메뉴 건너뛰기




Volumn 64, Issue 12, 2000, Pages 2686-2688

Effects of corticosterone on connectin content and protein breakdown in rat skeletal muscle

Author keywords

Calpain; Connectin; Corticosterone; Muscle protein breakdown

Indexed keywords

CALPAIN; CONNECTIN; CORTICOSTERONE; HISTIDINE DERIVATIVE; MUSCLE PROTEIN; PROTEIN KINASE;

EID: 0034567636     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.2686     Document Type: Article
Times cited : (15)

References (23)
  • 3
    • 0024852594 scopus 로고
    • Isolation ofa-con-nectin, an elastic protein, from rabbit skeletal muscle. X
    • Kimura, S. and Maruyama, K., Isolation ofa-con-nectin, an elastic protein, from rabbit skeletal muscle. XBiochem.,106,952-954 (1989).
    • (1989) Biochem. , vol.106 , pp. 952-954
    • Kimura, S.1    Maruyama, K.2
  • 4
    • 0026510571 scopus 로고
    • Characterization and localization of cx-connectm (Titin 1): An elastic protein isolated from rabbit skeletal muscle. X
    • Kimura, S., Matsuura, T., Ohtsuka, S., Nakauchi, Y., Matsuno, A., and Maruyama, K., Characterization and localization of cx-connectm (titin 1): an elastic protein isolated from rabbit skeletal muscle. XMuscle Res. Cell Motil,13,39-47 (1992).
    • (1992) Muscle Res. Cell Motil , vol.13 , pp. 39-47
    • Kimura, S.1    Matsuura, T.2    Ohtsuka, S.3    Nakauchi, Y.4    Matsuno, A.5    Maruyama, K.6
  • 5
    • 0018768983 scopus 로고
    • Effect of glucocorticoid administration on the rate of muscle protein breakdownin vivoin rats, as measured by urinary excretion of NT-methylhistidine
    • T-methylhistidine.Biochem.X,178,139-146 (1979).
    • (1979) Biochem , vol.10 , Issue.178 , pp. 139-146
    • Tomas, F.M.1    Munro, H.N.2    Young, V.R.3
  • 6
    • 0022521950 scopus 로고
    • Synergism of triiodothyronine and corticosterone on muscle protein breakdown
    • Hayashi, K., Kayali, A. G., and Young, V. R., Synergism of triiodothyronine and corticosterone on muscle protein breakdown.Biochim. Biophys. Acta,883,106-111 (1986).
    • (1986) Biochim. Biophys. Acta , vol.883 , pp. 106-111
    • Hayashi, K.1    Kayali, A.G.2    Young, V.R.3
  • 7
    • 0018751697 scopus 로고
    • Calcium-dependent regulation of protein synthesis and degradation in muscle
    • Kameyama, T. and Etlinger, J. D., Calcium-dependent regulation of protein synthesis and degradation in muscle.Nature,279,344-346 (1979).
    • (1979) Nature , vol.279 , pp. 344-346
    • Kameyama, T.1    Etlinger, J.D.2
  • 8
    • 0019175054 scopus 로고
    • The effects of calcium ions, ionophore A23187 and inhibition of energy metabolism on protein degradation in the rat diaphragm and epitroc-hlearis
    • Sugden, P. H., The effects of calcium ions, ionophore A23187 and inhibition of energy metabolism on protein degradation in the rat diaphragm and epitroc-hlearisin vitro. Biochem.X,190,593-603 (1980).
    • (1980) In Vitro. Biochem , vol.10 , Issue.190 , pp. 593-603
    • Sugden, P.H.1
  • 9
    • 0022402473 scopus 로고
    • Regulation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium. X
    • Zeman, R. J., Kameyama, T., Matsumoto, K., Bernstein, P., and Etlinger, J. D., Regulation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium. XBiol. Chem.,260,13619-13624 (1985).
    • (1985) Biol. Chem. , vol.260 , pp. 13619-13624
    • Zeman, R.J.1    Kameyama, T.2    Matsumoto, K.3    Bernstein, P.4    Etlinger, J.D.5
  • 10
    • 0023124150 scopus 로고
    • Differential effects of acute changes in cell Ca2+concentration on myofibrillar and non-myofibrillar protein breakdown in the rat extensor digitorum longus musclein vitro.Assessment by production of tyrosine and NT-methylhisti-dine
    • T-methylhisti-dine.Biochem.X,241,121-127 (1987).
    • (1987) Biochem , vol.10 , Issue.241 , pp. 121-127
    • Goodman, M.N.1
  • 11
    • 0029071646 scopus 로고
    • Functions of the proteasome: The lysis at the end of the tunnel
    • Goldberg, A. L., Functions of the proteasome: the lysis at the end of the tunnel.Science,268,522-523 (1995).
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 12
    • 0022376371 scopus 로고
    • Proteolysis of skeletal muscle in response to acute elevation of plasma cortisol in man
    • Legaspi, A., Albert, J. D., Calvano, S. E., Brennan, M. F., and Lowry, S. F., Proteolysis of skeletal muscle in response to acute elevation of plasma cortisol in man.Surg. Forum,36,16-18 (1985).
    • (1985) Surg. Forum , vol.36 , pp. 16-18
    • Legaspi, A.1    Albert, J.D.2    Calvano, S.E.3    Brennan, M.F.4    Lowry, S.F.5
  • 13
    • 0020521619 scopus 로고
    • Time course of the effect of catabolic doses of corticosterone on protein turnover in rat skeletal muscle and liver
    • Odedra, B. R., Bates, P. C., and Millward, D. J., Time course of the effect of catabolic doses of corticosterone on protein turnover in rat skeletal muscle and liver.Biochem.X,214,617-627 (1983).
    • (1983) Biochem , vol.10 , Issue.214 , pp. 617-627
    • Odedra, B.R.1    Bates, P.C.2    Millward, D.J.3
  • 14
    • 0023261107 scopus 로고
    • Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis
    • Kayali, A. G., Young, V. R., and Goodman, M. N., Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis.Am. J. Physiol.,252, E621-E626 (1987).
    • (1987) Am. J. Physiol. , vol.252 , pp. E621-E626
    • Kayali, A.G.1    Young, V.R.2    Goodman, M.N.3
  • 15
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. X
    • Solomon, V. and Goldberg, A. L., Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. XBiol. Chem.,271,26690-26697 (1996).
    • (1996) Biol. Chem. , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 16
    • 0023318433 scopus 로고
    • High performance liquid chromatographic method for the analysis of NT-methylhistidine in food, chicken excreta, and rat urine. X
    • T-methylhistidine in food, chicken excreta, and rat urine. XNutr. Sci. Vitaminol.,33,151-156 (1987).
    • (1987) Nutr. Sci. Vitaminol. , vol.33 , pp. 151-156
    • Hayashi, K.1    Maeda, Y.2    Toyomizu, M.3    Tomita, Y.4
  • 17
    • 0023505578 scopus 로고
    • Inhibition of chicken calpain by proteins of the cystatin superfamily and a2-niacroglobu-lin
    • 2-niacroglobu-lin.Biochem.X,248,589-594 (1987).
    • (1987) Biochem , vol.10 , Issue.248 , pp. 589-594
    • Crawford, C.1
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent. X
    • Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. XBiol. Chem.,193,265-275 (1951).
    • (1951) Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 19
    • 0024707814 scopus 로고
    • A method measuring a gigantic protein by SDS gel electrophoresis
    • Hattori, A. and Tatsumi, R., A method measuring a gigantic protein by SDS gel electrophoresis.Biochemistry(Jpn.),8,717-719 (1989).
    • (1989) Biochemistry(Jpn.) , vol.8 , pp. 717-719
    • Hattori, A.1    Tatsumi, R.2
  • 20
    • 0015501113 scopus 로고
    • Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methyl-histidine and its NT-acetyl derivative. X
    • T-acetyl derivative. XBiol. Chem.,247,3592-3600 (1972).
    • (1972) Biol. Chem. , vol.247 , pp. 3592-3600
    • Young, V.R.1    Alexis, S.D.2    Balica, B.S.3    Munro, H.N.4
  • 21
    • 0346792188 scopus 로고
    • Changes in tenderness of meat during postmortem aging
    • Takahashi, K., Changes in tenderness of meat during postmortem aging.Jpn. J. Zootech. Sci.,54,423-436 (1983).
    • (1983) Jpn. J. Zootech. Sci. , vol.54 , pp. 423-436
    • Takahashi, K.1
  • 22
    • 0026006653 scopus 로고
    • Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
    • Medina, R., Wing, S. S., Haas, A., and Goldberg, A. L., Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy.Biomed. Biochim. Acta,50,347-356 (1991).
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 347-356
    • Medina, R.1    Wing, S.S.2    Haas, A.3    Goldberg, A.L.4
  • 23
    • 0028212481 scopus 로고
    • Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasome. X
    • Mitch, W. E., Medina, R., Greiber, S., May, R. C., England, B. K., Price, S. R., Bailey, J. L., and Goldberg, A. L., Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasome. XClin. Invest.,93,2127-2133 (1994).
    • (1994) Clin. Invest. , vol.93 , pp. 2127-2133
    • Mitch, W.E.1    Medina, R.2    Greiber, S.3    May, R.C.4    England, B.K.5    Price, S.R.6    Bailey, J.L.7    Goldberg, A.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.