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Volumn 115, Issue 3 SUPPL. 1, 2003, Pages 15-23

Function of gastrointestinal smooth muscle: From signaling to contractile proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM ION; CALMODULIN; CALPONIN; CONTRACTILE PROTEIN; F ACTIN; G ACTIN; G PROTEIN COUPLED RECEPTOR; GLOBULAR PROTEIN; HEAT SHOCK PROTEIN 27; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; PHOSPHATASE; PHOSPHOLIPASE A2; PHOSPHOLIPASE C; PHOSPHOLIPASE D; PROTEIN KINASE C; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TROPOMYOSIN;

EID: 0042158731     PISSN: 00029343     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9343(03)00189-X     Document Type: Conference Paper
Times cited : (48)

References (78)
  • 2
    • 0024459688 scopus 로고
    • Cell calcium and its regulation in smooth muscle
    • Somlyo A.P., Himpens B. Cell calcium and its regulation in smooth muscle. FASEB J. 3:1989;2266-2276.
    • (1989) FASEB J , vol.3 , pp. 2266-2276
    • Somlyo, A.P.1    Himpens, B.2
  • 3
    • 0030976303 scopus 로고    scopus 로고
    • Signal transduction in gastrointestinal smooth muscle
    • Makhlouf G.M., Murthy K.S. Signal transduction in gastrointestinal smooth muscle. Cell Signal. 9:1997;269-276.
    • (1997) Cell Signal , vol.9 , pp. 269-276
    • Makhlouf, G.M.1    Murthy, K.S.2
  • 4
    • 0025646390 scopus 로고
    • Differential regulation of smooth muscle contraction in rabbit internal anal sphincter by substance P and bombesin
    • Bitar K.N., Hillemeier C., Biancani P., Balazovich K.J. Differential regulation of smooth muscle contraction in rabbit internal anal sphincter by substance P and bombesin. Life Sci. 47:1990;2429-2434.
    • (1990) Life Sci , vol.47 , pp. 2429-2434
    • Bitar, K.N.1    Hillemeier, C.2    Biancani, P.3    Balazovich, K.J.4
  • 5
    • 0025763083 scopus 로고
    • Regulation of smooth muscle contraction in rabbit internal anal sphincter by protein kinase C and Ins(1,4,5)P3
    • Bitar K.N., Hillemeier C., Biancani P., Balazovich K.J. Regulation of smooth muscle contraction in rabbit internal anal sphincter by protein kinase C and Ins(1,4,5)P3. Am J Physiol. 260:(Pt 1):1991;G537-G542.
    • (1991) Am J Physiol , vol.260 , Issue.1 PART
    • Bitar, K.N.1    Hillemeier, C.2    Biancani, P.3    Balazovich, K.J.4
  • 6
    • 0031754498 scopus 로고    scopus 로고
    • Src kinase and PI 3-kinase as a transduction pathway in ceramide-induced contraction of colonic smooth muscle
    • Ibitayo A.I., Tsunoda Y., Nozu F., Owyang C., Bitar K.N. Src kinase and PI 3-kinase as a transduction pathway in ceramide-induced contraction of colonic smooth muscle. Am J Physiol. 38:1998;G705-G711.
    • (1998) Am J Physiol , vol.38
    • Ibitayo, A.I.1    Tsunoda, Y.2    Nozu, F.3    Owyang, C.4    Bitar, K.N.5
  • 7
    • 0023626217 scopus 로고
    • Protein kinase C in the regulation of smooth muscle contraction
    • Rasmussen H., Takuwa Y., Park S. Protein kinase C in the regulation of smooth muscle contraction. FASEB J. 1:1987;177-185.
    • (1987) FASEB J , vol.1 , pp. 177-185
    • Rasmussen, H.1    Takuwa, Y.2    Park, S.3
  • 8
    • 0026687225 scopus 로고
    • Protein kinase C of smooth muscle
    • Andrea J.E., Walsh M.P. Protein kinase C of smooth muscle. Hypertension. 20:1992;585-595.
    • (1992) Hypertension , vol.20 , pp. 585-595
    • Andrea, J.E.1    Walsh, M.P.2
  • 9
    • 0029008523 scopus 로고
    • Kinase activation and smooth muscle contraction in the presence and absence of calcium
    • Whitney G., Throckmorton D., Isales C., et al. Kinase activation and smooth muscle contraction in the presence and absence of calcium. J Vasc Surg. 22:1995;37-44.
    • (1995) J Vasc Surg , vol.22 , pp. 37-44
    • Whitney, G.1    Throckmorton, D.2    Isales, C.3
  • 10
    • 0030760220 scopus 로고    scopus 로고
    • Bombesin-stimulated ceramide production and MAP kinase activation in rabbit rectosigmoid smooth muscle cells
    • Sbrissa D., Yamada H., Hajra A., Bitar K.N. Bombesin-stimulated ceramide production and MAP kinase activation in rabbit rectosigmoid smooth muscle cells. Am J Physiol. 272:(Pt 1):1997;G1615-G1625.
    • (1997) Am J Physiol , vol.272 , Issue.1 PART
    • Sbrissa, D.1    Yamada, H.2    Hajra, A.3    Bitar, K.N.4
  • 11
    • 0023197158 scopus 로고
    • 2+-permeable channel activated by ATP in smooth muscle
    • 2+-permeable channel activated by ATP in smooth muscle. Nature. 328:1987;275-278.
    • (1987) Nature , vol.328 , pp. 275-278
    • Benham, C.D.1    Tsien, R.W.2
  • 14
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves M.A., Holmes K.C. Structural mechanism of muscle contraction. Annu Rev Biochem. 68:1999;687-728.
    • (1999) Annu Rev Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 15
    • 0034921574 scopus 로고    scopus 로고
    • Invited review: Cross-bridge regulation by thin filament-associated proteins
    • Morgan K.G., Gangopadhyay S.S. Invited review cross-bridge regulation by thin filament-associated proteins . J Appl Physiol. 91:2001;953-962.
    • (2001) J Appl Physiol , vol.91 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 16
    • 0030623649 scopus 로고    scopus 로고
    • Contractile protein changes in urinary bladder smooth muscle during obstruction-induced hypertrophy
    • Chacko S., DiSanto M., Wang Z., Zderic S.A., Wein A.J. Contractile protein changes in urinary bladder smooth muscle during obstruction-induced hypertrophy. Scand J Urol Nephrol Suppl. 184:1997;67-76.
    • (1997) Scand J Urol Nephrol Suppl , vol.184 , pp. 67-76
    • Chacko, S.1    DiSanto, M.2    Wang, Z.3    Zderic, S.A.4    Wein, A.J.5
  • 17
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo A.P., Somlyo A.V. Signal transduction and regulation in smooth muscle. Nature. 372:1994;231-236.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 18
    • 0026709998 scopus 로고
    • Control of nonmuscle myosins by phosphorylation
    • Tan J.L., Ravid S., Spudich J.A. Control of nonmuscle myosins by phosphorylation. Annu Rev Biochem. 61:1992;721-759.
    • (1992) Annu Rev Biochem , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 19
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm K.E., Stull J.T. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu Rev Pharmacol Toxicol. 25:1985;593-620.
    • (1985) Annu Rev Pharmacol Toxicol , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 20
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • L.R. Johnson. New York: Raven Press
    • Hartshorne D.J. Biochemistry of the contractile process in smooth muscle. Johnson L.R. Physiology of the Gastrointestinal Tract. 2nd ed:1987;423-482 Raven Press, New York.
    • (1987) Physiology of the Gastrointestinal Tract 2nd Ed , pp. 423-482
    • Hartshorne, D.J.1
  • 23
    • 0026806485 scopus 로고
    • Arachidonic acid inhibits myosin light chain phosphatase and sensitizes smooth muscle to calcium
    • Gong M.C., Fuglsang A., Alessi D., et al. Arachidonic acid inhibits myosin light chain phosphatase and sensitizes smooth muscle to calcium. J Biol Chem. 267:1992;21492-21498.
    • (1992) J Biol Chem , vol.267 , pp. 21492-21498
    • Gong, M.C.1    Fuglsang, A.2    Alessi, D.3
  • 24
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D. Localization of protein kinases by anchoring proteins a theme in signal transduction . Science. 268:1995;247-251.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 25
    • 0026739870 scopus 로고
    • Phenylephrine-induced translocation of protein kinase C and shortening of two types of vascular cells of the ferret
    • Khalil R.A., Morgan K.G. Phenylephrine-induced translocation of protein kinase C and shortening of two types of vascular cells of the ferret. J Physiol. 455:1992;585-599.
    • (1992) J Physiol , vol.455 , pp. 585-599
    • Khalil, R.A.1    Morgan, K.G.2
  • 26
    • 0036092538 scopus 로고    scopus 로고
    • Hsp27 modulates agonist-induced association of translocated RhoA and PKC-α in muscle cells of the colon
    • Bitar K.N., Ibitayo A., Patil S.B. Hsp27 modulates agonist-induced association of translocated RhoA and PKC-α in muscle cells of the colon. J Appl Physiol. 92:2002;41-49.
    • (2002) J Appl Physiol , vol.92 , pp. 41-49
    • Bitar, K.N.1    Ibitayo, A.2    Patil, S.B.3
  • 27
    • 0032858218 scopus 로고    scopus 로고
    • Hsp27 in signal transduction and association with contractile proteins in smooth muscle cells
    • Ibitayo A.I., Sladick J., Tuteja S., et al. Hsp27 in signal transduction and association with contractile proteins in smooth muscle cells. Am J Physiol. 277:1999;G445-G454.
    • (1999) Am J Physiol , vol.277
    • Ibitayo, A.I.1    Sladick, J.2    Tuteja, S.3
  • 28
    • 0036083316 scopus 로고    scopus 로고
    • Hsp27 phosphorylation and interaction with actin-myosin in smooth muscle contraction
    • Bitar K.N. Hsp27 phosphorylation and interaction with actin-myosin in smooth muscle contraction. Am J Physiol. 282:2002;G894-G903.
    • (2002) Am J Physiol , vol.282
    • Bitar, K.N.1
  • 29
    • 0028168041 scopus 로고
    • 2+ sensitizing effect of protein kinase C on vascular smooth muscle: Inhibition of myosin light chain phosphatase
    • 2+ sensitizing effect of protein kinase C on vascular smooth muscle inhibition of myosin light chain phosphatase . J Gen Physiol. 104:1994;265-286.
    • (1994) J Gen Physiol , vol.104 , pp. 265-286
    • Masuo, M.1    Reardon, S.2    Ikebe, M.3    Kitazawa, T.4
  • 30
    • 0030583303 scopus 로고    scopus 로고
    • Protein kinase C increases force and slows relaxation in smooth muscle: Evidence for regulation of the myosin light chain phosphatase
    • Ikebe M., Brozovich F.V. Protein kinase C increases force and slows relaxation in smooth muscle evidence for regulation of the myosin light chain phosphatase . Biochem Biophys Res Commun. 14:1996;370-376.
    • (1996) Biochem Biophys Res Commun , vol.14 , pp. 370-376
    • Ikebe, M.1    Brozovich, F.V.2
  • 31
    • 0033214346 scopus 로고    scopus 로고
    • 2+ sensitization in Triton X-100 demembranated rabbit arterial smooth muscle
    • 2+ sensitization in Triton X-100 demembranated rabbit arterial smooth muscle. J Physiol. 520:1999;139-152.
    • (1999) J Physiol , vol.520 , pp. 139-152
    • Kitazawa, T.1    Takizawa, N.2    Ikebe, M.3    Eto, M.4
  • 32
    • 0029583638 scopus 로고
    • A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization
    • Eto M., Ohmori T., Suzuki M., Furuya K., Morita F. A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J Biochem. 118:1995;1104-1107.
    • (1995) J Biochem , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 33
    • 0034616292 scopus 로고    scopus 로고
    • Agonists trigger G protein-mediated activation of the CPI17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility
    • Kitazawa T., Eto M., Woodsome T.P., Brautigan D.L. Agonists trigger G protein-mediated activation of the CPI17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J Biol Chem. 275:2000;9897-9900.
    • (2000) J Biol Chem , vol.275 , pp. 9897-9900
    • Kitazawa, T.1    Eto, M.2    Woodsome, T.P.3    Brautigan, D.L.4
  • 34
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, Rho-kinase, and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo A.P., Somlyo A.V. Signal transduction by G-proteins, Rho-kinase, and protein phosphatase to smooth muscle and non-muscle myosin II. J Physiol. 522:2000;177-185.
    • (2000) J Physiol , vol.522 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 35
    • 0028152923 scopus 로고
    • Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme: The differential effects of the holoenzyme and its subunits on smooth muscle
    • Shirazi H., Iizuka K., Fadden P., et al. Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme the differential effects of the holoenzyme and its subunits on smooth muscle . J Biol Chem. 269:1994;31598-31606.
    • (1994) J Biol Chem , vol.269 , pp. 31598-31606
    • Shirazi, H.1    Iizuka, K.2    Fadden, P.3
  • 36
    • 0027972853 scopus 로고
    • Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase
    • Shimizu H., Ito M., Miyahara M., et al. Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase. J Biol Chem. 269:1994;30407-30411.
    • (1994) J Biol Chem , vol.269 , pp. 30407-30411
    • Shimizu, H.1    Ito, M.2    Miyahara, M.3
  • 37
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targeting subunits: The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi D., MacDougall L.K., Sola M.M., Ikebe M., Cohen P. The control of protein phosphatase-1 by targeting subunits the major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1 . Eur J Biochem. 210:1992;1023-1035.
    • (1992) Eur J Biochem , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 38
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura K., Ito M., Amano M., et al. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science. 273:1996;245-248.
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2    Amano, M.3
  • 39
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng J., Ito M., Ichikawa K., et al. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J Biol Chem. 274:1999;37385-37390.
    • (1999) J Biol Chem , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3
  • 40
    • 0027404913 scopus 로고
    • Intracellular cyclic GMP receptor proteins
    • Lincoln T.M., Cornwell T.L. Intracellular cyclic GMP receptor proteins. FASEB J. 7:1993;328-338.
    • (1993) FASEB J , vol.7 , pp. 328-338
    • Lincoln, T.M.1    Cornwell, T.L.2
  • 41
    • 0032848914 scopus 로고    scopus 로고
    • Cyclic nucleotide-dependent protein kinases: Intracellular receptors for cAMP and cGMP action
    • Francis S.H., Corbin J.D. Cyclic nucleotide-dependent protein kinases intracellular receptors for cAMP and cGMP action . Crit Rev Clin Lab Sci. 36:1999;275-328.
    • (1999) Crit Rev Clin Lab Sci , vol.36 , pp. 275-328
    • Francis, S.H.1    Corbin, J.D.2
  • 43
    • 0033584786 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase I alpha
    • Surks H.K., Mochizuki N., Kasai Y., et al. Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase I alpha. Science. 286:1999;1583-1587.
    • (1999) Science , vol.286 , pp. 1583-1587
    • Surks, H.K.1    Mochizuki, N.2    Kasai, Y.3
  • 44
    • 0034683163 scopus 로고    scopus 로고
    • Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle
    • MacDonald J.A., Walker L.A., Nakamoto R.K., et al. Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle. FEBS Lett. 479:2000;83-88.
    • (2000) FEBS Lett , vol.479 , pp. 83-88
    • MacDonald, J.A.1    Walker, L.A.2    Nakamoto, R.K.3
  • 45
    • 0031057516 scopus 로고    scopus 로고
    • Cyclic GMP causes Ca2+ desensitization in vascular smooth muscle by activating the myosin light chain phosphatase
    • Lee M.R., Li L., Kitazawa T. Cyclic GMP causes Ca2+ desensitization in vascular smooth muscle by activating the myosin light chain phosphatase. J Biol Chem. 272:1997;5063-5068.
    • (1997) J Biol Chem , vol.272 , pp. 5063-5068
    • Lee, M.R.1    Li, L.2    Kitazawa, T.3
  • 46
    • 0034925225 scopus 로고    scopus 로고
    • Invited review: Focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle
    • Gerthoffer W.T., Gunst S.J. Invited review focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle . J Appl Physiol. 91:2001;963-972.
    • (2001) J Appl Physiol , vol.91 , pp. 963-972
    • Gerthoffer, W.T.1    Gunst, S.J.2
  • 47
    • 0032617026 scopus 로고    scopus 로고
    • Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)
    • Landry J., Huot J. Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27). Biochem Soc Symp. 64:1999;79-89.
    • (1999) Biochem Soc Symp , vol.64 , pp. 79-89
    • Landry, J.1    Huot, J.2
  • 49
    • 0033869960 scopus 로고    scopus 로고
    • The macromolecular associations of heat shock protein-27 in vascular smooth muscle
    • Brophy C.M., Molinaro J.R., Dickinson M. The macromolecular associations of heat shock protein-27 in vascular smooth muscle. Surgery. 128:2000;320-326.
    • (2000) Surgery , vol.128 , pp. 320-326
    • Brophy, C.M.1    Molinaro, J.R.2    Dickinson, M.3
  • 50
    • 0028832107 scopus 로고
    • Characterization of 45-kDa/54-kDa Hsp27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein Hsp27
    • Huot J., Lambert H., Lavoie J.N., Guimond A., Houle F., Landry J. Characterization of 45-kDa/54-kDa Hsp27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein Hsp27. Eur J Biochem. 227:1995;416-427.
    • (1995) Eur J Biochem , vol.227 , pp. 416-427
    • Huot, J.1    Lambert, H.2    Lavoie, J.N.3    Guimond, A.4    Houle, F.5    Landry, J.6
  • 51
    • 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
    • Landry J., Lambert H., Zhou M., et al. 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;794-803.
    • (1992) J Biol Chem , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3
  • 52
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J., Cohen P., Trigon S., et al. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell. 78:1994;1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3
  • 53
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313:1992;307-313.
    • (1992) FEBS Lett , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 55
    • 0033864990 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle
    • Yamboliev I., Wiesmann K., Singer C., Hedges J., Gerthoffer W. Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle. Am J Physiol. 279:2000;C352-C360.
    • (2000) Am J Physiol , vol.279
    • Yamboliev, I.1    Wiesmann, K.2    Singer, C.3    Hedges, J.4    Gerthoffer, W.5
  • 56
    • 0027093717 scopus 로고
    • Actin mediated regulation of muscle contraction
    • [review]
    • Chalovich J.M. Actin mediated regulation of muscle contraction. [review] Pharmacol Ther. 55:1992;95-148.
    • (1992) Pharmacol Ther , vol.55 , pp. 95-148
    • Chalovich, J.M.1
  • 57
    • 0027749388 scopus 로고
    • Calponin: Thin filament-linked regulation of smooth muscle contraction
    • Winder S.J., Walsh M.P. Calponin thin filament-linked regulation of smooth muscle contraction . Cell Signal. 5:1993;677-686.
    • (1993) Cell Signal , vol.5 , pp. 677-686
    • Winder, S.J.1    Walsh, M.P.2
  • 58
    • 0028335358 scopus 로고
    • Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in an in vitro motility assay
    • Haeberle J.R. Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in an in vitro motility assay. J Biol Chem. 269:1994;12424-12431.
    • (1994) J Biol Chem , vol.269 , pp. 12424-12431
    • Haeberle, J.R.1
  • 59
    • 0025140416 scopus 로고
    • Inhibition of the actomyosin MgATPase by chicken gizzard calponin
    • Winder S., Walsh M. Inhibition of the actomyosin MgATPase by chicken gizzard calponin. Prog Clin Biol Res. 327:1990;141-148.
    • (1990) Prog Clin Biol Res , vol.327 , pp. 141-148
    • Winder, S.1    Walsh, M.2
  • 60
    • 0025817957 scopus 로고
    • Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle
    • Malmqvist U., Arner A. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Pflugers Arch. 418:1991;523-530.
    • (1991) Pflugers Arch , vol.418 , pp. 523-530
    • Malmqvist, U.1    Arner, A.2
  • 61
    • 0035875161 scopus 로고    scopus 로고
    • 2+ sensitization of guinea pig ileum contractility is not mediated by Rho-associated kinase
    • 2+ sensitization of guinea pig ileum contractility is not mediated by Rho-associated kinase. J Physiol. 533:(Pt 3):2001;651-664.
    • (2001) J Physiol , vol.533 , Issue.3 PART , pp. 651-664
    • Pfitzer, G.1    Sonntag-Bensch, D.2    Brkic-Koric, D.3
  • 62
    • 0028057169 scopus 로고
    • Agonist-induced redistribution of calponin in contractile vascular smooth muscle cells
    • Parker C.A., Takahashi K., Tao T., Morgan K.G. Agonist-induced redistribution of calponin in contractile vascular smooth muscle cells. Am J Physiol. 267:1994;C1262-C1270.
    • (1994) Am J Physiol , vol.267
    • Parker, C.A.1    Takahashi, K.2    Tao, T.3    Morgan, K.G.4
  • 63
    • 0032055970 scopus 로고    scopus 로고
    • Cytoskeletal targeting of calponin in differentiated, contractile smooth muscle cells of the ferret
    • Parker C.A., Takahashi K., Tang J.X., Tao T., Morgan K.G. Cytoskeletal targeting of calponin in differentiated, contractile smooth muscle cells of the ferret. J Physiol. 508:(Pt 1):1998;187-198.
    • (1998) J Physiol , vol.508 , Issue.1 PART , pp. 187-198
    • Parker, C.A.1    Takahashi, K.2    Tang, J.X.3    Tao, T.4    Morgan, K.G.5
  • 65
    • 0025879757 scopus 로고
    • Molecular cloning and sequence analysis of smooth muscle calponin
    • Takahashi K., Nadal-Ginard B. Molecular cloning and sequence analysis of smooth muscle calponin. J Biol Chem. 266:1991;13284-13288.
    • (1991) J Biol Chem , vol.266 , pp. 13284-13288
    • Takahashi, K.1    Nadal-Ginard, B.2
  • 66
    • 0027283067 scopus 로고
    • Mammalian calponin: Identification and expression of genetic variants
    • Strasser P., Gimona M., Moessler H., Herzog M., Small J.V. Mammalian calponin identification and expression of genetic variants . FEBS Lett. 330:1993;13-18.
    • (1993) FEBS Lett , vol.330 , pp. 13-18
    • Strasser, P.1    Gimona, M.2    Moessler, H.3    Herzog, M.4    Small, J.V.5
  • 67
    • 0028365640 scopus 로고
    • Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle
    • Applegate D., Feng W., Green R.S., Taubman M.B. Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle. J Biol Chem. 269:1994;10683-10690.
    • (1994) J Biol Chem , vol.269 , pp. 10683-10690
    • Applegate, D.1    Feng, W.2    Green, R.S.3    Taubman, M.B.4
  • 68
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation
    • Kasuga M. Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation. Mol Cell Biol. 14:1994;6674-6682.
    • (1994) Mol Cell Biol , vol.14 , pp. 6674-6682
    • Kasuga, M.1
  • 70
    • 0027460282 scopus 로고
    • Identification of the regulatory site in smooth muscle calponin that is phosphorylated by protein kinase C
    • Nakamura F., Mino T., Yamamoto J., Naka M., Tanaka T. Identification of the regulatory site in smooth muscle calponin that is phosphorylated by protein kinase C. J Biol Chem. 268:1993;6194-6201.
    • (1993) J Biol Chem , vol.268 , pp. 6194-6201
    • Nakamura, F.1    Mino, T.2    Yamamoto, J.3    Naka, M.4    Tanaka, T.5
  • 71
    • 0034704107 scopus 로고    scopus 로고
    • Regulation of protein kinase C by the cytoskeletal protein calponin
    • Leinweber B., Parissenti A.M., Gallant C., et al. Regulation of protein kinase C by the cytoskeletal protein calponin. J Biol Chem. 275:2000;40329-40336.
    • (2000) J Biol Chem , vol.275 , pp. 40329-40336
    • Leinweber, B.1    Parissenti, A.M.2    Gallant, C.3
  • 72
    • 0034709570 scopus 로고    scopus 로고
    • Identification of calponin as a novel substrate of Rho-kinase
    • Kaneko T., Amano M., Maeda A., et al. Identification of calponin as a novel substrate of Rho-kinase. Biochem Biophys Res Commun. 273:2000;110-116.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 110-116
    • Kaneko, T.1    Amano, M.2    Maeda, A.3
  • 73
    • 0033571710 scopus 로고    scopus 로고
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins
    • Leinweber B.D., Leavis P.C., Grabarek Z., Wang C.L., Morgan K.G. Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Biochem J. 344:(Pt 1):1999;117-123.
    • (1999) Biochem J , vol.344 , Issue.1 PART , pp. 117-123
    • Leinweber, B.D.1    Leavis, P.C.2    Grabarek, Z.3    Wang, C.L.4    Morgan, K.G.5
  • 74
    • 0030923431 scopus 로고    scopus 로고
    • Association of calponin with desmin intermediate filaments
    • Mabuchi K., Li B., Ip W., Tao T. Association of calponin with desmin intermediate filaments. J Biol Chem. 272:1997;22662-22666.
    • (1997) J Biol Chem , vol.272 , pp. 22662-22666
    • Mabuchi, K.1    Li, B.2    Ip, W.3    Tao, T.4
  • 75
    • 0022930623 scopus 로고
    • Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle
    • Takahashi K., Hiwada K., Kokubu T. Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle. Biochem Biophys Res Commun. 141:1986;20-26.
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 20-26
    • Takahashi, K.1    Hiwada, K.2    Kokubu, T.3
  • 76
    • 0032446186 scopus 로고    scopus 로고
    • The cytoskeleton of the vertebrate smooth muscle cell
    • Small J.V., Gimona M. The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol Scand. 164:1998;341-348.
    • (1998) Acta Physiol Scand , vol.164 , pp. 341-348
    • Small, J.V.1    Gimona, M.2
  • 77
    • 0032878503 scopus 로고    scopus 로고
    • Localization of calponin binding sites in the structure of 90 kDa heat shock protein (Hsp90)
    • Bogatcheva N.V., Ma Y., Urosev D., Gusev N.B. Localization of calponin binding sites in the structure of 90 kDa heat shock protein (Hsp90). FEBS Lett. 457:1999;369-374.
    • (1999) FEBS Lett , vol.457 , pp. 369-374
    • Bogatcheva, N.V.1    Ma, Y.2    Urosev, D.3    Gusev, N.B.4
  • 78
    • 0029070922 scopus 로고
    • Interaction of calponin with phospholipids
    • Fujii T., Yamana K., Ogoma Y., Kondo Y. Interaction of calponin with phospholipids. J Biochem. 117:1995;999-1003.
    • (1995) J Biochem , vol.117 , pp. 999-1003
    • Fujii, T.1    Yamana, K.2    Ogoma, Y.3    Kondo, Y.4


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