메뉴 건너뛰기




Volumn 120, Issue 1, 1997, Pages 93-104

Evidence that the tandem ig domains near the end of the muscle thick filament form an inelastic part of the I-band titin

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL TISSUE; ARTICLE; CALCULATION; ELASTICITY; HEART MUSCLE; MUSCLE LENGTH; MYOFILAMENT; NONHUMAN; PRIORITY JOURNAL; PSOAS MUSCLE; SARCOMERE; VERTEBRATE;

EID: 0031258656     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3898     Document Type: Article
Times cited : (18)

References (43)
  • 1
    • 0030604697 scopus 로고    scopus 로고
    • Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament
    • Bennett P. M., Gautel M. Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament. J. Mol. Biol. 259:1996;896-903.
    • (1996) J. Mol. Biol. , vol.259 , pp. 896-903
    • Bennett, P.M.1    Gautel, M.2
  • 2
    • 0002133440 scopus 로고
    • Myosin molecules thick filaments, and the actin-myosin complex
    • London: Academic Press. p. 98-203
    • Craig R., Knight P. Myosin molecules thick filaments, and the actin-myosin complex. Electron Microscopy of Proteins. 1983;Academic Press, London. p. 98-203.
    • (1983) Electron Microscopy of Proteins
    • Craig, R.1    Knight, P.2
  • 3
    • 85012661423 scopus 로고
    • Details of the I-band structure as revealed by the localisation of ferritin
    • Franzini-Armstrong C. Details of the I-band structure as revealed by the localisation of ferritin. Tissue Cell. 2:1970;327-338.
    • (1970) Tissue Cell , vol.2 , pp. 327-338
    • Franzini-Armstrong, C.1
  • 4
    • 0025062549 scopus 로고
    • Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin
    • Funatsu T., Higuchi H., Ishiwata S. Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin. J. Cell Biol. 110:1990;53-62.
    • (1990) J. Cell Biol. , vol.110 , pp. 53-62
    • Funatsu, T.1    Higuchi, H.2    Ishiwata, S.3
  • 5
    • 0027448024 scopus 로고
    • Elastic filaments in situ in cardiac muscle: Deep-etch replica analysis in combination with selective removal of actin and myosin filaments
    • Funatsu T., Kono E., Higuchi H., Kimura S., Ishiwata S., Yoshioka T., Maruyama K., Tsukita S. Elastic filaments in situ in cardiac muscle: Deep-etch replica analysis in combination with selective removal of actin and myosin filaments. J. Cell Biol. 120:1993;711-724.
    • (1993) J. Cell Biol. , vol.120 , pp. 711-724
    • Funatsu, T.1    Kono, E.2    Higuchi, H.3    Kimura, S.4    Ishiwata, S.5    Yoshioka, T.6    Maruyama, K.7    Tsukita, S.8
  • 6
    • 0029006530 scopus 로고
    • The anatomy of a molecular giant: How the sarcomeric cytoskeleton is assembled from molecules of the immunoglobulin superfamily
    • Fürst D. O., Gautel M. The anatomy of a molecular giant: How the sarcomeric cytoskeleton is assembled from molecules of the immunoglobulin superfamily. J. Mol. Cell. Cardiol. 27:1995;951-959.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 951-959
    • Fürst, D.O.1    Gautel, M.2
  • 7
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M-line
    • Fürst D. O., Osborne M., Nave R., Weber K. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M-line. J. Cell. Biol. 106:1988;1563-1572.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborne, M.2    Nave, R.3    Weber, K.4
  • 8
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel M., Goulding D. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385:1996;11-14.
    • (1996) FEBS Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 9
    • 0029801781 scopus 로고    scopus 로고
    • Assembly of the cardiac I-band region of titin/connectin: Expression of the cardiac-specific regions and their structural relation to the elastic segments
    • Gautel M., Lehtonen E., Pietruschka F. Assembly of the cardiac I-band region of titin/connectin: expression of the cardiac-specific regions and their structural relation to the elastic segments. J. Muscle Res. Cell Motil. 17:1996;449-461.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 449-461
    • Gautel, M.1    Lehtonen, E.2    Pietruschka, F.3
  • 10
    • 0029040311 scopus 로고
    • Evaluation of freeze substitution in rabbit skeletal muscle: Comparison of electron microscopy to X-ray diffraction
    • Hawkins C. J., Bennett P. M. Evaluation of freeze substitution in rabbit skeletal muscle: Comparison of electron microscopy to X-ray diffraction. J. Muscle Res. Cell Motil. 16:1995;303-318.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 303-318
    • Hawkins, C.J.1    Bennett, P.M.2
  • 11
    • 0026634116 scopus 로고
    • Localization and elasticity of connectin (titin) filaments in skinned frog muscle fibres subjected to partial depolymerization of thick filaments
    • Higuchi H., Suzuki T., Kimura S., Yoshiaka T., Maruyama K., Umazume Y. Localization and elasticity of connectin (titin) filaments in skinned frog muscle fibres subjected to partial depolymerization of thick filaments. J. Muscle Res. Cell Motil. 13:1992;285-294.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 285-294
    • Higuchi, H.1    Suzuki, T.2    Kimura, S.3    Yoshiaka, T.4    Maruyama, K.5    Umazume, Y.6
  • 12
    • 0024279614 scopus 로고
    • Thin filaments of rabbit skeletal muscle are in helical register
    • Hirose K., Wakabayashi T. Thin filaments of rabbit skeletal muscle are in helical register. J. Mol. Biol. 204:1988;797-801.
    • (1988) J. Mol. Biol. , vol.204 , pp. 797-801
    • Hirose, K.1    Wakabayashi, T.2
  • 13
    • 0026755352 scopus 로고
    • Passive force generation and titin isoforms in mammalian skeletal muscle
    • Horowits R. Passive force generation and titin isoforms in mammalian skeletal muscle. Biophys. J. 61:1992;392-398.
    • (1992) Biophys. J. , vol.61 , pp. 392-398
    • Horowits, R.1
  • 14
    • 0024426462 scopus 로고
    • Elastic behaviour of connectin filaments during thick filament movement in activated skeletal muscle
    • Horowits R., Maruyama K., Podolsky R. J. Elastic behaviour of connectin filaments during thick filament movement in activated skeletal muscle. J. Cell Biol. 109:1989;2169-2176.
    • (1989) J. Cell Biol. , vol.109 , pp. 2169-2176
    • Horowits, R.1    Maruyama, K.2    Podolsky, R.J.3
  • 15
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta S., Politou A. S., Pastore A. Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure. 4:1996;323-337.
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 16
    • 0023756132 scopus 로고
    • Extensible and less extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies
    • Itoh Y., Suzuki T., Kimura S., Ohashi K., Higuchi H., Sawada H., Shimizu T., Shibata M., Maruyama K. Extensible and less extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104:1988;504-508.
    • (1988) J. Biochem. , vol.104 , pp. 504-508
    • Itoh, Y.1    Suzuki, T.2    Kimura, S.3    Ohashi, K.4    Higuchi, H.5    Sawada, H.6    Shimizu, T.7    Shibata, M.8    Maruyama, K.9
  • 17
    • 0028955760 scopus 로고
    • Structure and function of titin and nebulin
    • Keller C. S. Structure and function of titin and nebulin. Curr. Opin. Cell Biol. 7:1995;32-38.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 32-38
    • Keller, C.S.1
  • 18
    • 0029886571 scopus 로고    scopus 로고
    • Elastic properties of single titin molecules made visible through fluorescent F-actin binding
    • Kellermayer M. S. Z., Granzier H. L. Elastic properties of single titin molecules made visible through fluorescent F-actin binding. Biochem. Biophys. Res. Commun. 221:1996;491-497.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 491-497
    • Kellermayer, M.S.Z.1    Granzier, H.L.2
  • 19
    • 0021125548 scopus 로고
    • Interactions of muscle β-connectin with myosin, actin and actomyosin at low ionic strengths
    • Kimura K., Maruyama K., Huang Y. P. Interactions of muscle β-connectin with myosin, actin and actomyosin at low ionic strengths. J. Biochem. 96:1984;499-506.
    • (1984) J. Biochem. , vol.96 , pp. 499-506
    • Kimura, K.1    Maruyama, K.2    Huang, Y.P.3
  • 20
    • 0028824480 scopus 로고
    • Titins, giant molecules in charge of muscle ultrastructure and elasticity
    • Labeit S., Kolmerer B. Titins, giant molecules in charge of muscle ultrastructure and elasticity. Science. 270:1995;293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 22
    • 0017156475 scopus 로고
    • Histology of highly stretched beef muscle. IV. Evidence for movement of gap filaments through the Z-line using the N2-line and M-line as markers
    • Locker R. H., Leet N. G. Histology of highly stretched beef muscle. iv. Evidence for movement of gap filaments through the Z-line using the N2-line and M-line as markers. J. Ultrastruct. Res. 56:1976;31-38.
    • (1976) J. Ultrastruct. Res. , vol.56 , pp. 31-38
    • Locker, R.H.1    Leet, N.G.2
  • 24
    • 0028289058 scopus 로고
    • Connectin, an elastic protein of striated muscle
    • Maruyama K. Connectin, an elastic protein of striated muscle. Biophys. Chem. 50:1994;73-85.
    • (1994) Biophys. Chem. , vol.50 , pp. 73-85
    • Maruyama, K.1
  • 25
    • 0022340387 scopus 로고
    • Connectin filaments link thick filaments and Z-lines in frog skeletal muscle as revealed by immunoelectron microscopy
    • Maruyama K., Yoshioka T., Higuchi H., Ohashi K., Kimura S., Natori R. Connectin filaments link thick filaments and Z-lines in frog skeletal muscle as revealed by immunoelectron microscopy. J. Cell Biol. 101:1985;2167-2172.
    • (1985) J. Cell Biol. , vol.101 , pp. 2167-2172
    • Maruyama, K.1    Yoshioka, T.2    Higuchi, H.3    Ohashi, K.4    Kimura, S.5    Natori, R.6
  • 27
    • 0019331904 scopus 로고
    • Fraying of A-filaments into three subfilaments
    • Maw M. C., Rowe A. J. Fraying of A-filaments into three subfilaments. Nature. 286:1980;412-414.
    • (1980) Nature , vol.286 , pp. 412-414
    • Maw, M.C.1    Rowe, A.J.2
  • 28
    • 0014318751 scopus 로고
    • Fine structure of tortoise skeletal muscle
    • Page S. G. Fine structure of tortoise skeletal muscle. J. Physiol. 197:1968;709-715.
    • (1968) J. Physiol. , vol.197 , pp. 709-715
    • Page, S.G.1
  • 29
    • 0030009318 scopus 로고    scopus 로고
    • The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains
    • Politou A., Gautel M., Improta S., Vangelista L., Pastore A. The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains. J. Mol. Biol. 255:1996;604-616.
    • (1996) J. Mol. Biol. , vol.255 , pp. 604-616
    • Politou, A.1    Gautel, M.2    Improta, S.3    Vangelista, L.4    Pastore, A.5
  • 30
    • 0022419472 scopus 로고
    • Rigor crossbridge structure in tilted single filament layers and flared-X formations from insect flight muscle
    • Ready M. K., Reedy M. C. Rigor crossbridge structure in tilted single filament layers and flared-X formations from insect flight muscle. J. Mol. Biol. 185:1985;145-176.
    • (1985) J. Mol. Biol. , vol.185 , pp. 145-176
    • Ready, M.K.1    Reedy, M.C.2
  • 31
    • 0027536473 scopus 로고
    • A survey of interactions made by the giant muscle protein titin
    • Soteriou A., Gamage M., Trinick J. A survey of interactions made by the giant muscle protein titin. J. Cell Sci. 104:1993;119-123.
    • (1993) J. Cell Sci. , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 33
    • 0019834569 scopus 로고
    • End-filaments: A new structural element of vertebrate skeletal muscle thick filaments
    • Trinick J. End-filaments: A new structural element of vertebrate skeletal muscle thick filaments. J. Mol. Biol. 151:1981;309-314.
    • (1981) J. Mol. Biol. , vol.151 , pp. 309-314
    • Trinick, J.1
  • 34
    • 0025877737 scopus 로고
    • Elastic filaments and giant proteins in muscle
    • Trinick J. Elastic filaments and giant proteins in muscle. Curr. Opin. Cell Biol. 3:1991;112-119.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 112-119
    • Trinick, J.1
  • 35
    • 0030091595 scopus 로고    scopus 로고
    • Titin as scaffold and spring
    • Trinick J. Titin as scaffold and spring. Curr. Biol. 6:1996;258-260.
    • (1996) Curr. Biol. , vol.6 , pp. 258-260
    • Trinick, J.1
  • 36
    • 0019325858 scopus 로고
    • Sequential disassembly of vertebrate muscle thick filaments
    • Trinick J., Cooper J. Sequential disassembly of vertebrate muscle thick filaments. J. Mol. Biol. 141:1980;315-321.
    • (1980) J. Mol. Biol. , vol.141 , pp. 315-321
    • Trinick, J.1    Cooper, J.2
  • 37
    • 0027313537 scopus 로고
    • Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle
    • Trombitás K., Pollack G. H. Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle. J. Muscle Res. Cell Motil. 14:1993;416-422.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 416-422
    • Trombitás, K.1    Pollack, G.H.2
  • 40
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • Wang K., McCarter R., Wright J., Beverly J., Ramirez-Mitchell R. Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension. Proc. Natl. Acad. Sci. USA. 88:1991;7101-7105.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 41
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin: Effects of divalent cations on proteolytic susceptibility
    • Weeds A. G., Pope B. Studies on the chymotryptic digestion of myosin: Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:1977;129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 42
    • 0024961666 scopus 로고
    • Does titin regulate the length of thick filaments?
    • Whiting A., Wardale J., Trinick J. Does titin regulate the length of thick filaments? J. Mol. Biol. 205:1989;263-268.
    • (1989) J. Mol. Biol. , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 43
    • 0022632506 scopus 로고
    • High resolution equatorial x-ray diffraction from single skinned rabbit psoas fibres
    • Yu L. C., Brenner B. High resolution equatorial x-ray diffraction from single skinned rabbit psoas fibres. Biophys. J. 49:1986;133-135.
    • (1986) Biophys. J. , vol.49 , pp. 133-135
    • Yu, L.C.1    Brenner, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.