메뉴 건너뛰기




Volumn 101, Issue 4, 2006, Pages 1189-1198

A mechanical model for adjustable passive stiffness in rabbit detrusor

Author keywords

Muscle model; Passive force; Preconditioning; Smooth muscle mechanics; Strain softening

Indexed keywords

CALDESMON; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 33749324251     PISSN: 87507587     EISSN: 15221601     Source Type: Journal    
DOI: 10.1152/japplphysiol.00396.2006     Document Type: Article
Times cited : (29)

References (45)
  • 1
    • 0032066417 scopus 로고    scopus 로고
    • Constitutive modeling of the large strain time-dependent behavior of elastomers
    • Bergstrom JS and Boyce MC. Constitutive modeling of the large strain time-dependent behavior of elastomers. J Mech Phys Solids 46: 931-954, 1998.
    • (1998) J Mech Phys Solids , vol.46 , pp. 931-954
    • Bergstrom, J.S.1    Boyce, M.C.2
  • 2
    • 0347021167 scopus 로고
    • Rigor and resistance to stretch in vertebrate smooth muscle
    • Butler TM, Siegman MJ, and Davies RE. Rigor and resistance to stretch in vertebrate smooth muscle. Am J Physiol 231: 1509-1514, 1976.
    • (1976) Am J Physiol , vol.231 , pp. 1509-1514
    • Butler, T.M.1    Siegman, M.J.2    Davies, R.E.3
  • 3
    • 0032142998 scopus 로고    scopus 로고
    • A cross-bridge mechanism can explain the thixotropic short-range elastic component of relaxed frog skeletal muscle
    • Campbell KS and Lakie M. A cross-bridge mechanism can explain the thixotropic short-range elastic component of relaxed frog skeletal muscle. J Physiol 510: 941-962, 1998.
    • (1998) J Physiol , vol.510 , pp. 941-962
    • Campbell, K.S.1    Lakie, M.2
  • 6
    • 0035844257 scopus 로고    scopus 로고
    • 2+-independent smooth muscle contraction: A novel function for integrin-linked kinase
    • 2+-independent smooth muscle contraction: a novel function for integrin-linked kinase. J Biol Chem 276: 16365-16373, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 16365-16373
    • Deng, J.T.1    Van Lierop, J.E.2    Sutherland, C.3    Walsh, M.P.4
  • 7
    • 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
  • 8
    • 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 RA. 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.A.3
  • 9
    • 0031080448 scopus 로고    scopus 로고
    • Strain softening in rat left ventricular myocardium
    • Emery JL, Omens JH, and McCulloch AD. Strain softening in rat left ventricular myocardium. J Biomech Eng 119: 6-12, 1997.
    • (1997) J Biomech Eng , vol.119 , pp. 6-12
    • Emery, J.L.1    Omens, J.H.2    McCulloch, A.D.3
  • 11
    • 0004280575 scopus 로고
    • New York: Springer-Verlag
    • Fung YC. Biomechanics. New York: Springer-Verlag, 1993.
    • (1993) Biomechanics
    • Fung, Y.C.1
  • 12
    • 1242294530 scopus 로고    scopus 로고
    • Caldesmon phosphorylation is catalyzed by two kinases in permeabilized and intact vascular smooth muscle
    • Gorenne I, Su X, and Moreland RS. Caldesmon phosphorylation is catalyzed by two kinases in permeabilized and intact vascular smooth muscle. J Cell Physiol 198: 461-469, 2004.
    • (2004) J Cell Physiol , vol.198 , pp. 461-469
    • Gorenne, I.1    Su, X.2    Moreland, R.S.3
  • 13
    • 0032158574 scopus 로고    scopus 로고
    • History-dependent mechanical behavior of guinea-pig small intestine
    • Gregersen H, Emery JL, and McCulloch AD. History-dependent mechanical behavior of guinea-pig small intestine. Ann Biomed Eng 26: 850-858, 1998.
    • (1998) Ann Biomed Eng , vol.26 , pp. 850-858
    • Gregersen, H.1    Emery, J.L.2    McCulloch, A.D.3
  • 14
    • 0029071331 scopus 로고
    • Mechanisms for the mechanical plasticity of tracheal smooth muscle
    • Gunst SJ, Meiss RA, Wu MF, and Rowe M. Mechanisms for the mechanical plasticity of tracheal smooth muscle. Am J Physiol Cell Physiol 268: C1267-C1276, 1995.
    • (1995) Am J Physiol Cell Physiol , vol.268
    • Gunst, S.J.1    Meiss, R.A.2    Wu, M.F.3    Rowe, M.4
  • 15
    • 0035140711 scopus 로고    scopus 로고
    • Selected contribution: Plasticity of airway smooth muscle stiffness and extensibility: Role of length-adaptive mechanisms
    • Gunst SJ and Wu MF. Selected contribution: plasticity of airway smooth muscle stiffness and extensibility: role of length-adaptive mechanisms. J Appl Physiol 90: 741-749, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 741-749
    • Gunst, S.J.1    Wu, M.F.2
  • 16
    • 0015791892 scopus 로고
    • Length-tension relationship of smooth muscle of the hog carotid artery
    • Herlihy JT and Murphy RA. Length-tension relationship of smooth muscle of the hog carotid artery. Circ Res 33: 257-283, 1973.
    • (1973) Circ Res , vol.33 , pp. 257-283
    • Herlihy, J.T.1    Murphy, R.A.2
  • 17
    • 0034846777 scopus 로고    scopus 로고
    • Dependency of detrusor contractions on calcium sensitization and calcium entry through LOE-908-sensitive channels
    • Jezior JR, Brady JD, Rosenstein DI, McCammon KA, Miner AS, and Ratz PH. Dependency of detrusor contractions on calcium sensitization and calcium entry through LOE-908-sensitive channels. Br J Pharmacol 134: 78-87, 2001.
    • (2001) Br J Pharmacol , vol.134 , pp. 78-87
    • Jezior, J.R.1    Brady, J.D.2    Rosenstein, D.I.3    McCammon, K.A.4    Miner, A.S.5    Ratz, P.H.6
  • 18
    • 0037033791 scopus 로고    scopus 로고
    • Smitin, a novel smooth muscle titin-like protein, interacts with myosin filaments in vivo and in vitro
    • Kim K and Keller TC 3rd. Smitin, a novel smooth muscle titin-like protein, interacts with myosin filaments in vivo and in vitro. J Cell Biol 156: 101-111, 2002.
    • (2002) J Cell Biol , vol.156 , pp. 101-111
    • Kim, K.1    Keller III, T.C.2
  • 19
    • 0030894659 scopus 로고    scopus 로고
    • Effect of pressurization on mechanical properties of mesenteric small arteries from spontaneously hypertensive rats
    • Laurant P, Touyz RM, and Schiffrin EL. Effect of pressurization on mechanical properties of mesenteric small arteries from spontaneously hypertensive rats. J Vasc Res 34: 117-125, 1997.
    • (1997) J Vasc Res , vol.34 , pp. 117-125
    • Laurant, P.1    Touyz, R.M.2    Schiffrin, E.L.3
  • 22
    • 0038121457 scopus 로고    scopus 로고
    • Bladder smooth muscle cell phenotypic changes and implication of expression of contractile proteins (especially caldesmon) in rats after partial outlet obstruction
    • Matsumoto S, Hanai T, Ohnishi N, Yamamoto K, and Kurita T. Bladder smooth muscle cell phenotypic changes and implication of expression of contractile proteins (especially caldesmon) in rats after partial outlet obstruction. Int J Urol 10: 339-345, 2003.
    • (2003) Int J Urol , vol.10 , pp. 339-345
    • Matsumoto, S.1    Hanai, T.2    Ohnishi, N.3    Yamamoto, K.4    Kurita, T.5
  • 23
    • 0032904860 scopus 로고    scopus 로고
    • Influence of intercellular tissue connections on airway muscle mechanics
    • Meiss RA. Influence of intercellular tissue connections on airway muscle mechanics. J Appl Physiol 86: 5-15, 1999.
    • (1999) J Appl Physiol , vol.86 , pp. 5-15
    • Meiss, R.A.1
  • 24
    • 11144262856 scopus 로고    scopus 로고
    • Active and passive components in the length-dependent stiffness of tracheal smooth muscle during isotonic shortening
    • Meiss RA and Pidaparti RM. Active and passive components in the length-dependent stiffness of tracheal smooth muscle during isotonic shortening. J Appl Physiol 98: 234-241, 2005.
    • (2005) J Appl Physiol , vol.98 , pp. 234-241
    • Meiss, R.A.1    Pidaparti, R.M.2
  • 25
    • 0942276803 scopus 로고    scopus 로고
    • Mechanical state of airway smooth muscle at very short lengths
    • Meiss RA and Pidaparti RM. Mechanical state of airway smooth muscle at very short lengths. J Appl Physiol 96: 655-667, 2004.
    • (2004) J Appl Physiol , vol.96 , pp. 655-667
    • Meiss, R.A.1    Pidaparti, R.M.2
  • 26
    • 0036866149 scopus 로고    scopus 로고
    • Pathophysiology: The varieties of bladder overactivity
    • Mostwin JL. Pathophysiology: the varieties of bladder overactivity. Urology 60: 22-27, 2002.
    • (2002) Urology , vol.60 , pp. 22-27
    • Mostwin, J.L.1
  • 27
    • 0000320199 scopus 로고
    • Softening of rubber by deformation
    • Mullins L. Softening of rubber by deformation. Rubber Chem Technol 42: 339-362, 1969.
    • (1969) Rubber Chem Technol , vol.42 , pp. 339-362
    • Mullins, L.1
  • 29
    • 8644265221 scopus 로고    scopus 로고
    • Changes in the biaxial viscoelastic response of the urinary bladder following spinal cord injury
    • Nagatomi J, Gloeckner DC, Chancellor MB, DeGroat WC, and Sacks MS. Changes in the biaxial viscoelastic response of the urinary bladder following spinal cord injury. Ann Biomed Eng 32: 1409-1419, 2004.
    • (2004) Ann Biomed Eng , vol.32 , pp. 1409-1419
    • Nagatomi, J.1    Gloeckner, D.C.2    Chancellor, M.B.3    DeGroat, W.C.4    Sacks, M.S.5
  • 30
    • 23844453003 scopus 로고    scopus 로고
    • Quantification of bladder smooth muscle orientation in normal and spinal cord injured rats
    • Nagatomi J, Toosi KK, Grashow JS, Chancellor MB, and Sacks MS. Quantification of bladder smooth muscle orientation in normal and spinal cord injured rats. Ann Biomed Eng 33: 1078-1089, 2005.
    • (2005) Ann Biomed Eng , vol.33 , pp. 1078-1089
    • Nagatomi, J.1    Toosi, K.K.2    Grashow, J.S.3    Chancellor, M.B.4    Sacks, M.S.5
  • 31
    • 0035800862 scopus 로고    scopus 로고
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation. J Biol Chem 276: 29567-29574, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 29567-29574
    • Niiro, N.1    Ikebe, M.2
  • 32
    • 0023626217 scopus 로고
    • Protein kinase C in the regulation of smooth muscle contraction
    • Rasmussen H, Takuwa Y, and Park S. Protein kinase C in the regulation of smooth muscle contraction. FASEB J 1: 177-185, 1987.
    • (1987) FASEB J , vol.1 , pp. 177-185
    • Rasmussen, H.1    Takuwa, Y.2    Park, S.3
  • 33
    • 0027174307 scopus 로고
    • 1-adrenergic receptor occupancy decreases relaxing potency of nifedipine by increasing myosin light chain phosphorylation
    • 1-adrenergic receptor occupancy decreases relaxing potency of nifedipine by increasing myosin light chain phosphorylation. Circ Res 72: 1308-1316, 1993.
    • (1993) Circ Res , vol.72 , pp. 1308-1316
    • Ratz, P.H.1
  • 34
    • 0029091928 scopus 로고
    • Receptor activation induces short-term modulation of arterial contractions: Memory in vascular smooth muscle
    • Ratz PH. Receptor activation induces short-term modulation of arterial contractions: memory in vascular smooth muscle. Am J Physiol Cell Physiol 269: C417-C423, 1995.
    • (1995) Am J Physiol Cell Physiol , vol.269
    • Ratz, P.H.1
  • 35
    • 0037383113 scopus 로고    scopus 로고
    • Length-dependent regulation of basal myosin phosphorylation and force in detrusor smooth muscle
    • Ratz PH and Miner AS. Length-dependent regulation of basal myosin phosphorylation and force in detrusor smooth muscle. Am J Physiol Regul Integr Comp Physiol 284: R1063-R1070, 2003.
    • (2003) Am J Physiol Regul Integr Comp Physiol , vol.284
    • Ratz, P.H.1    Miner, A.S.2
  • 36
    • 0037304573 scopus 로고    scopus 로고
    • Effect of antihypertensive treatment on small artery remodeling in hypertension
    • Schiffrin EL. Effect of antihypertensive treatment on small artery remodeling in hypertension. Can J Physiol Pharmacol 81: 168-176, 2003.
    • (2003) Can J Physiol Pharmacol , vol.81 , pp. 168-176
    • Schiffrin, E.L.1
  • 37
    • 0032748050 scopus 로고    scopus 로고
    • Rapid effects of estrogen and progesterone on tone and spontaneous rhythmic contractions of the rabbit bladder
    • Shenfeld OZ, McCammon KA, Blackmore PF, and Ratz PH. Rapid effects of estrogen and progesterone on tone and spontaneous rhythmic contractions of the rabbit bladder. Urol Res 27: 386-392, 1999.
    • (1999) Urol Res , vol.27 , pp. 386-392
    • Shenfeld, O.Z.1    McCammon, K.A.2    Blackmore, P.F.3    Ratz, P.H.4
  • 38
    • 0031986453 scopus 로고    scopus 로고
    • Bethanechol activates a post-receptor negative feedback mechanism in rabbit urinary bladder smooth muscle
    • Shenfeld OZ, Morgan CW, and Ratz PH. Bethanechol activates a post-receptor negative feedback mechanism in rabbit urinary bladder smooth muscle. J Urol 159: 252-257, 1998.
    • (1998) J Urol , vol.159 , pp. 252-257
    • Shenfeld, O.Z.1    Morgan, C.W.2    Ratz, P.H.3
  • 39
    • 0346391091 scopus 로고
    • Calcium-dependent resistance to stretch and stress relaxation in resting smooth muscles
    • Siegman MJ, Butler TM, Mooers SU, and Davies RE. Calcium-dependent resistance to stretch and stress relaxation in resting smooth muscles. Am J Physiol 231: 1501-1508, 1976.
    • (1976) Am J Physiol , vol.231 , pp. 1501-1508
    • Siegman, M.J.1    Butler, T.M.2    Mooers, S.U.3    Davies, R.E.4
  • 40
    • 0017239312 scopus 로고
    • Crossbridge attachment, resistance to stretch, and viscoelasticity in resting mammalian smooth muscle
    • Siegman MJ, Butler TM, Mooers SU, and Davies RE. Crossbridge attachment, resistance to stretch, and viscoelasticity in resting mammalian smooth muscle. Science 191: 383-385, 1976.
    • (1976) Science , vol.191 , pp. 383-385
    • Siegman, M.J.1    Butler, T.M.2    Mooers, S.U.3    Davies, R.E.4
  • 41
    • 21144434279 scopus 로고    scopus 로고
    • ROK-induced cross-link formation stiffens passive muscle: Reversible strain-induced stress softening in rabbit detrusor
    • Speich JE, Borgsmiller L, Call C, Mohr R, and Ratz PH. ROK-induced cross-link formation stiffens passive muscle: reversible strain-induced stress softening in rabbit detrusor. Am J Physiol Cell Physiol 289: C12-C21, 2005.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Speich, J.E.1    Borgsmiller, L.2    Call, C.3    Mohr, R.4    Ratz, P.H.5
  • 42
    • 3543074094 scopus 로고    scopus 로고
    • Calponin (CaP) as a latch-bridge protein - A new concept in regulation of contractility in smooth muscles
    • Szymanski PT. Calponin (CaP) as a latch-bridge protein - a new concept in regulation of contractility in smooth muscles. J Muscle Res Cell Motil 25: 7-19, 2004.
    • (2004) J Muscle Res Cell Motil , vol.25 , pp. 7-19
    • Szymanski, P.T.1
  • 43
    • 0017197777 scopus 로고
    • Isometric and isotonic length-tension relations and variations in longitudinal smooth muscle from rabbit urinary bladder
    • Uvelius B. Isometric and isotonic length-tension relations and variations in longitudinal smooth muscle from rabbit urinary bladder. Acta Physiol Scand 97: 1-12, 1976.
    • (1976) Acta Physiol Scand , vol.97 , pp. 1-12
    • Uvelius, B.1
  • 44
    • 0024778348 scopus 로고
    • A model for caldesmon in latch-bridge formation in smooth muscle
    • Walsh MP and Sutherland C. A model for caldesmon in latch-bridge formation in smooth muscle. Adv Exp Med Biol 255: 337-346, 1989.
    • (1989) Adv Exp Med Biol , vol.255 , pp. 337-346
    • Walsh, M.P.1    Sutherland, C.2
  • 45
    • 1542349922 scopus 로고    scopus 로고
    • Smooth muscle hypertrophy following partial bladder outlet obstruction is associated with overexpression of non-muscle caldesmon
    • Zhang EY, Stein R, Chang S, Zheng Y, Zderic SA, Wein AJ, and Chacko S. Smooth muscle hypertrophy following partial bladder outlet obstruction is associated with overexpression of non-muscle caldesmon. Am J Pathol 164: 601-612, 2004.
    • (2004) Am J Pathol , vol.164 , pp. 601-612
    • Zhang, E.Y.1    Stein, R.2    Chang, S.3    Zheng, Y.4    Zderic, S.A.5    Wein, A.J.6    Chacko, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.