochem , vol.188 , pp. 495-500
    • Tanaka, T.1    Ohta, H.2    Kanda, K.3    Tanaka, T.4    Hidaka, H.5    Sobue, K.6
  • 50
    • 0022410617 scopus 로고
    • Phosphorylation of caldesmon by protein kinase C
    • Umekawa H and Hidaka H. Phosphorylation of caldesmon by protein kinase C. Biochem Biophys Res Commun 132: 56-62, 1985.
    • (1985) Biochem Biophys Res Commun , vol.132 , pp. 56-62
    • Umekawa, H.1    Hidaka, H.2
  • 52
    • 0030434253 scopus 로고    scopus 로고
    • Serotonin activates the mitogen-activated protein kinase pathway in vascular smooth muscle: Use of the mitogen-activated protein kinase inhibitor PD098059
    • Watts SW. Serotonin activates the mitogen-activated protein kinase pathway in vascular smooth muscle: use of the mitogen-activated protein kinase inhibitor PD098059. J Pharmacol Exp Ther 279: 1541-1550, 1996.
    • (1996) J Pharmacol Exp Ther , vol.279 , pp. 1541-1550
    • Watts, S.W.1
  • 54
    • 0027239788 scopus 로고
    • Contractile elements and myosin light chain phosphorylation in myometrial tissue from non-pregnant and pregnant women
    • Word RA, Stull JT, Casey ML, and Kamm KE. Contractile elements and myosin light chain phosphorylation in myometrial tissue from non-pregnant and pregnant women. J Clin Invest 92: 29-37, 1993.
    • (1993) J Clin Invest , vol.92 , pp. 29-37
    • Word, R.A.1    Stull, J.T.2    Casey, M.L.3    Kamm, K.E.4
  • 55
    • 0036086110 scopus 로고    scopus 로고
    • ERK MAP kinases regulate smooth muscle contraction in ovine uterine artery: Effect of pregnancy
    • Xiao DL and Zhang L. ERK MAP kinases regulate smooth muscle contraction in ovine uterine artery: effect of pregnancy. Am J Physiol Heart Circ Physiol 282: H292-H300, 2002.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282
    • Xiao, D.L.1    Zhang, L.2
  • 57
    • 0141523109 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases and contractile responses in ovine adult and fetal cerebral arteries
    • Zhao Y, Long W, Zhang L, and Longo LD. Extracellular signal-regulated kinases and contractile responses in ovine adult and fetal cerebral arteries. J Physiol 551: 691-703, 2003.
    • (2003) J Physiol , vol.551 , pp. 691-703
    • Zhao, Y.1    Long, W.2    Zhang, L.3    Longo, L.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.