메뉴 건너뛰기




Volumn 20, Issue 3, 1999, Pages 291-303

Sarcomeric binding pattern of exogenously added intact caldesmon and its C-terminal 20-kDa fragment in skinned fibers of skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE MAGNESIUM; CALDESMON; MYOSIN; RHODAMINE;

EID: 0032773777     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005490405222     Document Type: Article
Times cited : (1)

References (45)
  • 2
    • 0009633974 scopus 로고
    • X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths
    • Brenner B, Yu LC and Podolsky RJ (1984) X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths. Biophys J 50: 1101-1108.
    • (1984) Biophys J , vol.50 , pp. 1101-1108
    • Brenner, B.1    Yu, L.C.2    Podolsky, R.J.3
  • 3
    • 0025945650 scopus 로고
    • Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon: Implications for the pathway to force generation
    • Brenner B, Yu LC and Chalovich JM (1991) Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon: Implications for the pathway to force generation. Proc Natl Acad Sci USA 88: 5739-5743.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5739-5743
    • Brenner, B.1    Yu, L.C.2    Chalovich, J.M.3
  • 4
    • 0021686984 scopus 로고
    • Smooth muscle caldesmon: Rapid purification and F-actin cross-linking properties
    • Bretscher A (1984) Smooth muscle caldesmon: Rapid purification and F-actin cross-linking properties. J Biol Chem 259: 12873-12880.
    • (1984) J Biol Chem , vol.259 , pp. 12873-12880
    • Bretscher, A.1
  • 5
    • 0021147148 scopus 로고
    • Sarcomere structures in the rabbit psoas muscle as revealed by fluorescent analogs of phalloidin
    • Bukatina AE, Sonkin BY, Alievskaya LL and Yashin VA (1984) Sarcomere structures in the rabbit psoas muscle as revealed by fluorescent analogs of phalloidin. Histochemistry 81: 301-304.
    • (1984) Histochemistry , vol.81 , pp. 301-304
    • Bukatina, A.E.1    Sonkin, B.Y.2    Alievskaya, L.L.3    Yashin, V.A.4
  • 6
    • 0001214811 scopus 로고    scopus 로고
    • Structure and function of the thin filament proteins of smooth muscle
    • edited by Kao, C.Y. & Carsten, M.E. New York: Cambridge University Press
    • Chalovich JM and Pfitzer G (1997) Structure and function of the thin filament proteins of smooth muscle. In Cellular Aspects of Smooth Muscle Function (edited by Kao, C.Y. & Carsten, M.E.), pp. 253-287. New York: Cambridge University Press.
    • (1997) Cellular Aspects of Smooth Muscle Function , pp. 253-287
    • Chalovich, J.M.1    Pfitzer, G.2
  • 7
    • 0028802608 scopus 로고
    • Flexation of caldesmon: Effect of conformation on the properties of caldesmon
    • Crosbie RH, Chalovich JM and Reisler E (1995) Flexation of caldesmon: Effect of conformation on the properties of caldesmon. J Muscle Res Cell Motil 16: 509-518. Abstract.
    • (1995) J Muscle Res Cell Motil , vol.16 , pp. 509-518
    • Crosbie, R.H.1    Chalovich, J.M.2    Reisler, E.3
  • 8
    • 4243397820 scopus 로고    scopus 로고
    • Molecular modeling of actomyosin crossbridge cycle. III. Regulation of tropomyosin-actin-S1 complex
    • Dreizen P, Shi J and Shen C (1996) Molecular modeling of actomyosin crossbridge cycle. III. Regulation of tropomyosin-actin-S1 complex. Biophys J 70: A259.
    • (1996) Biophys J , vol.70
    • Dreizen, P.1    Shi, J.2    Shen, C.3
  • 9
    • 0019395642 scopus 로고
    • The Mr 165,000 M-protein myomesin. A specific protein of cross-striated muscle cells
    • Eppenberger HM, Perriard JC, Rosenberg UB and Strehler EE (1981) The Mr 165,000 M-protein myomesin. A specific protein of cross-striated muscle cells. J Cell Biol 89: 185-193.
    • (1981) J Cell Biol , vol.89 , pp. 185-193
    • Eppenberger, H.M.1    Perriard, J.C.2    Rosenberg, U.B.3    Strehler, E.E.4
  • 10
    • 0022668792 scopus 로고
    • Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle
    • Fürst DO, Cross RA, DeMey J, and Small JV (1986) Caldesmon is an elongated, flexible molecule localized in the actomyosin domains of smooth muscle. EMBO J 5: 251-257.
    • (1986) EMBO J , vol.5 , pp. 251-257
    • Fürst, D.O.1    Cross, R.A.2    DeMey, J.3    Small, J.V.4
  • 11
    • 0023801362 scopus 로고
    • Caldesmon: Molecular weight and subunit composition by analytical ultracentrifugation
    • Graceffa P, Wang CLA and Stafford WF (1988) Caldesmon: Molecular weight and subunit composition by analytical ultracentrifugation. J Biol Chem 263: 14196-14202.
    • (1988) J Biol Chem , vol.263 , pp. 14196-14202
    • Graceffa, P.1    Wang, C.L.A.2    Stafford, W.F.3
  • 13
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada Y, Sakurda K, Aoki T, Thomas DD and Yanagida T (1990) Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J Mol Biol 216: 49-68.
    • (1990) J Mol Biol , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurda, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 14
    • 0023945560 scopus 로고
    • Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin
    • Hemric ME and Chalovich JM (1988) Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin. J Biol Chem 263: 1878-1885.
    • (1988) J Biol Chem , vol.263 , pp. 1878-1885
    • Hemric, M.E.1    Chalovich, J.M.2
  • 15
    • 0025200974 scopus 로고
    • Characterization of caldesmon binding to myosin
    • Hemric ME and Chalovich JM (1990) Characterization of caldesmon binding to myosin. J Biol Chem 265 (32): 19672-19678.
    • (1990) J Biol Chem , vol.265 , Issue.32 , pp. 19672-19678
    • Hemric, M.E.1    Chalovich, J.M.2
  • 16
    • 0030927201 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: Effects of caldesmon
    • Hodgkinson JL, Marston SB, Craig R, Vibert P and Lehman W (1997) Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon. Biophys J 72: 2398-2404.
    • (1997) Biophys J , vol.72 , pp. 2398-2404
    • Hodgkinson, J.L.1    Marston, S.B.2    Craig, R.3    Vibert, P.4    Lehman, W.5
  • 17
    • 0023845108 scopus 로고
    • Binding of caldesmon to smooth muscle myosin
    • Ikebe M and Reardon S (1988) Binding of caldesmon to smooth muscle myosin. J Biol Chem 263: 3055-3058.
    • (1988) J Biol Chem , vol.263 , pp. 3055-3058
    • Ikebe, M.1    Reardon, S.2
  • 18
    • 0029033789 scopus 로고
    • Mode of caldesmon binding to smooth muscle thin filament: Possible projection of the amino-terminal domain of caldesmon from native thin filament
    • Katayama E and Ikebe M (1995) Mode of caldesmon binding to smooth muscle thin filament: Possible projection of the amino-terminal domain of caldesmon from native thin filament. Biophys J 68: 2419-2428.
    • (1995) Biophys J , vol.68 , pp. 2419-2428
    • Katayama, E.1    Ikebe, M.2
  • 19
    • 0029005992 scopus 로고
    • Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological temperature and ionic strength conditions. Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation
    • Kraft T, Chalovich JM, Yu LC and Brenner B (1995a) Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological temperature and ionic strength conditions. Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophys J 68: 2404-2418.
    • (1995) Biophys J , vol.68 , pp. 2404-2418
    • Kraft, T.1    Chalovich, J.M.2    Yu, L.C.3    Brenner, B.4
  • 20
    • 0029155974 scopus 로고
    • Equilibration of fluorescently labeled molecules in skinned skeletal muscle fibers visualized by confocal microscopy
    • Kraft T, Rutishauser B, Messerli M, Perriard JC, Wallimann T and Brenner B (1995b) Equilibration of fluorescently labeled molecules in skinned skeletal muscle fibers visualized by confocal microscopy. Biophys J 69: 1246-1258.
    • (1995) Biophys J , vol.69 , pp. 1246-1258
    • Kraft, T.1    Rutishauser, B.2    Messerli, M.3    Perriard, J.C.4    Wallimann, T.5    Brenner, B.6
  • 21
    • 0001560058 scopus 로고    scopus 로고
    • Binding of creatine kinase to the 1-band of skinned skeletal muscle fibers is mediated by glycolytic enzymes: An in situ biochemical approach
    • Kraft T, Nier V, Brenner B and Wallimann T (1996) Binding of creatine kinase to the 1-band of skinned skeletal muscle fibers is mediated by glycolytic enzymes: An in situ biochemical approach. Biophys J 70: A292.
    • (1996) Biophys J , vol.70
    • Kraft, T.1    Nier, V.2    Brenner, B.3    Wallimann, T.4
  • 22
    • 0024509574 scopus 로고
    • Caldesmon and the structure of smooth muscle thin filaments. Immunolocalization of caldesmon on thin filaments
    • Lehman W, Craig R, Lui J and Mood C (1989) Caldesmon and the structure of smooth muscle thin filaments. Immunolocalization of caldesmon on thin filaments. J Muscle Res Cell Motil 10: 101-112.
    • (1989) J Muscle Res Cell Motil , vol.10 , pp. 101-112
    • Lehman, W.1    Craig, R.2    Lui, J.3    Mood, C.4
  • 23
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • Lehman W, Vibert P, Uman P and Craig R (1995) Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J Mol Biol 251: 191-196.
    • (1995) J Mol Biol , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 24
    • 0031555487 scopus 로고    scopus 로고
    • Visualization of caldesmon on smooth muscle thin filaments
    • Lehman W, Vibert P and Craig R (1997) Visualization of caldesmon on smooth muscle thin filaments. J Mol Biol 274: 310-317.
    • (1997) J Mol Biol , vol.274 , pp. 310-317
    • Lehman, W.1    Vibert, P.2    Craig, R.3
  • 25
    • 0029002507 scopus 로고
    • Role of ATP in the binding of caldesmon to smooth muscle myosin
    • Lu FWM and Chalovich JM (1995) Role of ATP in the binding of caldesmon to smooth muscle myosin. Biochemistry 34: 6359-6365.
    • (1995) Biochemistry , vol.34 , pp. 6359-6365
    • Lu, F.W.M.1    Chalovich, J.M.2
  • 26
    • 0023664509 scopus 로고
    • Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sullhydryl cross-linking
    • Lynch WP, Riseman VM and Bretscher A (1987) Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sullhydryl cross-linking. J Biol Chem 2262: 7429-7437.
    • (1987) J Biol Chem , vol.2262 , pp. 7429-7437
    • Lynch, W.P.1    Riseman, V.M.2    Bretscher, A.3
  • 27
    • 0027478542 scopus 로고
    • Electron microscopic images suggest both ends of caldesmon interact with actin filaments
    • Mabuchi K, Lin JJC and Wang CLA (1993) Electron microscopic images suggest both ends of caldesmon interact with actin filaments. J Muscle Res Cell Motil 14: 54-64.
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 54-64
    • Mabuchi, K.1    Lin, J.J.C.2    Wang, C.L.A.3
  • 28
    • 0025881953 scopus 로고
    • Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin
    • Mabuchi K and Wang CLA (1991) Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin. J Muscle Res Cell Motil 12: 145-151.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 145-151
    • Mabuchi, K.1    Wang, C.L.A.2
  • 29
    • 0028986526 scopus 로고
    • Analysis of equatorial X-ray diffraction patterns from muscle fibers: Factors that affect the intensities
    • Malinchik S and Yu LC (1995) Analysis of equatorial X-ray diffraction patterns from muscle fibers: Factors that affect the intensities. Biophys J 68: 2023-2031.
    • (1995) Biophys J , vol.68 , pp. 2023-2031
    • Malinchik, S.1    Yu, L.C.2
  • 30
    • 0028964210 scopus 로고
    • Effect of caltropin on caldesmon-actin interaction
    • Mani RS and Kay CM (1995) Effect of caltropin on caldesmon-actin interaction. J Biol Chem 270 (12): 6658-6663.
    • (1995) J Biol Chem , vol.270 , Issue.12 , pp. 6658-6663
    • Mani, R.S.1    Kay, C.M.2
  • 31
    • 0025971459 scopus 로고
    • Conformational change of turkey-gizzard caldesmon induced by specific chemical modification with carbodiimide
    • Martin F, Harricane MC, Audemard E, Pons F and Mornet D (1991) Conformational change of turkey-gizzard caldesmon induced by specific chemical modification with carbodiimide. Eur J Biochem 195: 335-342.
    • (1991) Eur J Biochem , vol.195 , pp. 335-342
    • Martin, F.1    Harricane, M.C.2    Audemard, E.3    Pons, F.4    Mornet, D.5
  • 32
    • 0025308841 scopus 로고
    • Caldesmon and the structure of smooth muscle thin filaments: Electronmicroscopy of isolated thin filaments
    • Moody C, Lehmann W and Craig R (1990) Caldesmon and the structure of smooth muscle thin filaments: electronmicroscopy of isolated thin filaments. J Muscle Res Cell Mot 11: 176-185.
    • (1990) J Muscle Res Cell Mot , vol.11 , pp. 176-185
    • Moody, C.1    Lehmann, W.2    Craig, R.3
  • 33
    • 0023260790 scopus 로고
    • The effects of phosphorylation of smooth-muscle caldesmon
    • Ngai PK and Walsh MP (1987) The effects of phosphorylation of smooth-muscle caldesmon. Biochem J 244: 417-425.
    • (1987) Biochem J , vol.244 , pp. 417-425
    • Ngai, P.K.1    Walsh, M.P.2
  • 35
    • 0022419472 scopus 로고
    • Rigor crossbridge structure in tilted single filament layers and flared-X formations from insect flight muscle
    • Reedy MK and Reedy MC (1985) Rigor crossbridge structure in tilted single filament layers and flared-X formations from insect flight muscle. J Mol Biol 185 (1): 145-176.
    • (1985) J Mol Biol , vol.185 , Issue.1 , pp. 145-176
    • Reedy, M.K.1    Reedy, M.C.2
  • 36
    • 0032546584 scopus 로고    scopus 로고
    • Caldesmon-actin-tropomyosin contains two types of binding sites for myosin SI
    • Sen A and Chalovich JM (1998) Caldesmon-actin-tropomyosin contains two types of binding sites for myosin SI. Biochemistry 37: 7526-7531.
    • (1998) Biochemistry , vol.37 , pp. 7526-7531
    • Sen, A.1    Chalovich, J.M.2
  • 37
    • 0023163894 scopus 로고
    • 2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin
    • 2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin. J Biol Chem 262: 116-122.
    • (1987) J Biol Chem , vol.262 , pp. 116-122
    • Smith, C.W.J.1    Pritchard, K.2    Marston, S.B.3
  • 38
    • 0000160284 scopus 로고
    • Protein assembly and metabolic regulation: Physiological and evolutionary perspectives
    • Somero GN and Hand SC (1990) Protein assembly and metabolic regulation: physiological and evolutionary perspectives. Physiol Zool 63 (3): 443-471.
    • (1990) Physiol Zool , vol.63 , Issue.3 , pp. 443-471
    • Somero, G.N.1    Hand, S.C.2
  • 39
    • 0024348164 scopus 로고
    • The binding of caldesmon to actin and its effect on the ATPase activity of soluble myosin subfragments in the presence and absence of tropomyosin
    • Velaz L, Hemric ME, Benson CE and Chalovich JM (1989) The binding of caldesmon to actin and its effect on the ATPase activity of soluble myosin subfragments in the presence and absence of tropomyosin. J Biol Chem 264: 9602-9610.
    • (1989) J Biol Chem , vol.264 , pp. 9602-9610
    • Velaz, L.1    Hemric, M.E.2    Benson, C.E.3    Chalovich, J.M.4
  • 40
    • 0025267475 scopus 로고
    • Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon
    • Velaz L, Ingraham RH and Chalovich JM (1990) Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon. J Biol Chem 265: 2929-2934.
    • (1990) J Biol Chem , vol.265 , pp. 2929-2934
    • Velaz, L.1    Ingraham, R.H.2    Chalovich, J.M.3
  • 41
    • 0027514929 scopus 로고
    • Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments
    • Vibert P, Craig R and Lehman W (1993) Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments. J Cell Biol 123: 313-321.
    • (1993) J Cell Biol , vol.123 , pp. 313-321
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 42
    • 0028593425 scopus 로고
    • Overexpression, purification, and characterization of full-length and mutant caldesmons using a baculovirus expression system
    • Wang Z, Horiuchi KY, Jacob SS, Gopalakurup S and Chacko S (1994) Overexpression, purification, and characterization of full-length and mutant caldesmons using a baculovirus expression system. J Musc Res Cell Motility 15: 646-658.
    • (1994) J Musc Res Cell Motility , vol.15 , pp. 646-658
    • Wang, Z.1    Horiuchi, K.Y.2    Jacob, S.S.3    Gopalakurup, S.4    Chacko, S.5
  • 43
    • 0023263329 scopus 로고
    • Irradiations of rabbit myofibrils with an ultraviolet microbeam. II. Phalloidin protects actin in solution but not in myofibrils from depolymerization by ultraviolet light
    • Wilson P, Fuller E and Forer A (1987) Irradiations of rabbit myofibrils with an ultraviolet microbeam. II. Phalloidin protects actin in solution but not in myofibrils from depolymerization by ultraviolet light. Biochem Cell Biol 65: 376-385.
    • (1987) Biochem Cell Biol , vol.65 , pp. 376-385
    • Wilson, P.1    Fuller, E.2    Forer, A.3
  • 44
    • 0024518455 scopus 로고
    • Structures of actomyosin crossbridges in relaxed and rigor muscle fibers
    • Yu LC and Brenner B (1989) Structures of actomyosin crossbridges in relaxed and rigor muscle fibers. Biophys J 55: 441-453.
    • (1989) Biophys J , vol.55 , pp. 441-453
    • Yu, L.C.1    Brenner, B.2
  • 45
    • 0030799487 scopus 로고    scopus 로고
    • Distribution and orientation of rhodamine-phalloidin bound to thin filaments in skeletal and cardiac myofibrils
    • Zhukarev V, Sanger JM, Sanger JW, Goldman YE and Shuman H (1997) Distribution and orientation of rhodamine-phalloidin bound to thin filaments in skeletal and cardiac myofibrils. Cell Motil Cytoskeleton 37 (4): 363-377.
    • (1997) Cell Motil Cytoskeleton , vol.37 , Issue.4 , pp. 363-377
    • Zhukarev, V.1    Sanger, J.M.2    Sanger, J.W.3    Goldman, Y.E.4    Shuman, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.