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Volumn 296, Issue 6, 2009, Pages

Properties of easily releasable myofilaments: Are they the first step in myofibrillar protein turnover?

Author keywords

Calpain; Muscle; Proteasome

Indexed keywords

CALPAIN; MUSCLE PROTEIN;

EID: 66749160236     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00022.2009     Document Type: Article
Times cited : (37)

References (48)
  • 1
    • 0346923055 scopus 로고
    • Diabetes enhances calpain degradation of cardiac myofibrils and easily releasable myofilaments
    • edited by M Nagano and NS Dhalla. New York: Raven
    • Belcastro AN, Machan C, Gilchrist JS. Diabetes enhances calpain degradation of cardiac myofibrils and easily releasable myofilaments. In: The Diabetic Heart, edited by M Nagano and NS Dhalla. New York: Raven, 1991, p. 301-310.
    • (1991) The Diabetic Heart , pp. 301-310
    • Belcastro, A.N.1    Machan, C.2    Gilchrist, J.S.3
  • 2
    • 0025877817 scopus 로고
    • Regulation of ATP-stimulated releasable myofilaments from cardiac and skeletal muscle myofibrils
    • Belcastro AN, Scrubb J, Gilchrist JS. Regulation of ATP-stimulated releasable myofilaments from cardiac and skeletal muscle myofibrils. Mol Cell Biochem 103: 113-120, 1991.
    • (1991) Mol Cell Biochem , vol.103 , pp. 113-120
    • Belcastro, A.N.1    Scrubb, J.2    Gilchrist, J.S.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein ultilizing the principle of dye-binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein ultilizing the principle of dye-binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0022550946 scopus 로고
    • Effect of starvation or treatment with corticosterone on the amount of easily releasable myofilaments in rat skeletal muscles
    • Dahlmann B, Rutschmann M, Reinauer H. Effect of starvation or treatment with corticosterone on the amount of easily releasable myofilaments in rat skeletal muscles. Biochem J 234: 659-664, 1986. (Pubitemid 16028392)
    • (1986) Biochemical Journal , vol.234 , Issue.3 , pp. 659-664
    • Dahlmann, B.1    Rutschmann, M.2    Reinauer, H.3
  • 7
    • 0017101433 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme. Biochemistry 15: 2159-2167, 1976.
    • (1976) Biochemistry , vol.15 , pp. 2159-2167
    • Dayton, W.R.1    Reville, W.J.2    Goll, D.E.3    Stromer, M.H.4
  • 9
    • 21244496302 scopus 로고    scopus 로고
    • Apoptosis in muscle atrophy: Relevance to sarcopenia
    • DOI 10.1016/j.exger.2005.04.003, PII S0531556505000653
    • Dupont-Versteegden EE. Apoptosis in muscle atrophy: relevance to sarcopenia. Exp Gerontol 40: 473-481, 2005. (Pubitemid 40884500)
    • (2005) Experimental Gerontology , vol.40 , Issue.6 , pp. 473-481
    • Dupont-Versteegden, E.E.1
  • 10
    • 0016883431 scopus 로고
    • Compositional studies of myofibrils from rabbit striated muscle
    • Etlinger JD, Zak R, Fischman DA. Compositional studies of myofibrils from rabbit striated muscle. J Cell Biol 68: 123-141, 1976.
    • (1976) J Cell Biol , vol.68 , pp. 123-141
    • Etlinger, J.D.1    Zak, R.2    Fischman, D.A.3
  • 11
    • 0016771837 scopus 로고
    • Isolation of newly synthesized myosin filaments from skeletal muscle homogenates and myofibrils
    • Etlinger JD, Zak R, Fischman DA, Rabinowitz M. Isolation of newly synthesized myosin filaments from skeletal muscle homogenates and myofibrils. Nature 255: 259-261, 1975.
    • (1975) Nature , vol.255 , pp. 259-261
    • Etlinger, J.D.1    Zak, R.2    Fischman, D.A.3    Rabinowitz, M.4
  • 12
    • 0014690566 scopus 로고
    • Protein turnover in skeletal muscle. I. Protein catabolism during work-induced hypertrophy and growth induced with growth hormone
    • Goldberg AL. Protein turnover in skeletal muscle. I. Protein catabolism during work-induced hypertrophy and growth induced with growth hormone. J Biol Chem 244: 3217-3222, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 3217-3222
    • Goldberg, A.L.1
  • 13
    • 0014690578 scopus 로고
    • Protein turnover in skeletal muscle. II. Effects of denervation and cortisone on protein catabolism in skeletal muscle
    • Goldberg AL. Protein turnover in skeletal muscle. II. Effects of denervation and cortisone on protein catabolism in skeletal muscle. J Biol Chem 244: 3223-3229, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 3223-3229
    • Goldberg, A.L.1
  • 14
    • 0025762431 scopus 로고
    • Cell-free incorporation of newly synthesized myosin subunits into thick filaments
    • Goldfine SM, Einheber S, Fischman DA. Cell-free incorporation of newly synthesized myosin subunits into thick filaments. J Muscle Res Cell Motil 12: 161-170, 1991.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 161-170
    • Goldfine, S.M.1    Einheber, S.2    Fischman, D.A.3
  • 15
    • 0025832699 scopus 로고
    • Role of the Z band in the mechanical properties of the heart
    • Goldstein MA, Schroeter JP, Michael LH. Role of the Z band in the mechanical properties of the heart. FASEB J 5: 2167-2174, 1991. (Pubitemid 21905850)
    • (1991) FASEB Journal , vol.5 , Issue.8 , pp. 2167-2174
    • Goldstein, M.A.1    Schroeter, J.P.2    Michael, L.H.3
  • 16
    • 0025868336 scopus 로고
    • Studies of the α-actinin/actin interaction in the Z-disk by using calpain
    • Goll DE, Dayton WR, Singh I, Robson RM. Studies of the α-actinin/actin interaction in the Z-disk by using calpain. J Biol Chem 266: 8501-8510, 1991. (Pubitemid 21906538)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.13 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4
  • 17
    • 0003134732 scopus 로고
    • Skeletal muscle proteases and protein turnover
    • edited by DR Campion, GJ Hausman, and RJ Martin. New York: Plenum
    • Goll DE, Kleese WC, Szpacenko A. Skeletal muscle proteases and protein turnover. In: Animal Growth Regulation, edited by DR Campion, GJ Hausman, and RJ Martin. New York: Plenum, 1989, p. 141-182.
    • (1989) Animal Growth Regulation , pp. 141-182
    • Goll, D.E.1    Kleese, W.C.2    Szpacenko, A.3
  • 18
    • 45949101825 scopus 로고    scopus 로고
    • Myofibrillar protein turnover: The proteasome and the calpains
    • Goll DE, Neti G, Mares SW, Thompson VF. Myofibrillar protein turnover: the proteasome and the calpains. J Anim Sci 86: 19-35, 2008.
    • (2008) J Anim Sci , vol.86 , pp. 19-35
    • Goll, D.E.1    Neti, G.2    Mares, S.W.3    Thompson, V.F.4
  • 21
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall AG, Bardawill CJ, David MM. Determination of serum proteins by means of the biuret reaction. J Biol Chem 177: 751-766, 1949.
    • (1949) J Biol Chem , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 23
    • 0023895662 scopus 로고
    • Small-angle x-ray scattering investigation of the solution structure of troponin C
    • Hubbard SR, Hodgson KO, Doniach S. Small-angle X-ray scattering investigation of the solution structure of troponin C. J Biol Chem 263: 4151-4158, 1988. (Pubitemid 18096588)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.9 , pp. 4151-4158
    • Hubbard, S.R.1    Hodgson, K.O.2    Doniach, S.3
  • 24
    • 0027026199 scopus 로고
    • Ovine skeletal muscle multicatalytic proteinase complex (proteasome): Purification, characterization, and comparison of its effects on myofibrils with μ-calpains
    • Koohmaraie M. Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization, and comparison of its effects on myofibrils with μ-calpains. J Anim Sci 70: 3697-3708, 1992.
    • (1992) J Anim Sci , vol.70 , pp. 3697-3708
    • Koohmaraie, M.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0021959998 scopus 로고
    • Identical distribution of fluorescently labeled brain and muscle actins in living cardiac fibroblasts and myocytes
    • DOI 10.1083/jcb.100.1.292
    • McKenna N, Meigs JB, Wang YL. Identical distribution of fluorescently labeled brain and muscle actins in living cardiac fibroblasts and myocytes. J Cell Biol 100: 292-296, 1985. (Pubitemid 15151906)
    • (1985) Journal of Cell Biology , vol.100 , Issue.1 , pp. 292-296
    • McKenna, N.1    Meigs, J.B.2    Wang, Y.-L.3
  • 30
    • 0033804049 scopus 로고    scopus 로고
    • Protein diffusion in living skeletal muscle fibers: Dependence on protein size, fiber type, and contraction
    • Papadopoulos S, Jürgens KD, Gros G. Protein diffusion in living skeletal muscle fibers: dependence on protein size, fiber type, and contraction. Biophys J 79: 2084-2094, 2000.
    • (2000) Biophys J , vol.79 , pp. 2084-2094
    • Papadopoulos, S.1    Jürgens, K.D.2    Gros, G.3
  • 31
    • 21844525142 scopus 로고
    • Easily releasable myofilaments in post mortem bovine muscle
    • Reville WJ, Murray BA, Ahern S, Zeece MG. Easily releasable myofilaments in post mortem bovine muscles. Sci Aliments 14: 431-440, 1994. (Pubitemid 24816970)
    • (1994) Sciences des Aliments , vol.14 , Issue.4 , pp. 431
    • Reville, W.J.1    Murray, B.A.2    Ahern, S.3    Zeece, M.G.4
  • 32
    • 12144262858 scopus 로고    scopus 로고
    • Skeletal muscle fiber atrophy: Altered thin filament density changes slow fiber force and shortening velocity
    • DOI 10.1152/ajpcell.00386.2004
    • Riley DA, Bain JLW, Romatowshi G, Fitts RH. Skeletal muscle atrophy: altered thin filament density changes in slow fiber force and shortening velocity. Am J Physiol Cell Physiol 288: C360-C365, 2005. (Pubitemid 40105347)
    • (2005) American Journal of Physiology - Cell Physiology , vol.288 , Issue.2
    • Riley, D.A.1    Bain, J.L.W.2    Romatowski, J.G.3    Fitts, R.H.4
  • 33
    • 0014321738 scopus 로고
    • Determination of proteins in "Tris" buffer by the biuret reaction
    • Robson RM, Goll DE, Temple MJ. Determination of proteins in "Tris" buffer by the biuret reaction. Anal Biochem 24: 339-341, 1968.
    • (1968) Anal Biochem , vol.24 , pp. 339-341
    • Robson, R.M.1    Goll, D.E.2    Temple, M.J.3
  • 36
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • DOI 10.1074/jbc.271.43.26690
    • Solomon V, Goldberg AL. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J Biol Chem 271: 26690-26697, 1996. (Pubitemid 26359075)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 38
    • 0032869609 scopus 로고    scopus 로고
    • Exchange of α-actinin in isolated rigor myofibrils
    • DOI 10.1023/A:1005561912352
    • Swartz DR. Exchange of α-actinin in isolated myofibrils. J Muscle Res Cell Motil 20: 457-467, 1999. (Pubitemid 29476301)
    • (1999) Journal of Muscle Research and Cell Motility , vol.20 , Issue.5-6 , pp. 457-467
    • Swartz, D.R.1
  • 40
    • 0033649520 scopus 로고    scopus 로고
    • Purification of μ-calpain, m-calpain, and calpastatin from animal tissues
    • edited by JS Elce. Totowa, NJ: Humana
    • Thompson VF, Goll DE. Purification of μ-calpain, m-calpain, and calpastatin from animal tissues. In: Methods in Molecular Biology. Calpain Methods and Protocols, edited by JS Elce. Totowa, NJ: Humana, 2000, vol.144, p. 3-16.
    • (2000) Methods in Molecular Biology. Calpain Methods and Protocols , vol.144 , pp. 3-16
    • Thompson, V.F.1    Goll, D.E.2
  • 41
    • 0034653992 scopus 로고    scopus 로고
    • A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases
    • DOI 10.1006/abio.1999.4475
    • Thompson VF, Saldaña S, Cong J, Goll DE. A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases. Anal Biochem 279: 170-178, 2000. (Pubitemid 30165005)
    • (2000) Analytical Biochemistry , vol.279 , Issue.2 , pp. 170-178
    • Thompson, V.F.1    Saldana, S.2    Cong, J.3    Goll, B.E.4
  • 42
    • 0037066395 scopus 로고    scopus 로고
    • The calpain system in human placenta
    • DOI 10.1016/S0024-3205(02)01506-0, PII S0024320502015060
    • Thompson VF, Saldaña S, Cong J, Luedke DM, Goll DE. The calpain system in human placenta. Life Sci 70: 2493-12408, 2002. (Pubitemid 34267038)
    • (2002) Life Sciences , vol.70 , Issue.21 , pp. 2493-2508
    • Thompson, V.F.1    Saldaa, S.2    Cong, J.3    Luedke, D.M.4    Goll, D.E.5
  • 44
    • 0019888648 scopus 로고
    • Easily releasable myofilaments from skeletal and cardiac muscles maintained in vitro. Role in myofibrillar assembly and turnover
    • van der Westhuyzen DR, Matsumoto K, Etlinger JD. Easily releasable myofilaments from skeletal and cardiac muscles maintained in vitro. Role in myofibrillar assembly and turnover. J Biol Chem 256: 11791-11797, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 11791-11797
    • Van Der Westhuyzen, D.R.1    Matsumoto, K.2    Etlinger, J.D.3
  • 46
    • 0032797384 scopus 로고    scopus 로고
    • Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism
    • Williams AB, DeCourten-Myers GM, Fisher JE, Luo G, Sun X, Hasselgren PO. Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism. FASEB J 13: 1435-1443, 1999. (Pubitemid 29382511)
    • (1999) FASEB Journal , vol.13 , Issue.11 , pp. 1435-1443
    • Williams, A.B.1    Decourten-Myers, G.M.2    Fischer, J.E.3    Luo, G.4    Sun, X.5    Hasselgren, P.-O.6
  • 48
    • 0021112289 scopus 로고
    • Quantitative determination of myosin and actin in rabbit skeletal muscle
    • Yates LD, Greaser ML. Quantitative determination of myosin and actin in rabbit skeletal muscle. J Mol Biol 168: 123-141, 1983.
    • (1983) J Mol Biol , vol.168 , pp. 123-141
    • Yates, L.D.1    Greaser, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.