메뉴 건너뛰기




Volumn 35, Issue 5, 2003, Pages 676-684

Down-regulation of genes in the lysosomal and ubiquitin-proteasome proteolytic pathways in calpain-3-deficient muscle

Author keywords

Calpain 3; Cathepsins; Protein breakdown; Skeletal muscle; Ubiquitin proteasome system

Indexed keywords

CALPAIN 3; CATHEPSIN B; CATHEPSIN L; MESSENGER RNA; PROTEASOME; UBIQUITIN;

EID: 0037401984     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(02)00357-6     Document Type: Article
Times cited : (23)

References (41)
  • 2
    • 77956783904 scopus 로고    scopus 로고
    • 2+-dependent systems
    • E. E. Bittar & A. J. Rivett (Eds.). Greenwich, CT: JAI Press Inc.
    • 2+-dependent systems. In E. E. Bittar & A. J. Rivett (Eds.), Intracellular protein degradation (pp. 235-266). Greenwich, CT: JAI Press Inc.
    • (1998) Intracellular protein degradation , pp. 235-266
    • Attaix, D.1    Taillandier, D.2
  • 4
    • 0034937370 scopus 로고    scopus 로고
    • Pathophysiology of limb girdle muscular dystrophy type 2A: Hypothesis and new insights into the IκBα/NFκB survival pathway in skeletal muscle
    • Baghdiguian S., Richard I., Martin M., Coopman P., Beckmann J.S., Mangeat P., Lefranc G. Pathophysiology of limb girdle muscular dystrophy type 2A: hypothesis and new insights into the IκBα/NFκB survival pathway in skeletal muscle. Journal of Molecular Medicine. 79:2001;254-261.
    • (2001) Journal of Molecular Medicine , vol.79 , pp. 254-261
    • Baghdiguian, S.1    Richard, I.2    Martin, M.3    Coopman, P.4    Beckmann, J.S.5    Mangeat, P.6    Lefranc, G.7
  • 5
    • 0029040739 scopus 로고
    • Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma
    • Baracos V.E., DeVivo C., Hoyle D.H.R., Goldberg A.L. Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma. American Journal of Physiology. 268:1995;E996-1006.
    • (1995) American Journal of Physiology , vol.268 , pp. 996-1006
    • Baracos, V.E.1    DeVivo, C.2    Hoyle, D.H.R.3    Goldberg, A.L.4
  • 6
    • 0025915530 scopus 로고
    • Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B
    • Béchet D.M., Ferrara M.J., Mordier S.B., Roux M.P., Deval C.D., Obled A. Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B. Journal of Biological Chemistry. 266:1991;14104-14112.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 14104-14112
    • Béchet, D.M.1    Ferrara, M.J.2    Mordier, S.B.3    Roux, M.P.4    Deval, C.D.5    Obled, A.6
  • 8
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell. 80:1995;675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 9
    • 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
  • 11
    • 0030590441 scopus 로고    scopus 로고
    • No alteration in gene expression of components of the ubiquitin-proteasome proteolytic pathway in dystrophin-deficient muscles
    • Combaret L., Taillandier D., Voisin L., Samuels S.E., Boespflug-Tanguy O., Attaix D. No alteration in gene expression of components of the ubiquitin-proteasome proteolytic pathway in dystrophin-deficient muscles. FEBS Letters. 393:1996;292-296.
    • (1996) FEBS Letters , vol.393 , pp. 292-296
    • Combaret, L.1    Taillandier, D.2    Voisin, L.3    Samuels, S.E.4    Boespflug-Tanguy, O.5    Attaix, D.6
  • 12
    • 0037081769 scopus 로고    scopus 로고
    • Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats
    • Combaret L., Tilignac T., Claustre A., Voisin L., Taillandier D., Obled C., Tanaka K., Attaix D. Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats. Biochemical Journal. 361:2002;185-192.
    • (2002) Biochemical Journal , vol.361 , pp. 185-192
    • Combaret, L.1    Tilignac, T.2    Claustre, A.3    Voisin, L.4    Taillandier, D.5    Obled, C.6    Tanaka, K.7    Attaix, D.8
  • 13
    • 0035890654 scopus 로고    scopus 로고
    • Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting
    • Deval C., Mordier S., Obled C., Béchet D., Combaret L., Attaix D., Ferrara M. Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting. Biochemical Journal. 360:2001;143-150.
    • (2001) Biochemical Journal , vol.360 , pp. 143-150
    • Deval, C.1    Mordier, S.2    Obled, C.3    Béchet, D.4    Combaret, L.5    Attaix, D.6    Ferrara, M.7
  • 14
    • 0030481058 scopus 로고    scopus 로고
    • Chromosome 15-linked limb-girdle muscular dystrophy: Clinical phenotypes in Reunion Island and French metropolitan communities
    • Fardeau M., Eymard B., Mignard C., Tome F.M., Richard I., Beckmann J.S. Chromosome 15-linked limb-girdle muscular dystrophy: clinical phenotypes in Reunion Island and French metropolitan communities. Neuromuscular Disorders. 6:1996;447-453.
    • (1996) Neuromuscular Disorders , vol.6 , pp. 447-453
    • Fardeau, M.1    Eymard, B.2    Mignard, C.3    Tome, F.M.4    Richard, I.5    Beckmann, J.S.6
  • 18
    • 0036845620 scopus 로고    scopus 로고
    • Patterns of gene expression in atrophying skeletal muscles: Response to food deprivation
    • Jagoe R.T., Lecker S.H., Gomes M., Goldberg A.L. Patterns of gene expression in atrophying skeletal muscles: response to food deprivation. FASEB Journal. 16:2002;1697-1712.
    • (2002) FASEB Journal , vol.16 , pp. 1697-1712
    • Jagoe, R.T.1    Lecker, S.H.2    Gomes, M.3    Goldberg, A.L.4
  • 20
    • 0021687268 scopus 로고
    • Increases in cathepsins B and L and thiol proteinase inhibitor in muscle of dystrophic hamsters. Their localization in invading phagocytes
    • Kominami E., Bando Y., Ii K., Hizawa K., Katunuma N. Increases in cathepsins B and L and thiol proteinase inhibitor in muscle of dystrophic hamsters. Their localization in invading phagocytes. Journal of Biochemistry. 96:1984;1841-1848.
    • (1984) Journal of Biochemistry , vol.96 , pp. 1841-1848
    • Kominami, E.1    Bando, Y.2    Ii, K.3    Hizawa, K.4    Katunuma, N.5
  • 21
  • 22
    • 0022479243 scopus 로고
    • Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle
    • Lowell B.B., Ruderman N.B., Goodman M.N. Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochemical Journal. 234:1986;237-240.
    • (1986) Biochemical Journal , vol.234 , pp. 237-240
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 25
    • 0030330801 scopus 로고    scopus 로고
    • Lysosomal metabolism of proteins
    • Mason R.W. Lysosomal metabolism of proteins. Subcellular Biochemistry. 27:1996;159-190.
    • (1996) Subcellular Biochemistry , vol.27 , pp. 159-190
    • Mason, R.W.1
  • 26
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart C.M. Targeting of substrates to the 26S proteasome. FASEB Journal. 11:1997;1055-1066.
    • (1997) FASEB Journal , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 29
    • 0023219132 scopus 로고
    • Calcium-activated neutral protease and its endogenous inhibitor in tissues of dystrophic and normal mice
    • Rabbani N., Moses L., Anandaraj M.P. Calcium-activated neutral protease and its endogenous inhibitor in tissues of dystrophic and normal mice. Biochemical Medicine and Metabolic Biology. 37:1987;282-286.
    • (1987) Biochemical Medicine and Metabolic Biology , vol.37 , pp. 282-286
    • Rabbani, N.1    Moses, L.2    Anandaraj, M.P.3
  • 32
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium dependent protease distinct from both m- and μ-types. Specific expression of the mRNA in skeletal muscle
    • Sorimachi H., Imajoh-Ohmi S., Emori Y., Kawasaki H., Ohno S., Minami Y., Suzuki K. Molecular cloning of a novel mammalian calcium dependent protease distinct from both m- and μ-types. Specific expression of the mRNA in skeletal muscle. Journal of Biological Chemistry. 264:1989;20106-20111.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5    Minami, Y.6    Suzuki, K.7
  • 33
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., Suzuki K. Structure and physiological function of calpains. Biochemical Journal. 328:1997;721-732.
    • (1997) Biochemical Journal , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 37
    • 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? Journal of Biological Chemistry. 257:1982;1613-1621.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 1613-1621
    • Tischler, M.E.1    Desautels, M.2    Goldberg, A.L.3
  • 38
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein mcb1 is a component of the 26S proteasome in saccharomyces cerevisiae and plays a nonessential, substrate specific role in protein turnover
    • Van Nocker S., Sadis S.Q., Rubin D.M., Glickman M., Fu H.Y., Coux O., Wefes I., Finley D., Vierstra R.D. The multiubiquitin-chain-binding protein mcb1 is a component of the 26S proteasome in saccharomyces cerevisiae and plays a nonessential, substrate specific role in protein turnover. Molecular and Cellular Biology. 16:1996;6020-6028.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.Q.2    Rubin, D.M.3    Glickman, M.4    Fu, H.Y.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 41
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
    • Wing S.S., Goldberg A.L. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. American Journal of Physiology. 264:1993;E668-E676.
    • (1993) American Journal of Physiology , vol.264
    • Wing, S.S.1    Goldberg, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.