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Volumn 14, Issue 15, 2005, Pages 2125-2134

Erratum: Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin-proteasome pathway (Human Molecular Genetics (2005) vol. 14 (15) (2125-2134) doi:10.1093/hmg/ddi217);Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin - Proteasome pathway

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN 3; HEAT SHOCK PROTEIN; PROTEASOME; UBIQUITIN;

EID: 26444610334     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddm044     Document Type: Erratum
Times cited : (117)

References (36)
  • 3
    • 0034739841 scopus 로고    scopus 로고
    • Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IKBa/nuclear factor KB pathway perturbation in mice
    • Richard, I., Roudaut, C., Marchand, S., Baghdiguian, S., Herasse, M., Stockholm, D., Ono, Y., Suel, L., Bourg, N., Sorimachi, H. et al. (2000) Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IKBa/nuclear factor KB pathway perturbation in mice. J. Cell Biol., 151, 1-9.
    • (2000) J. Cell Biol. , vol.151 , pp. 1-9
    • Richard, I.1    Roudaut, C.2    Marchand, S.3    Baghdiguian, S.4    Herasse, M.5    Stockholm, D.6    Ono, Y.7    Suel, L.8    Bourg, N.9    Sorimachi, H.10
  • 4
    • 3242725958 scopus 로고    scopus 로고
    • Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro
    • Kramerova, I., Kudryashova, E., Tidball, J.G. and Spencer, M.J. (2004) Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro. Hum. Mol. Genet., 13, 1373-1388.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1373-1388
    • Kramerova, I.1    Kudryashova, E.2    Tidball, J.G.3    Spencer, M.J.4
  • 6
    • 0031172869 scopus 로고    scopus 로고
    • Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs
    • Kinbara, K., Sorimachi, H., Ishiura, S. and Suzuki, K. (1997) Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs. Arch. Biochem. Biophys., 342, 99-107.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 99-107
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 7
    • 13344285357 scopus 로고
    • Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence
    • Sorimachi, H., Kinbara, K., Kimura, S., Takahashi, M., Ishiura, S., Sasagawa, N., Sorimachi, N., Shimada, H., Tagawa, K., Maruyama, K. et al. (1995) Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J. Biol. Chem., 270, 31158-31162.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31158-31162
    • Sorimachi, H.1    Kinbara, K.2    Kimura, S.3    Takahashi, M.4    Ishiura, S.5    Sasagawa, N.6    Sorimachi, N.7    Shimada, H.8    Tagawa, K.9    Maruyama, K.10
  • 8
    • 0025019455 scopus 로고
    • Atrophy of the soleus muscle by hindlimb unweighting
    • Thomason, D.B. and Booth, F. W. (1990) Atrophy of the soleus muscle by hindlimb unweighting. J. Appl. Physiol., 68, 1-12.
    • (1990) J. Appl. Physiol. , vol.68 , pp. 1-12
    • Thomason, D.B.1    Booth, F.W.2
  • 9
    • 0027498075 scopus 로고
    • Distinguishing unloading-versus reloading-induced changes in rat soleus muscle
    • Krippendorf, B.B. and Riley, D.A. (1993) Distinguishing unloading-versus reloading-induced changes in rat soleus muscle. Muscle Nerve, 16, 99-108.
    • (1993) Muscle Nerve , vol.16 , pp. 99-108
    • Krippendorf, B.B.1    Riley, D.A.2
  • 10
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe, R.T. and Goldberg, A.L. (2001) What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr. Opin. Clin. Nutr. Metab. Care, 4, 183-190.
    • (2001) Curr. Opin. Clin. Nutr. Metab. Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 12
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • Solomon, V. and Goldberg, A.L. (1996) 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) J. Biol. Chem. , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 13
    • 0035164533 scopus 로고    scopus 로고
    • Muscle cachexia: Current concepts of intracellular mechanisms and molecular regulation
    • Hasselgren, P.O. and Fischer, J.E. (2001) Muscle cachexia: Current concepts of intracellular mechanisms and molecular regulation. Ann. Surg., 233, 9-17.
    • (2001) Ann. Surg. , vol.233 , pp. 9-17
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 14
    • 0037115363 scopus 로고    scopus 로고
    • Expression of a calpastatin transgene slows muscle coasting and obviates changes in myosin isoform expression during murine muscle disuse
    • Tidball, J.G. and Spencer, M.J. (2002) Expression of a calpastatin transgene slows muscle coasting and obviates changes in myosin isoform expression during murine muscle disuse. J. Physiol., 545, 819-828.
    • (2002) J. Physiol. , vol.545 , pp. 819-828
    • Tidball, J.G.1    Spencer, M.J.2
  • 16
    • 0342948832 scopus 로고    scopus 로고
    • Chronic contractile activity upregulates the proteasome system in rabbit skeletal muscle
    • Ordway, G.A., Neufer, P.D., Chin, E.R. and DeMartino, G.N. (2000) Chronic contractile activity upregulates the proteasome system in rabbit skeletal muscle. J. Appl. Physiol., 88, 1134-1141.
    • (2000) J. Appl. Physiol. , vol.88 , pp. 1134-1141
    • Ordway, G.A.1    Neufer, P.D.2    Chin, E.R.3    DeMartino, G.N.4
  • 17
    • 0038339517 scopus 로고    scopus 로고
    • Myogenic and nonmyogenic cells differentially express proteinases, Hsc/Hsp70, and BAG-1 during skeletal muscle regeneration
    • Duguez, S., Bihan, M.C., Gouttefangeas, D., Feasson, L. and Freyssenet, D. (2003) Myogenic and nonmyogenic cells differentially express proteinases, Hsc/Hsp70, and BAG-1 during skeletal muscle regeneration. Am. J. Physiol. Endocrinol. Metab., 285, E206-E215.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.285
    • Duguez, S.1    Bihan, M.C.2    Gouttefangeas, D.3    Feasson, L.4    Freyssenet, D.5
  • 18
    • 0037101928 scopus 로고    scopus 로고
    • Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle
    • Feasson, L., Stockholm, D., Freyssenet, D., Richard, I., Duguez, S., Beckmann, J.S. and Denis, C. (2002) Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle. J. Physiol., 543, 297-306.
    • (2002) J. Physiol. , vol.543 , pp. 297-306
    • Feasson, L.1    Stockholm, D.2    Freyssenet, D.3    Richard, I.4    Duguez, S.5    Beckmann, J.S.6    Denis, C.7
  • 19
    • 0041592634 scopus 로고    scopus 로고
    • Cardiomyopathic features associated with muscular dystrophy are independent of dystrophin absence in cardiovasculature
    • Hainsey, T.A., Senapati, S., Kuhn, D.E. and Rafael, J.A. (2003) Cardiomyopathic features associated with muscular dystrophy are independent of dystrophin absence in cardiovasculature. Neuromuscul. Disord., 13, 294-302.
    • (2003) Neuromuscul. Disord. , vol.13 , pp. 294-302
    • Hainsey, T.A.1    Senapati, S.2    Kuhn, D.E.3    Rafael, J.A.4
  • 20
    • 0030783172 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
    • Straub, V., Rafael, J.A., Chamberlain, J.S. and Campbell, K.P. (1997) Animal models for muscular dystrophy show different patterns of sarcolemmal disruption. J. Cell Biol., 139, 375-385.
    • (1997) J. Cell Biol. , vol.139 , pp. 375-385
    • Straub, V.1    Rafael, J.A.2    Chamberlain, J.S.3    Campbell, K.P.4
  • 21
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass, D.J. (2003) Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat. Cell Biol., 5, 87-90.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 22
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt, T.N., Drujan, D., Clarke, B.A., Panaro, F., Timofeyva, Y., Kline, W.O., Gonzalez, M., Yancopoulos, G.D. and Glass, D.J. (2004) The IGF-1/ PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell, 14 395-403.
    • (2004) Mol. Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6    Gonzalez, M.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 23
    • 2942748588 scopus 로고    scopus 로고
    • The role of ubiquitin-proteasome-dependent proteolysis in the remodelling of skeletal muscle
    • Taillandier, D., Combaret, L., Pouch, M.N., Samuels, S.E., Bechet, D. and Attaix, D. (2004) The role of ubiquitin-proteasome-dependent proteolysis in the remodelling of skeletal muscle. Proc. Nutr. Soc. 63, 357-361.
    • (2004) Proc. Nutr. Soc. , vol.63 , pp. 357-361
    • Taillandier, D.1    Combaret, L.2    Pouch, M.N.3    Samuels, S.E.4    Bechet, D.5    Attaix, D.6
  • 24
    • 0036798005 scopus 로고    scopus 로고
    • Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology
    • Spencer, M.J. and Mellgren, R.L. (2002) Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology. Hum. Mol. Genet., 11, 2645-2655.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2645-2655
    • Spencer, M.J.1    Mellgren, R.L.2
  • 25
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A.L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature, 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 26
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L. and Kopito, R.R. (1998) Aggresomes: A cellular response to misfolded proteins. J. Cell Biol., 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 27
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: Aggravating aggresomes
    • Garcia-Mata, R., Gao, Y.S. and Sztul, E. (2002) Hassles with taking out the garbage: Aggravating aggresomes. Traffic, 3, 388-396.
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 28
    • 0025988513 scopus 로고
    • Calcium-dependent and calcium-independent protease activities in skeletal muscle during sepsis
    • Bhattacharyya, J., Thompson, K. and Sayeed, M.M. (1991) Calcium-dependent and calcium-independent protease activities in skeletal muscle during sepsis. Circ. Shock, 35, 117-122.
    • (1991) Circ. Shock , vol.35 , pp. 117-122
    • Bhattacharyya, J.1    Thompson, K.2    Sayeed, M.M.3
  • 29
    • 0035287456 scopus 로고    scopus 로고
    • Dantrolene reduces serum TNFalpha and corticosterone levels and muscle calcium, calpain gene expression, and protein breakdown in septic rats
    • Fischer, D.R., Sun, X., Williams, A.B., Gang, G., Pritts, T.A., James, J.H., Molloy, M., Fischer, J.E., Paul, R.J. and Hasselgren, P.O. (2001) Dantrolene reduces serum TNFalpha and corticosterone levels and muscle calcium, calpain gene expression, and protein breakdown in septic rats. Shock, 15, 200-207.
    • (2001) Shock , vol.15 , pp. 200-207
    • Fischer, D.R.1    Sun, X.2    Williams, A.B.3    Gang, G.4    Pritts, T.A.5    James, J.H.6    Molloy, M.7    Fischer, J.E.8    Paul, R.J.9    Hasselgren, P.O.10
  • 32
    • 2942754280 scopus 로고    scopus 로고
    • Mechanotransduction and the regulation of protein synthesis in skeletal muscle
    • Hornberger, T.A. and Esser, K.A. (2004) Mechanotransduction and the regulation of protein synthesis in skeletal muscle. Proc. Nutr. Soc. 63, 331-335.
    • (2004) Proc. Nutr. Soc. , vol.63 , pp. 331-335
    • Hornberger, T.A.1    Esser, K.A.2
  • 33
    • 1342310797 scopus 로고    scopus 로고
    • Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo
    • Alzghoul, M.B., Gerrard, D., Watkins, B.A. and Hannon, K. (2004) Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo. FASEB J., 18, 221-223.
    • (2004) FASEB J. , vol.18 , pp. 221-223
    • Alzghoul, M.B.1    Gerrard, D.2    Watkins, B.A.3    Hannon, K.4
  • 34
    • 0036838249 scopus 로고    scopus 로고
    • Skeletal muscle plasticity: Cellular and molecular responses to altered physical activity paradigms
    • Baldwin, K.M. and Haddad, F. (2002) Skeletal muscle plasticity: Cellular and molecular responses to altered physical activity paradigms. Am. J. Phys. Med. Rehabil., 81, S40-851.
    • (2002) Am. J. Phys. Med. Rehabil. , vol.81
    • Baldwin, K.M.1    Haddad, F.2
  • 35
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H. and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol. Rev., 82, 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 36
    • 0036716317 scopus 로고    scopus 로고
    • Innervation-dependent phosphorylation and accumulation of alphaB-crystallin and Hsp27 as insoluble complexes in disused muscle
    • Kato, K., Ito, H., Kamei, K., Iwamoto, I. and Inaguma, Y. (2002) Innervation-dependent phosphorylation and accumulation of alphaB-crystallin and Hsp27 as insoluble complexes in disused muscle. FASEB J., 16, 1432-1434.
    • (2002) FASEB J. , vol.16 , pp. 1432-1434
    • Kato, K.1    Ito, H.2    Kamei, K.3    Iwamoto, I.4    Inaguma, Y.5


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