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Volumn 35, Issue 5, 2003, Pages 665-675

Regulation of proteolysis during reloading of the unweighted soleus muscle

Author keywords

Calpains; Cathepsins; Proteasome; Recovery; Simulated weightlessness; Skeletal muscle; Ubiquitin

Indexed keywords

CATHEPSIN D; MESSENGER RNA; PROTEASOME; UBIQUITIN;

EID: 0037401709     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(03)00004-9     Document Type: Article
Times cited : (62)

References (37)
  • 3
    • 1542352846 scopus 로고    scopus 로고
    • Mechanism of ubiquitination and proteasome-dependent proteolysis in skeletal muscle
    • J. Zempleni, H. Daniel (Eds.). Wallingford, Oxon: CAB International, in press
    • Attaix, D., Combaret, L., Kee, A., & Taillandier, D. (2003). Mechanism of ubiquitination and proteasome-dependent proteolysis in skeletal muscle. In J. Zempleni, H. Daniel (Eds.), Molecular nutrition. Wallingford, Oxon: CAB International, in press.
    • (2003) Molecular nutrition
    • Attaix, D.1    Combaret, L.2    Kee, A.3    Taillandier, D.4
  • 5
    • 0026555037 scopus 로고
    • Proteases and proteolysis in the lysosome
    • Bohley P., Seglen P.O. Proteases and proteolysis in the lysosome. Experientia. 48:1992;151-157.
    • (1992) Experientia , vol.48 , pp. 151-157
    • Bohley, P.1    Seglen, P.O.2
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry. 162:1987;156-159.
    • (1987) Analytical Biochemistry , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0031626721 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway of intracellular protein degradation: Implications for muscle atrophy during unloading
    • DeMartino G.N., Ordway G.A. Ubiquitin-proteasome pathway of intracellular protein degradation: implications for muscle atrophy during unloading. Exercise and Sport Sciences Reviews. 26:1998;219-252.
    • (1998) Exercise and Sport Sciences Reviews , vol.26 , pp. 219-252
    • DeMartino, G.N.1    Ordway, G.A.2
  • 9
    • 0035745756 scopus 로고    scopus 로고
    • Functional and structural adaptations of skeletal muscle to microgravity
    • Fitts R.H., Riley D.R., Widrick J.J. Functional and structural adaptations of skeletal muscle to microgravity. Journal of Experimental Biology. 204:2001;3201-3208.
    • (2001) Journal of Experimental Biology , vol.204 , pp. 3201-3208
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 10
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiological Reviews. 82:2002;373-428.
    • (2002) Physiological Reviews , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 12
    • 0002656887 scopus 로고
    • The dynamics of ubiquitin pools within skeletal muscle
    • M. Schlesinger, A. Hershko (Eds.), Cold Spring Harbor: Cold Spring Harbor Laboratory
    • Haas, A. L. & Riley, D.A. (1988). The dynamics of ubiquitin pools within skeletal muscle. In M. Schlesinger, A. Hershko (Eds.), The ubiquitin system (pp. 178-185), Cold Spring Harbor: Cold Spring Harbor Laboratory.
    • (1988) The ubiquitin system , pp. 178-185
    • Haas, A.L.1    Riley, D.A.2
  • 13
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey J.W.B. Translational control in mammalian cells. Annual Review of Biochemistry. 60:1991;717-755.
    • (1991) Annual Review of Biochemistry , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 15
    • 0031794724 scopus 로고    scopus 로고
    • Regulatory signals in messenger RNA: Determinants of nutrient-gene interaction and metabolic compartmentation
    • Hesketh J.E., Vasconcelos M.H., Bermano G. Regulatory signals in messenger RNA: determinants of nutrient-gene interaction and metabolic compartmentation. British Journal of Nutrition. 80:1998;307-321.
    • (1998) British Journal of Nutrition , vol.80 , pp. 307-321
    • Hesketh, J.E.1    Vasconcelos, M.H.2    Bermano, G.3
  • 17
    • 0025317119 scopus 로고
    • Running during recovery from hindlimb suspension induces transient muscle injury
    • Kasper C.E., White T.P., Maxwell L.C. Running during recovery from hindlimb suspension induces transient muscle injury. Journal of Applied Physiology. 68:1990;533-539.
    • (1990) Journal of Applied Physiology , vol.68 , pp. 533-539
    • Kasper, C.E.1    White, T.P.2    Maxwell, L.C.3
  • 18
    • 0027498075 scopus 로고
    • Distinguishing unloading-induced versus reloading induced changes in rat soleus muscle
    • Krippendorf B.B., Riley D.A. Distinguishing unloading-induced versus reloading induced changes in rat soleus muscle. Muscle & Nerve. 16:1993;99-108.
    • (1993) Muscle & Nerve , vol.16 , pp. 99-108
    • Krippendorf, B.B.1    Riley, D.A.2
  • 19
    • 0028354213 scopus 로고
    • Temporal changes in sarcomere lesions of rat adductor longus muscles during hindlimb reloading
    • Krippendorf B.B., Riley D.A. Temporal changes in sarcomere lesions of rat adductor longus muscles during hindlimb reloading. Anatomical Record. 238:1994;304-310.
    • (1994) Anatomical Record , vol.238 , pp. 304-310
    • Krippendorf, B.B.1    Riley, D.A.2
  • 21
    • 0001602527 scopus 로고    scopus 로고
    • Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway
    • Kwon Y.T., Kashina A.S., Varshavsky A. Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Molecular Cell Biology. 19:1999;182-193.
    • (1999) Molecular Cell Biology , vol.19 , pp. 182-193
    • Kwon, Y.T.1    Kashina, A.S.2    Varshavsky, A.3
  • 23
    • 0032169461 scopus 로고    scopus 로고
    • Gallium arsenide modulates proteolytic cathepsin activities and antigen processing by macrophages
    • Lewis T.A., Hartmann C.B., McCoy K.L. Gallium arsenide modulates proteolytic cathepsin activities and antigen processing by macrophages. Journal of Immunology. 161:1998;2151-2157.
    • (1998) Journal of Immunology , vol.161 , pp. 2151-2157
    • Lewis, T.A.1    Hartmann, C.B.2    McCoy, K.L.3
  • 26
    • 0028144238 scopus 로고
    • Changes in fibre-type composition and myosin heavy chain IId isoform in rat soleus muscle during recovery period after hindlimb suspension
    • Oishi Y., Yamamoto H., Miyamoto E. Changes in fibre-type composition and myosin heavy chain IId isoform in rat soleus muscle during recovery period after hindlimb suspension. European Journal of Applied Physiology. 68:1994;102-106.
    • (1994) European Journal of Applied Physiology , vol.68 , pp. 102-106
    • Oishi, Y.1    Yamamoto, H.2    Miyamoto, E.3
  • 27
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annual Review of Biochemistry. 70:2001;503-533.
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 29
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • Solomon V., Lecker S.H., Goldberg A.L. The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. The Journal of Biological Chemistry. 273:1998;25216-25222.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 33
    • 0024457063 scopus 로고
    • Protein metabolism and β-myosin heavy-chain mRNA in unweighted soleus muscle
    • Thomason D.B., Biggs R.B., Booth F.W. Protein metabolism and β-myosin heavy-chain mRNA in unweighted soleus muscle. American Journal of Physiology. 257:1989;R300-R305.
    • (1989) American Journal of Physiology , vol.257
    • Thomason, D.B.1    Biggs, R.B.2    Booth, F.W.3
  • 35
    • 0020081889 scopus 로고
    • Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle?
    • Tischler M.E., Desautels M., Goldberg A.L. Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? The Journal of Biological Chemistry. 257:1982;1613-1621.
    • (1982) The Journal of Biological Chemistry , vol.257 , pp. 1613-1621
    • Tischler, M.E.1    Desautels, M.2    Goldberg, A.L.3
  • 37
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: Structure of the rat gene and regulation upon fasting and by insulin
    • Wing S.S., Banville D. 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. American Journal of Physiology. 267:1994;E39-E48.
    • (1994) American Journal of Physiology , vol.267
    • Wing, S.S.1    Banville, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.