메뉴 건너뛰기




Volumn 110, Issue 1, 1990, Pages 53-62

Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin

Author keywords

[No Author keywords available]

Indexed keywords

ALISMATACEAE; ORYCTOLAGUS CUNICULUS; ANIMALIA;

EID: 0025062549     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.110.1.53     Document Type: Article
Times cited : (115)

References (39)
  • 1
    • 0022551969 scopus 로고
    • 2+ regulatory domain in human brevin
    • 2+ regulatory domain in human brevin. J. Cell Biol. 102:1439-1446.
    • (1986) J. Cell Biol. , vol.102 , pp. 1439-1446
    • Bryan, J.1    Hwo, S.2
  • 2
    • 0021962636 scopus 로고
    • Human plasma actin-depolymerizing factor: Purification, biological activity and localization in leukocytes and platelets
    • Chaponnier, C., P. Patebex, and G. Gabbiani. 1985. Human plasma actin-depolymerizing factor: purification, biological activity and localization in leukocytes and platelets. Eur. J. Biochem. 146:267-276.
    • (1985) Eur. J. Biochem. , vol.146 , pp. 267-276
    • Chaponnier, C.1    Patebex, P.2    Gabbiani, G.3
  • 4
    • 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
    • Furst, D. O., M. Osborn, R. Nave, and K. Weber. 1988. 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. 106:1563-1572.
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Furst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 6
    • 0023371445 scopus 로고
    • Lattice swelling with the selective digestion of elastic components in single-skinned fibers of frog muscle
    • Higuchi, H. 1987. Lattice swelling with the selective digestion of elastic components in single-skinned fibers of frog muscle. Biophys. J. 52:29-32.
    • (1987) Biophys. J. , vol.52 , pp. 29-32
    • Higuchi, H.1
  • 7
    • 0021813195 scopus 로고
    • Localization of the parallel elastic components in frog skinned muscle fibers studied by the dissociation of the A- and I-bands
    • Higuchi, H., and Y. Umazume. 1985. Localization of the parallel elastic components in frog skinned muscle fibers studied by the dissociation of the A- and I-bands. Biophys. J. 48:137-147.
    • (1985) Biophys. J. , vol.48 , pp. 137-147
    • Higuchi, H.1    Umazume, Y.2
  • 8
    • 0022780963 scopus 로고
    • Lattice shrinkage with increasing resting tension in stretched, single skinned fibers of frog muscle
    • Higuchi, H., and Y. Umazume. 1986. Lattice shrinkage with increasing resting tension in stretched, single skinned fibers of frog muscle. Biophys. J. 50:385-389.
    • (1986) Biophys. J. , vol.50 , pp. 385-389
    • Higuchi, H.1    Umazume, Y.2
  • 10
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments
    • Horowits, R., and R. J. Podolsky. 1987. The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments. J. Cell Biol. 105:2217-2223.
    • (1987) J. Cell Biol. , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 11
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowitz, R., E. S. Kempner, M. E. Bisher, and R. J. Podolsky. 1986. A physiological role for titin and nebulin in skeletal muscle. Nature (Lond.). 323:160-164.
    • (1986) Nature (Lond.) , vol.323 , pp. 160-164
    • Horowitz, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 12
    • 72949127255 scopus 로고
    • The maximum length for contraction in vertebrate striated muscle
    • Huxley, A. F., and L. D. Peachey. 1961. The maximum length for contraction in vertebrate striated muscle. J. Physiol. (Lond.). 156:150-165.
    • (1961) J. Physiol. (Lond.) , vol.156 , pp. 150-165
    • Huxley, A.F.1    Peachey, L.D.2
  • 13
    • 85010249552 scopus 로고
    • The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley, H. E., and W. Brown. 1967. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30:383-434.
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 14
    • 0021999557 scopus 로고
    • Does actin bind to the ends of thin filaments in skeletal muscle?
    • Ishiwata, S., and T. Funatsu. 1985. Does actin bind to the ends of thin filaments in skeletal muscle? J. Cell Biol. 100:282-291.
    • (1985) J. Cell Biol. , vol.100 , pp. 282-291
    • Ishiwata, S.1    Funatsu, T.2
  • 15
    • 0007797760 scopus 로고
    • An optical method for the analysis of periodicities in electron micrographs, and some observations on the mechanism of negative staining
    • Klug, A., and J. E. Berger. 1964. An optical method for the analysis of periodicities in electron micrographs, and some observations on the mechanism of negative staining. J. Mol. Biol. 10:565-569.
    • (1964) J. Mol. Biol. , vol.10 , pp. 565-569
    • Klug, A.1    Berger, J.E.2
  • 16
    • 0016808429 scopus 로고
    • Histology of highly-stretched beef muscle. I. The fine structure of grossly stretched single fibers
    • Locker, R. H., and N. G. Leet. 1975. Histology of highly-stretched beef muscle. I. The fine structure of grossly stretched single fibers. J. Ultrastruct. Res. 52:64-75.
    • (1975) J. Ultrastruct. Res. , vol.52 , pp. 64-75
    • Locker, R.H.1    Leet, N.G.2
  • 17
  • 18
    • 0019873637 scopus 로고
    • Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry
    • Luther, P. K., P. M. G. Munro, and J. M. Squire. 1981. Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry. J. Mol. Biol. 151:703-730.
    • (1981) J. Mol. Biol. , vol.151 , pp. 703-730
    • Luther, P.K.1    Munro, P.M.G.2    Squire, J.M.3
  • 19
    • 0022402720 scopus 로고
    • Myofibrils bear most of the resting tension in frog skeletal muscle
    • Magid, A., and D. J. Law. 1985. Myofibrils bear most of the resting tension in frog skeletal muscle. Science (Wash. DC). 230:1280-1282.
    • (1985) Science (Wash. DC) , vol.230 , pp. 1280-1282
    • Magid, A.1    Law, D.J.2
  • 20
    • 0022487438 scopus 로고
    • Connectin, an elastic filamentous protein of striated muscle
    • Maruyama, K. 1986. Connectin, an elastic filamentous protein of striated muscle. Int. Rev. Cytol. 104:81-114.
    • (1986) Int. Rev. Cytol. , vol.104 , pp. 81-114
    • Maruyama, K.1
  • 21
    • 0022340387 scopus 로고
    • Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
    • Maruyama, K., T. Yoshioka, H. Higuchi, K, Ohashi, S. Kimura, and R. Natori. 1985. Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy. J. Cell Biol. 101:2167-2172.
    • (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
  • 22
    • 0001740396 scopus 로고
    • The property and contraction process of isolated myofibrils
    • Natori, R. 1954. The property and contraction process of isolated myofibrils. Jikeikai Med. J. 1:119-126.
    • (1954) Jikeikai Med. J. , vol.1 , pp. 119-126
    • Natori, R.1
  • 24
    • 0001639575 scopus 로고
    • The connections between A- and I-band filaments in striated frog muscle
    • Sjostrand, F. S. 1962. The connections between A- and I-band filaments in striated frog muscle. J. Ultrastruct. Res. 7:225-246.
    • (1962) J. Ultrastruct. Res. , vol.7 , pp. 225-246
    • Sjostrand, F.S.1
  • 25
    • 0019857184 scopus 로고
    • The ultrasensitive silver "protein" stall also detects nanograms of nucleic acids
    • Somerville, L. L., and K. Wang. 1981. The ultrasensitive silver "protein" stall also detects nanograms of nucleic acids. Biochem. Biophys. Res. Commun. 102:53-58.
    • (1981) Biochem. Biophys. Res. Commun. , vol.102 , pp. 53-58
    • Somerville, L.L.1    Wang, K.2
  • 26
    • 0019834569 scopus 로고
    • End-filaments: A new structural element of vertebrate skeletal muscle thick filaments
    • Trinick, J. A. 1981. End-filaments: a new structural element of vertebrate skeletal muscle thick filaments. J. Mol. Biol 151:309-314.
    • (1981) J. Mol. Biol , vol.151 , pp. 309-314
    • Trinick, J.A.1
  • 28
    • 0021982444 scopus 로고
    • Sarcomere-associatedcytoskeletal lattices in striated muscle. reviews and hypothesis
    • J. W. Shay, editor. Plenum Publishing Corp., New York
    • Wang, K. 1985. Sarcomere-associatedcytoskeletal lattices in striated muscle. reviews and hypothesis. In Cell and Muscle Motility. Vol. 6. J. W. Shay, editor. Plenum Publishing Corp., New York. 315-369.
    • (1985) Cell and Muscle Motility , vol.6 , pp. 315-369
    • Wang, K.1
  • 29
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line
    • Wang, K., and J. Wright. 1988. Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol. 107:2199-2212.
    • (1988) J. Cell Biol. , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 30
    • 0022079716 scopus 로고
    • Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils
    • Wang, S., and M. L. Greaser. 1985. Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils. J. Muscle Res. Cell Motil. 6:293-312.
    • (1985) J. Muscle Res. Cell Motil. , vol.6 , pp. 293-312
    • Wang, S.1    Greaser, M.L.2
  • 31
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin: Effects of divalent cations on proteolytic susceptibility
    • Weeds, A. G., and B. Pope. 1977. Studies on the chymotryptic digestion of myosin: effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 32
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting, A., J. Wardale, and J. Trinick. 1989. Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205:263-268.
    • (1989) J. Mol. Biol. , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 33
    • 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., E. Fuller, and A. Forer. 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
  • 35
    • 0022259764 scopus 로고
    • Fine structure of wide and narrow vertebrate muscle Z-lines: A proposed model and computer simulation of Z-line architecture
    • Yamaguchi, M., M. Izumimoto, R. M. Robson, and M. H. Stromer. 1985. Fine structure of wide and narrow vertebrate muscle Z-lines: a proposed model and computer simulation of Z-line architecture. J. Mol. Biol. 184:621-644.
    • (1985) J. Mol. Biol. , vol.184 , pp. 621-644
    • Yamaguchi, M.1    Izumimoto, M.2    Robson, R.M.3    Stromer, M.H.4
  • 36
    • 0022362676 scopus 로고
    • Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle
    • Yanagida, T., T. Arata, and F. Oosawa. 1985. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature (Lond.). 316:366-369.
    • (1985) Nature (Lond.) , vol.316 , pp. 366-369
    • Yanagida, T.1    Arata, T.2    Oosawa, F.3
  • 37
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin, H. L., and T. P. Stossel. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature (Lond.). 281:583-586.
    • (1979) Nature (Lond.) , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2
  • 38
    • 0022646981 scopus 로고
    • Effects of mild trypsin treatment on the passive tension generation and connectin splitting in stretched skinned fibers from frog skeletal muscle
    • Yoshioka, T., H. Higuchi, S. Kimura, K. Ohashi, Y. Umazume, and K. Maruyama. 1986. Effects of mild trypsin treatment on the passive tension generation and connectin splitting in stretched skinned fibers from frog skeletal muscle. Biomed. Res. 7:181-186.
    • (1986) Biomed. Res. , vol.7 , pp. 181-186
    • Yoshioka, T.1    Higuchi, H.2    Kimura, S.3    Ohashi, K.4    Umazume, Y.5    Maruyama, K.6
  • 39
    • 0023237341 scopus 로고
    • DNase I interactions with filaments of skeletal muscles
    • Zimmer, D. B., and M. A. Goldstein. 1987. DNase I interactions with filaments of skeletal muscles. J. Muscle Res. Cell Motil. 8:30-38.
    • (1987) J. Muscle Res. Cell Motil. , vol.8 , pp. 30-38
    • Zimmer, D.B.1    Goldstein, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.