메뉴 건너뛰기




Volumn 94, Issue 5, 2003, Pages 2034-2042

Adaptations in human muscle sarcoplasmic reticulum to prolonged submaximal training

Author keywords

Ca2+ release; Ca2+ uptake; Ca2+ ATPase; Calcium homeostasis; Exercise

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 7E6; MONOCLONAL ANTIBODY A52; PROTEIN SERCA; PROTEIN SERCA1; PROTEIN SERCA2A; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 1642420443     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/japplphysiol.00244.2002     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: Its crucial role for muscle function, plasticity and disease
    • Berchtold MW, Brinkmeier H, and Müntener M. Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity and disease. Physiol Rev 80: 1216-1265, 2000.
    • (2000) Physiol Rev , vol.80 , pp. 1216-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Müntener, M.3
  • 3
    • 0025174750 scopus 로고
    • Ca-ATPase isozyme expression in sarcoplasmic reticulum is altered by chronic stimulation of skeletal muscle
    • Briggs FN, Lee KF, Feher JJ, Wechsler AS, Ohlendieck K, and Campbell KP. Ca-ATPase isozyme expression in sarcoplasmic reticulum is altered by chronic stimulation of skeletal muscle. FEBS Lett 259: 269-272, 1990.
    • (1990) FEBS Lett , vol.259 , pp. 269-272
    • Briggs, F.N.1    Lee, K.F.2    Feher, J.J.3    Wechsler, A.S.4    Ohlendieck, K.5    Campbell, K.P.6
  • 4
    • 0024577369 scopus 로고
    • Effects of exercise of varying duration on sarcoplasmic reticulum function
    • Byrd SK, Bode AK, and Klug GA. Effects of exercise of varying duration on sarcoplasmic reticulum function. J Appl Physiol 66: 1383-1388, 1989.
    • (1989) J Appl Physiol , vol.66 , pp. 1383-1388
    • Byrd, S.K.1    Bode, A.K.2    Klug, G.A.3
  • 5
    • 0025003883 scopus 로고
    • 2+-ATPase and changes in its tryptic cleavage
    • 2+-ATPase and changes in its tryptic cleavage. Eur J Biochem 195: 92-100, 1990.
    • (1990) Eur J Biochem , vol.195 , pp. 92-100
    • Dux, L.1    Green, H.J.2    Pette, D.3
  • 6
  • 8
    • 0030789142 scopus 로고    scopus 로고
    • Ryanodine receptors of striated muscles: A complex channel capable of multiple interactions
    • Franzini-Armstrong C and Protasi F. Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions. Physiol Rev 77: 699-729, 1997.
    • (1997) Physiol Rev , vol.77 , pp. 699-729
    • Franzini-Armstrong, C.1    Protasi, F.2
  • 9
    • 0034212222 scopus 로고    scopus 로고
    • 2+-regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle-fibers
    • 2+-regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle-fibers. Biochim Biophys Acta 1466: 151-168, 2000.
    • (2000) Biochim Biophys Acta , vol.1466 , pp. 151-168
    • Froemming, G.R.1    Murray, B.E.2    Harmon, S.3    Pette, D.4    Ohlendieck, K.5
  • 12
    • 0021282213 scopus 로고
    • Exercise induced fibre type transitions with regard to myosin, parvalbumin and sarcoplasmic reticulum in muscles of the rat
    • Green HJ, Klug GA, Reichmann H, Seedorf U, Wieher W, and Pette D. Exercise induced fibre type transitions with regard to myosin, parvalbumin and sarcoplasmic reticulum in muscles of the rat. Pflügers Arch 400: 432-438, 1984.
    • (1984) Pflügers Arch , vol.400 , pp. 432-438
    • Green, H.J.1    Klug, G.A.2    Reichmann, H.3    Seedorf, U.4    Wieher, W.5    Pette, D.6
  • 13
    • 0021895138 scopus 로고
    • 2+-indicators with greatly improved fluorescence properties
    • 2+-indicators with greatly improved fluorescence properties. J Biol Chem 260: 3440-3450, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 14
    • 0030861193 scopus 로고    scopus 로고
    • Early functional and biochemical adaptations to low-frequency to low-frequency stimulation of rabbit fast-twitch muscle
    • Hicks A, Ohlendieck K, Göpel SO, and Pette D. Early functional and biochemical adaptations to low-frequency to low-frequency stimulation of rabbit fast-twitch muscle. Am J Physiol Cell Physiol 273: C297-C305, 1997.
    • (1997) Am J Physiol Cell Physiol , vol.273
    • Hicks, A.1    Ohlendieck, K.2    Göpel, S.O.3    Pette, D.4
  • 15
    • 0035868808 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum function and muscle contractile character following fatiguing exercise in humans
    • Hill CA, Thompson MW, Ruell PA, Thom JM, and White MJ. Sarcoplasmic reticulum function and muscle contractile character following fatiguing exercise in humans. J Physiol 531: 871-878, 2001.
    • (2001) J Physiol , vol.531 , pp. 871-878
    • Hill, C.A.1    Thompson, M.W.2    Ruell, P.A.3    Thom, J.M.4    White, M.J.5
  • 17
    • 0019860233 scopus 로고
    • The effect of exercise training on sarcoplasmic reticulum function in fast and slow skeletal muscle
    • Kim DH, Wible GS, Witzmann FA, and Fitts RH. The effect of exercise training on sarcoplasmic reticulum function in fast and slow skeletal muscle. Life Sci 28: 2671-2677, 1981.
    • (1981) Life Sci , vol.28 , pp. 2671-2677
    • Kim, D.H.1    Wible, G.S.2    Witzmann, F.A.3    Fitts, R.H.4
  • 18
    • 0032488809 scopus 로고    scopus 로고
    • 2+-ATPase in low-frequency stimulated rabbit muscle
    • 2+-ATPase in low-frequency stimulated rabbit muscle. FEBS Lett 422: 381-384, 1998.
    • (1998) FEBS Lett , vol.422 , pp. 381-384
    • Klebl, B.M.1    Ayoub, T.A.2    Pette, D.3
  • 20
    • 0026691835 scopus 로고
    • Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps
    • Lytton J, Westlin M, Burk SE, Shull GE, and MacLennan DH. Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps. J Biol Chem 267: 14483-14489, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 14483-14489
    • Lytton, J.1    Westlin, M.2    Burk, S.E.3    Shull, G.E.4    MacLennan, D.H.5
  • 21
    • 0028310359 scopus 로고
    • Effects of intensified endurance training on the concentration of Na,K-ATPase and Ca-ATPase in human skeletal muscle
    • Madsen K, Franch J, and Clausen T. Effects of intensified endurance training on the concentration of Na,K-ATPase and Ca-ATPase in human skeletal muscle. Acta Physiol Scand 150: 251-258, 1989.
    • (1989) Acta Physiol Scand , vol.150 , pp. 251-258
    • Madsen, K.1    Franch, J.2    Clausen, T.3
  • 22
    • 0030592166 scopus 로고    scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum: Facts, speculations and questions for the future
    • 2+-ATPase of sarcoplasmic reticulum: facts, speculations and questions for the future. Biochim Biophys Acta 1275: 111-117, 1996.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 111-117
    • Martonosi, A.N.1
  • 24
    • 0025254169 scopus 로고
    • Calcium sequestration by isolated sarcoplasmic reticulum: Real time monitoring using ratiometric dual emission spectrofluorometry and the fluorescent calcium binding indo-I
    • O'Brien PJ. Calcium sequestration by isolated sarcoplasmic reticulum: real time monitoring using ratiometric dual emission spectrofluorometry and the fluorescent calcium binding indo-I. Mol Cell Biochem 94: 113-119, 1990.
    • (1990) Mol Cell Biochem , vol.94 , pp. 113-119
    • O'Brien, P.J.1
  • 25
    • 0026022922 scopus 로고
    • Myocardial Ca-sequestration failure and compensatory increase in Ca-ATPase with congestive cardiomyopathy: Kinetic characterization by a homogenate microassay using real-time ratiometric indo-I spectrofluorometry
    • O'Brien PJ, Shen H, Weiler J, Mirsalami M, and Julian R. Myocardial Ca-sequestration failure and compensatory increase in Ca-ATPase with congestive cardiomyopathy: kinetic characterization by a homogenate microassay using real-time ratiometric indo-I spectrofluorometry. Mol Cell Biochem 102: 1-12, 1991.
    • (1991) Mol Cell Biochem , vol.102 , pp. 1-12
    • O'Brien, P.J.1    Shen, H.2    Weiler, J.3    Mirsalami, M.4    Julian, R.5
  • 26
    • 0026316261 scopus 로고
    • Analysis of excitation-contraction coupling components in chronically stimulated canine skeletal muscle
    • Ohlendieck K, Briggs FN, Lee KF, Wechsler AS, and Campbell KP. Analysis of excitation-contraction coupling components in chronically stimulated canine skeletal muscle. Eur J Biochem 202: 739-747, 1991.
    • (1991) Eur J Biochem , vol.202 , pp. 739-747
    • Ohlendieck, K.1    Briggs, F.N.2    Lee, K.F.3    Wechsler, A.S.4    Campbell, K.P.5
  • 29
    • 0031023872 scopus 로고    scopus 로고
    • Mammalian skeletal muscle fiber type transitions
    • Pette D and Staron RS. Mammalian skeletal muscle fiber type transitions. Int Rev Cytol 170: 143-223, 1997.
    • (1997) Int Rev Cytol , vol.170 , pp. 143-223
    • Pette, D.1    Staron, R.S.2
  • 30
    • 0033034939 scopus 로고    scopus 로고
    • What does chronic electrical stimulation teach us about muscle plasticity?
    • Pette D and Vrbova C. What does chronic electrical stimulation teach us about muscle plasticity? Muscle Nerve 22: 666-677, 1999.
    • (1999) Muscle Nerve , vol.22 , pp. 666-677
    • Pette, D.1    Vrbova, C.2
  • 31
    • 0029002014 scopus 로고
    • Measurement of sarcoplasmic reticulum function in mammalian skeletal muscle. Technical aspects
    • Ruell PA, Booth J, McKenna MJ, and Sutton JR. Measurement of sarcoplasmic reticulum function in mammalian skeletal muscle. Technical aspects. Anal Biochem 228: 194-201, 1995.
    • (1995) Anal Biochem , vol.228 , pp. 194-201
    • Ruell, P.A.1    Booth, J.2    McKenna, M.J.3    Sutton, J.R.4
  • 32
    • 0002887220 scopus 로고
    • Skeletal muscle adaptability: Significance for metabolism and performance
    • Bethesda, MD: Am. Physiol. Soc., sect. 10, chapt. 19
    • Saltin B and Gollnick PD. Skeletal muscle adaptability: significance for metabolism and performance. In: Handbook of Physiology. Skeletal Muscle. Bethesda, MD: Am. Physiol. Soc., 1983, sect. 10, chapt. 19, p. 555-631.
    • (1983) Handbook of Physiology. Skeletal Muscle , pp. 555-631
    • Saltin, B.1    Gollnick, P.D.2
  • 33
    • 0015579498 scopus 로고
    • A simplified method for the quantitative assay of small amounts of protein in biologic material
    • Schacterle GR and Pollock RL. A simplified method for the quantitative assay of small amounts of protein in biologic material. Anal Biochem 51: 654-655, 1973.
    • (1973) Anal Biochem , vol.51 , pp. 654-655
    • Schacterle, G.R.1    Pollock, R.L.2
  • 34
    • 0027253394 scopus 로고
    • Regulation of sarcoplasmic reticulum gene expression by hindlimb unweighting
    • Schulte LM, Navarro J, and Kandarian SC. Regulation of sarcoplasmic reticulum gene expression by hindlimb unweighting. Am J Physiol Cell Physiol 264: C1308-C1315, 1993.
    • (1993) Am J Physiol Cell Physiol , vol.264
    • Schulte, L.M.1    Navarro, J.2    Kandarian, S.C.3
  • 38
    • 0035281831 scopus 로고    scopus 로고
    • ATP utilization for calcium uptake and force production in different types of human muscle fibres
    • Szentesi P, Zaremba W, van Mechelen W, and Stienen GJM. ATP utilization for calcium uptake and force production in different types of human muscle fibres. J Physiol 531: 393-403, 2001.
    • (2001) J Physiol , vol.531 , pp. 393-403
    • Szentesi, P.1    Zaremba, W.2    Van Mechelen, W.3    Stienen, G.J.M.4
  • 42
    • 0031880450 scopus 로고    scopus 로고
    • Functional aspects of skeletal muscle contractile apparatus and sarcoplasmic reticulum after fatigue
    • Williams JH, Ward CW, Spangenburg EE, and Nelson RM. Functional aspects of skeletal muscle contractile apparatus and sarcoplasmic reticulum after fatigue. J Appl Physiol 85: 619-626, 1998.
    • (1998) J Appl Physiol , vol.85 , pp. 619-626
    • Williams, J.H.1    Ward, C.W.2    Spangenburg, E.E.3    Nelson, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.