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Volumn 16, Issue 13, 2002, Pages 1697-1712

Patterns of gene expression in atrophying skeletal muscles: Response to food deprivation

Author keywords

Cachexia; cDNA microarray; Proteasome; Ubiquitin

Indexed keywords

ATROGIN 1; CELL PROTEIN; COMPLEMENTARY DNA; GLUCOSE; GLUTAMATE AMMONIA LIGASE; GLYCOLYTIC ENZYME; LIGASE; MESSENGER RNA; MYOSIN BINDING PROTEIN H; PHOSPHORYLASE KINASE; POLYUBIQUITIN; PROTEASOME; PYRUVATE DEHYDROGENASE KINASE 4; SOMATOMEDIN BINDING PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0036845620     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.02-0312com     Document Type: Article
Times cited : (270)

References (98)
  • 1
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin- proteasome pathway in normal and disease states
    • Lecker, S. H., Solomon, V., Mitch, W. E., and Goldberg, A. L. (1999) Muscle protein breakdown and the critical role of the ubiquitin- proteasome pathway in normal and disease states. J. Nutr. 129, 227S-237S
    • (1999) J. Nutr. , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 2
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting: The role of the ubiquitin-proteasome pathway
    • Mitch, W. E., and Goldberg, A. L. (1996) Mechanisms of muscle wasting: The role of the ubiquitin-proteasome pathway. New Engl. J. Med. 335, 1897-1905
    • (1996) New Engl. J. Med. , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 3
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
    • Wing, S. S., and Goldberg, A. L. (1993) Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264, E668-E676
    • (1993) Am. J. Physiol. , vol.264
    • Wing, S.S.1    Goldberg, A.L.2
  • 5
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa, N. E., Odessey, R., and Goldberg, A. L. (1997) Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J. Clin. Invest. 100, 197-203
    • (1997) J. Clin. Invest. , vol.100 , pp. 197-203
    • Tawa, N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 6
    • 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
  • 7
    • 0029000181 scopus 로고
    • Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy
    • Medina, R., Wing, S. S., and Goldberg, A. L. (1995) Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem. J. 307, 631-637
    • (1995) Biochem. J. , vol.307 , pp. 631-637
    • Medina, R.1    Wing, S.S.2    Goldberg, A.L.3
  • 8
    • 0030009316 scopus 로고    scopus 로고
    • The acidosis of chronic renal failure activates muscle proteolysis in rats by augmenting transcription of genes encoding proteins of the ATP- dependent ubiquitinproteasome pathway
    • Bailey, J. L., Wang, X., England, B. K., Price, S. R., Ding, X., and Mitch, W. E. (1996) The acidosis of chronic renal failure activates muscle proteolysis in rats by augmenting transcription of genes encoding proteins of the ATP- dependent ubiquitinproteasome pathway. J. Clin. Invest. 97, 1447-1453
    • (1996) J. Clin. Invest. , vol.97 , pp. 1447-1453
    • Bailey, J.L.1    Wang, X.2    England, B.K.3    Price, S.R.4    Ding, X.5    Mitch, W.E.6
  • 9
    • 0029861468 scopus 로고    scopus 로고
    • Muscle wasting in insulinopenic rats results from activation of the ATP- dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription
    • Price, S. R., Bailey, J. L., Wang, X., Jurkovitz, C., England, B. K., Ding, X., Phillips, L. S., and Mitch, W. E. (1996) Muscle wasting in insulinopenic rats results from activation of the ATP- dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription. J. Clin. Invest. 98, 1703-1708
    • (1996) J. Clin. Invest. , vol.98 , pp. 1703-1708
    • Price, S.R.1    Bailey, J.L.2    Wang, X.3    Jurkovitz, C.4    England, B.K.5    Ding, X.6    Phillips, L.S.7    Mitch, W.E.8
  • 10
    • 0033389976 scopus 로고    scopus 로고
    • Mechanisms causing muscle proteolysis in uremia: The influence of insulin and cytokines
    • Mitch, W. E., Du, J., Bailey, J. L., and Price, S. R. (1999) Mechanisms causing muscle proteolysis in uremia: The influence of insulin and cytokines. Miner. Electrolyte Metab. 25, 216-219
    • (1999) Miner. Electrolyte Metab. , vol.25 , pp. 216-219
    • Mitch, W.E.1    Du, J.2    Bailey, J.L.3    Price, S.R.4
  • 11
    • 0011374949 scopus 로고    scopus 로고
    • Starvation
    • Cherrington, A. D., ed.: The Endocrine Pancreas and Regulation Of Metabolism, Oxford University Press, Oxford
    • Owen, O. E., Smalley, K. J., and Jungas, R. L. (2001) Starvation. In Handbook of Physiology Section 7: The Endocrine System (Cherrington, A. D., ed) Vol. II: The Endocrine Pancreas and Regulation Of Metabolism, pp. 1199-1225, Oxford University Press, Oxford
    • (2001) Handbook of Physiology Section 7: The Endocrine System , vol.2 , pp. 1199-1225
    • Owen, O.E.1    Smalley, K.J.2    Jungas, R.L.3
  • 12
    • 0018101654 scopus 로고
    • Regulation and significance of amino acid metabolism in skeletal muscle
    • Goldberg, A. L., and Chang, T. W. (1978) Regulation and significance of amino acid metabolism in skeletal muscle. Federation Proc. 37, 2301-2307
    • (1978) Federation Proc. , vol.37 , pp. 2301-2307
    • Goldberg, A.L.1    Chang, T.W.2
  • 13
    • 0022969340 scopus 로고
    • Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation
    • Lowell, B. B., Ruderman, N. B., and Goodman, M. N. (1986) Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation. Metabolism 35, 1121-1127
    • (1986) Metabolism , vol.35 , pp. 1121-1127
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 16
    • 0021742764 scopus 로고
    • Effects of starvation, diabetes and acute insulin treatment on the regulation of polypeptide-chain initiation in rat skeletal muscle
    • Harmon, C. S., Proud, C. G., and Pain, V. M. (1984) Effects of starvation, diabetes and acute insulin treatment on the regulation of polypeptide-chain initiation in rat skeletal muscle. Biochem. J. 223, 687-696
    • (1984) Biochem. J. , vol.223 , pp. 687-696
    • Harmon, C.S.1    Proud, C.G.2    Pain, V.M.3
  • 17
    • 0021314929 scopus 로고
    • Effects of food deprivation and refeeding on total protein and actomyosin degradation
    • Li, J. B., and Wassner, S. J. (1984) Effects of food deprivation and refeeding on total protein and actomyosin degradation. Am. J. Physiol. 246, E32-E37
    • (1984) Am. J. Physiol. , vol.246
    • Li, J.B.1    Wassner, S.J.2
  • 18
    • 0024989544 scopus 로고
    • Glucose utilization in heart, diaphragm and skeletal muscle during the fed-to-starved transition
    • Holness, M. J., and Sugden, M. C. (1990) Glucose utilization in heart, diaphragm and skeletal muscle during the fed-to-starved transition. Biochem. J. 270, 245-249
    • (1990) Biochem. J. , vol.270 , pp. 245-249
    • Holness, M.J.1    Sugden, M.C.2
  • 19
    • 0023519957 scopus 로고
    • Leucine, glucose, and energy metabolism after 3 days of fasting in healthy human subjects
    • Nair, K. S., Woolf, P. D., Welle, S. L., and Matthews, D. E. (1987) Leucine, glucose, and energy metabolism after 3 days of fasting in healthy human subjects. Am. J. Clin. Nutr. 46, 557-562
    • (1987) Am. J. Clin. Nutr. , vol.46 , pp. 557-562
    • Nair, K.S.1    Woolf, P.D.2    Welle, S.L.3    Matthews, D.E.4
  • 21
    • 0032792498 scopus 로고    scopus 로고
    • Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes
    • Wu, P., Inskeep, K., Bowker-Kinley, M. M., Popov, K. M., and Harris, R. A. (1999) Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes. Diabetes 48, 1593-1599
    • (1999) Diabetes , vol.48 , pp. 1593-1599
    • Wu, P.1    Inskeep, K.2    Bowker-Kinley, M.M.3    Popov, K.M.4    Harris, R.A.5
  • 22
    • 0033921984 scopus 로고    scopus 로고
    • Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle
    • Hildebrandt, A. L., and Neufer, P. D. (2000) Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle. Am. J. Physiol. 278, E1078-E1086
    • (2000) Am. J. Physiol. , vol.278
    • Hildebrandt, A.L.1    Neufer, P.D.2
  • 24
    • 0034730124 scopus 로고    scopus 로고
    • Importance of replication in microarray gene expression studies: Statistical methods and evidence from repetitive cDNA hybridizations
    • Lee, M. L., Kuo, F. C., Whitmore, G. A., and Sklar, J. (2000) Importance of replication in microarray gene expression studies: Statistical methods and evidence from repetitive cDNA hybridizations. Proc. Natl. Acad. Sci. USA 97, 9834-9839
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9834-9839
    • Lee, M.L.1    Kuo, F.C.2    Whitmore, G.A.3    Sklar, J.4
  • 25
    • 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. (1991) Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomed. Biochim. Acta 50, 347-356
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 347-356
    • Medina, R.1    Wing, S.S.2    Haas, A.3    Goldberg, A.L.4
  • 26
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., and Goldberg, A. L. (2001) Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA 98, 14440-14445
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 28
    • 0035166684 scopus 로고    scopus 로고
    • Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathway
    • Kwon, Y. T., Xia, Z., Davydov, I. V., Lecker, S. H., and Varshavsky, A. (2001) Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathway. Mol. Cell. Biol. 21, 8007-8021
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8007-8021
    • Kwon, Y.T.1    Xia, Z.2    Davydov, I.V.3    Lecker, S.H.4    Varshavsky, A.5
  • 29
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • Lecker, S. H., Solomon, V., Price, S. R., Kwon, Y. T., Mitch, W. E., and Goldberg, A. L. (1999) Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J. Clin. Invest. 104, 1411-1420
    • (1999) J. Clin. Invest. , vol.104 , pp. 1411-1420
    • Lecker, S.H.1    Solomon, V.2    Price, S.R.3    Kwon, Y.T.4    Mitch, W.E.5    Goldberg, A.L.6
  • 30
    • 0034685026 scopus 로고    scopus 로고
    • The gene expression of ubiquitin ligase E3alpha is upregulated in skeletal muscle during sepsis in rats-potential role of glucocorticoids
    • Fischer, D., Sun, X., Gang, G., Pritts, T., and Hasselgren, P. O. (2000) The gene expression of ubiquitin ligase E3alpha is upregulated in skeletal muscle during sepsis in rats-potential role of glucocorticoids. Biochem. Biophys. Res. Commun. 267, 504-508
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 504-508
    • Fischer, D.1    Sun, X.2    Gang, G.3    Pritts, T.4    Hasselgren, P.O.5
  • 31
    • 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., and Goldberg, A. L. (1998) The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J. Biol. Chem. 273, 25216-25222
    • (1998) J. Biol. Chem. , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 32
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: Structure of the rat gene and regulation upon fasting and by insulin
    • Wing, S. S., and Banville, D. (1994) 14-kDa ubiquitin-conjugating enzyme: Structure of the rat gene and regulation upon fasting and by insulin. Am. J. Physiol. 267, E39-E48
    • (1994) Am. J. Physiol. , vol.267
    • Wing, S.S.1    Banville, D.2
  • 33
    • 0023065242 scopus 로고
    • Intracellular protein catabolism and its control during nutrient deprivation and supply
    • Mortimore, G. E., and Poso, A. R. (1987) Intracellular protein catabolism and its control during nutrient deprivation and supply. Annu. Rev. Nutr. 7, 539-564
    • (1987) Annu. Rev. Nutr. , vol.7 , pp. 539-564
    • Mortimore, G.E.1    Poso, A.R.2
  • 34
    • 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., Bechet, D., Combaret, L., Attaix, D., and Ferrara, M. (2001) Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting. Biochem. J. 360, 143-150
    • (2001) Biochem. J. , vol.360 , pp. 143-150
    • Deval, C.1    Mordier, S.2    Obled, C.3    Bechet, D.4    Combaret, L.5    Attaix, D.6    Ferrara, M.7
  • 38
    • 0015466451 scopus 로고
    • Oxidation of amino acids by diaphragms from fed and fasted rats
    • Goldberg, A. L., and Odessey, R. (1972) Oxidation of amino acids by diaphragms from fed and fasted rats. Am. J. Physiol. 223, 1384-1391
    • (1972) Am. J. Physiol. , vol.223 , pp. 1384-1391
    • Goldberg, A.L.1    Odessey, R.2
  • 39
    • 0021057359 scopus 로고
    • Glutamine synthetase activity of muscle in acidosis
    • King, P. A., Goldstein, L., and Newsholme, E. A. (1983) Glutamine synthetase activity of muscle in acidosis. Biochem. J. 216, 523-525
    • (1983) Biochem. J. , vol.216 , pp. 523-525
    • King, P.A.1    Goldstein, L.2    Newsholme, E.A.3
  • 40
    • 84874586518 scopus 로고    scopus 로고
    • Regulation of glucose metabolism in skeletal muscle
    • Cherrington, A. D., ed.: The Endocrine Pancreas and Regulation of Metabolism, Oxford University Press, Oxford
    • Kruszynska, Y. T., Ciaraldi, T. P., and Henry, R. R. (2001) Regulation of glucose metabolism in skeletal muscle. In Handbook of Physiology Section 7: The Endocrine System (Cherrington, A. D., ed) Vol. II: The Endocrine Pancreas and Regulation of Metabolism, pp. 579-607, Oxford University Press, Oxford
    • (2001) Handbook of Physiology Section 7: The Endocrine System , vol.2 , pp. 579-607
    • Kruszynska, Y.T.1    Ciaraldi, T.P.2    Henry, R.R.3
  • 41
    • 0030292743 scopus 로고    scopus 로고
    • Lilly lecture 1995. Glucose transport: Pivotal step in insulin action
    • Kahn, B. B. (1996) Lilly lecture 1995. Glucose transport: Pivotal step in insulin action. Diabetes 45, 1644-1654
    • (1996) Diabetes , vol.45 , pp. 1644-1654
    • Kahn, B.B.1
  • 42
    • 0034653968 scopus 로고    scopus 로고
    • Fibre-type specific modification of the activity and regulation of skeletal muscle pyruvate dehydrogenase kinase (PDK) by prolonged starvation and refeeding is associated with targeted regulation of PDK isoenzyme 4 expression
    • Sugden, M. C., Kraus, A., Harris, R. A., and Holness, M.J. (2000) Fibre-type specific modification of the activity and regulation of skeletal muscle pyruvate dehydrogenase kinase (PDK) by prolonged starvation and refeeding is associated with targeted regulation of PDK isoenzyme 4 expression. Biochem. J. 346, 651-657
    • (2000) Biochem. J. , vol.346 , pp. 651-657
    • Sugden, M.C.1    Kraus, A.2    Harris, R.A.3    Holness, M.J.4
  • 43
    • 0034282947 scopus 로고    scopus 로고
    • Starvation increases the amount of pyruvate dehydrogenase kinase in several mammalian tissues
    • Wu, P., Blair, P. V., Sato, J., Jaskiewicz, J., Popov, K. M., and Harris, R. A. (2000) Starvation increases the amount of pyruvate dehydrogenase kinase in several mammalian tissues. Arch. Biochem. Biophys. 381, 1-7
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 1-7
    • Wu, P.1    Blair, P.V.2    Sato, J.3    Jaskiewicz, J.4    Popov, K.M.5    Harris, R.A.6
  • 44
    • 0031973056 scopus 로고    scopus 로고
    • Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart
    • Wu, P., Sato, J., Zhao, Y., Jaskiewicz, J., Popov, K. M., and Harris, R. A. (1998) Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart. Biochem. J. 329, 197-201
    • (1998) Biochem. J. , vol.329 , pp. 197-201
    • Wu, P.1    Sato, J.2    Zhao, Y.3    Jaskiewicz, J.4    Popov, K.M.5    Harris, R.A.6
  • 45
    • 0031972736 scopus 로고    scopus 로고
    • Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex
    • Bowker-Kinley, M. M., Davis, W. I., Wu, P., Harris, R. A., and Popov, K. M. (1998) Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex. Biochem. J. 329, 191-196
    • (1998) Biochem. J. , vol.329 , pp. 191-196
    • Bowker-Kinley, M.M.1    Davis, W.I.2    Wu, P.3    Harris, R.A.4    Popov, K.M.5
  • 46
    • 0033567657 scopus 로고    scopus 로고
    • Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure
    • Brushia, R.J., and Walsh, D. A. (1999) Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure. Front. Biosci. 4, D618-641
    • (1999) Front. Biosci. , vol.4
    • Brushia, R.J.1    Walsh, D.A.2
  • 47
    • 0028396932 scopus 로고
    • Differing patterns of carbohydrate metabolism in liver and muscle
    • Geddes, R., and Chow, J. C. (1994) Differing patterns of carbohydrate metabolism in liver and muscle. Carbohydr. Res. 256, 139-147
    • (1994) Carbohydr. Res. , vol.256 , pp. 139-147
    • Geddes, R.1    Chow, J.C.2
  • 48
    • 0024312124 scopus 로고
    • Rat skeletal muscle lysosomes contain glycogen
    • Calder, P. C., and Geddes, R. (1989) Rat skeletal muscle lysosomes contain glycogen. Int. J. Biochem. 21, 561-567
    • (1989) Int. J. Biochem. , vol.21 , pp. 561-567
    • Calder, P.C.1    Geddes, R.2
  • 49
    • 0025856183 scopus 로고
    • Regulation of lipoprotein lipase in adipose and muscle tissues during fasting
    • Ladu, M.J., Kapsas, H., and Palmer, W. K. (1991) Regulation of lipoprotein lipase in adipose and muscle tissues during fasting. Am. J. Physiol. 260, R953-R959
    • (1991) Am. J. Physiol. , vol.260
    • Ladu, M.J.1    Kapsas, H.2    Palmer, W.K.3
  • 50
    • 0034693232 scopus 로고    scopus 로고
    • Defective uptake and utilization of long chain fatty acids in muscle and adipose tissues of CD36 knockout mice
    • Coburn, C. T., Knapp, F. F., Jr., Febbraio, M., Beets, A. L., Silverstein, R. L., and Abumrad, N. A. (2000) Defective uptake and utilization of long chain fatty acids in muscle and adipose tissues of CD36 knockout mice. J. Biol. Chem. 275, 32523-32529
    • (2000) J. Biol. Chem. , vol.275 , pp. 32523-32529
    • Coburn, C.T.1    Knapp F.F., Jr.2    Febbraio, M.3    Beets, A.L.4    Silverstein, R.L.5    Abumrad, N.A.6
  • 51
    • 0033609919 scopus 로고    scopus 로고
    • MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonylCoA decarboxylase deficiency
    • Sacksteder, K. A., Morrell, J. C., Wanders, R. J., Matalon, R., and Gould, S. J. (1999) MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA decarboxylase and is mutated in malonylCoA decarboxylase deficiency. J. Biol. Chem. 274, 24461-24468
    • (1999) J. Biol. Chem. , vol.274 , pp. 24461-24468
    • Sacksteder, K.A.1    Morrell, J.C.2    Wanders, R.J.3    Matalon, R.4    Gould, S.J.5
  • 52
    • 0021435685 scopus 로고
    • Sites of protein conservation and loss during starvation: Influence of adiposity
    • Goodman, M. N., Lowell, B., Belur, E., and Ruderman, N. B. (1984) Sites of protein conservation and loss during starvation: Influence of adiposity. Am. J. Physiol. 246, E383-E390
    • (1984) Am. J. Physiol. , vol.246
    • Goodman, M.N.1    Lowell, B.2    Belur, E.3    Ruderman, N.B.4
  • 53
    • 0025067467 scopus 로고
    • Peroxisomes of the rat cardiac and soleus muscles increase after starvation. A biochemical and immunocytochemical study
    • Yokota, S., and Asayama, K. (1990) Peroxisomes of the rat cardiac and soleus muscles increase after starvation. A biochemical and immunocytochemical study. Histochemistry 93, 287-293
    • (1990) Histochemistry , vol.93 , pp. 287-293
    • Yokota, S.1    Asayama, K.2
  • 55
    • 0035936764 scopus 로고    scopus 로고
    • Obesity and the regulation of energy balance
    • Spiegelman, B. M., and Flier, J. S. (2001) Obesity and the regulation of energy balance. Cell 104, 531-543
    • (2001) Cell , vol.104 , pp. 531-543
    • Spiegelman, B.M.1    Flier, J.S.2
  • 56
    • 0031832185 scopus 로고    scopus 로고
    • Role of UCP homologues in skeletal muscles and brown adipose tissue: Mediators of thermogenesis or regulators of lipids as fuel substrate?
    • Samec, S., Seydoux, J., and Dulloo, A. G. (1998) Role of UCP homologues in skeletal muscles and brown adipose tissue: Mediators of thermogenesis or regulators of lipids as fuel substrate? FASEB J. 12, 715-724
    • (1998) FASEB J. , vol.12 , pp. 715-724
    • Samec, S.1    Seydoux, J.2    Dulloo, A.G.3
  • 60
    • 0034709614 scopus 로고    scopus 로고
    • Phenotypic expression of IGF binding protein transcripts in muscle, in vitro and in vivo
    • Bayol, S., Loughna, P. T., and Brownson, C. (2000) Phenotypic expression of IGF binding protein transcripts in muscle, in vitro and in vivo. Biochem. Biophys. Res. Commun. 273, 282-286
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 282-286
    • Bayol, S.1    Loughna, P.T.2    Brownson, C.3
  • 61
    • 0001757608 scopus 로고    scopus 로고
    • Insulin-like growth factor binding proteins
    • Kostoyo, J. L., ed.: Hormonal Control of Growth, Oxford University Press, New York
    • Clemmons, D. R. (1999) Insulin-like growth factor binding proteins. In Handbook of Physiology Section 7: The Endocrine System (Kostoyo, J. L., ed) Vol. V: Hormonal Control of Growth, pp. 573- 602, Oxford University Press, New York
    • (1999) Handbook of Physiology Section 7: The Endocrine System , vol.5 , pp. 573-602
    • Clemmons, D.R.1
  • 62
    • 0034881776 scopus 로고    scopus 로고
    • Influence of linker histone H1 on chromatin remodeling
    • Hill, D. A. (2001) Influence of linker histone H1 on chromatin remodeling. Biochem. Cell Biol. 79, 317-324
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 317-324
    • Hill, D.A.1
  • 63
    • 0035725036 scopus 로고    scopus 로고
    • H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions
    • Adam, M., Robert, F., Larochelle, M., and Gaudreau, L. (2001) H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions. Mol. Cell. Biol. 21, 6270-6279
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6270-6279
    • Adam, M.1    Robert, F.2    Larochelle, M.3    Gaudreau, L.4
  • 64
    • 0032705145 scopus 로고    scopus 로고
    • MEF2: A transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation
    • Naya, F. S., and Olson, E. (1999) MEF2: A transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation. Curr. Opin. Cell Biol. 11, 683-688
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 683-688
    • Naya, F.S.1    Olson, E.2
  • 65
    • 0034687741 scopus 로고    scopus 로고
    • Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5
    • McKinsey, T. A., Zhang, C. L., and Olson, E. N. (2000) Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5. Proc. Natl. Acad. Sci. USA 97, 14400-14405
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14400-14405
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 66
    • 0033597362 scopus 로고    scopus 로고
    • The CACC box and myocyte enhancer factor-2 sites within the myosin light chain 2 slow promoter cooperate in regulating nerve-specific transcription in skeletal muscle
    • Esser, K., Nelson, T., Lupa-Kimball, V., and Blough, E. (1999) The CACC box and myocyte enhancer factor-2 sites within the myosin light chain 2 slow promoter cooperate in regulating nerve-specific transcription in skeletal muscle. J. Biol. Chem. 274, 12095-12102
    • (1999) J. Biol. Chem. , vol.274 , pp. 12095-12102
    • Esser, K.1    Nelson, T.2    Lupa-Kimball, V.3    Blough, E.4
  • 67
    • 0017089167 scopus 로고
    • Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles
    • Li, J. B., and Goldberg, A. L. (1976) Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles. Am. J. Physiol. 231, 441-448
    • (1976) Am. J. Physiol. , vol.231 , pp. 441-448
    • Li, J.B.1    Goldberg, A.L.2
  • 68
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras, A. C., Raught, B., and Sonenberg, N. (2001) Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15, 807-826
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 69
    • 0034307483 scopus 로고    scopus 로고
    • Internal ribosome initiation of translation and the control of cell death
    • Holcik, M., Sonenberg, N., and Korneluk, R. G. (2000) Internal ribosome initiation of translation and the control of cell death. Trends Genet. 16, 469-473
    • (2000) Trends Genet. , vol.16 , pp. 469-473
    • Holcik, M.1    Sonenberg, N.2    Korneluk, R.G.3
  • 70
    • 0041717651 scopus 로고    scopus 로고
    • Apoptosis and atrophy in rat slow skeletal muscles in chronic heart failure
    • Libera, L. D., Zennaro, R., Sandri, M., Ambrosio, G. B., and Vescovo, G. (1999) Apoptosis and atrophy in rat slow skeletal muscles in chronic heart failure. Am. J. Physiol. 277, C982-C986
    • (1999) Am. J. Physiol. , vol.277
    • Libera, L.D.1    Zennaro, R.2    Sandri, M.3    Ambrosio, G.B.4    Vescovo, G.5
  • 75
    • 0020692628 scopus 로고
    • Inhibition of cardiac proteolysis by colchicine. Selective effects on degradation of protein subclasses
    • Crie, J. S., Ord, J. M., Wakeland, J. R., and Wildenthal, K. (1983) Inhibition of cardiac proteolysis by colchicine. Selective effects on degradation of protein subclasses. Biochem. J. 210, 63-71
    • (1983) Biochem. J. , vol.210 , pp. 63-71
    • Crie, J.S.1    Ord, J.M.2    Wakeland, J.R.3    Wildenthal, K.4
  • 76
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 78
    • 0035969898 scopus 로고    scopus 로고
    • Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example
    • Maret, W., Yetman, C. A., and Jiang, L. (2001) Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example. Chem. Biol. Interact. 130- 132, 891-901
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 891-901
    • Maret, W.1    Yetman, C.A.2    Jiang, L.3
  • 79
    • 0032804191 scopus 로고    scopus 로고
    • Induction of metallothionein by stress and its molecular mechanisms
    • Jacob, S. T., Ghoshal, K., and Sheridan, J. F. (1999) Induction of metallothionein by stress and its molecular mechanisms. Gene Exp. 7, 301-310
    • (1999) Gene Exp. , vol.7 , pp. 301-310
    • Jacob, S.T.1    Ghoshal, K.2    Sheridan, J.F.3
  • 80
    • 0030964708 scopus 로고    scopus 로고
    • A pair of adjacent glucocorticoid response elements regulate expression of two mouse metallothionein genes
    • Kelly, E. J., Sandgren, E. P., Brinster, R. L., and Palmiter, R. D. (1997) A pair of adjacent glucocorticoid response elements regulate expression of two mouse metallothionein genes. Proc. Natl. Acad. Sci. USA 94, 10045-10050
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10045-10050
    • Kelly, E.J.1    Sandgren, E.P.2    Brinster, R.L.3    Palmiter, R.D.4
  • 82
    • 12644292924 scopus 로고    scopus 로고
    • Absence of the beta subunit (cchb1) of the skeletal muscle dihydropyridine receptor alters expression of the alpha 1 subunit and eliminates excitationcontraction coupling
    • Gregg, R. G., Messing, A., Strube, C., Beurg, M., Moss, R., Behan, M., Sukhareva, M., Haynes, S., Powell, J. A., Coronado, R., and Powers, P. A. (1996) Absence of the beta subunit (cchb1) of the skeletal muscle dihydropyridine receptor alters expression of the alpha 1 subunit and eliminates excitationcontraction coupling. Proc. Natl. Acad. Sci. USA 93, 13961-13966
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13961-13966
    • Gregg, R.G.1    Messing, A.2    Strube, C.3    Beurg, M.4    Moss, R.5    Behan, M.6    Sukhareva, M.7    Haynes, S.8    Powell, J.A.9    Coronado, R.10    Powers, P.A.11
  • 85
    • 0034635476 scopus 로고    scopus 로고
    • Regulation of P311 expression by Met-hepatocyte growth factor/scatter factor and the ubiquitin/proteasome system
    • Taylor, G. A., Hudson, E., Resau, J. H., and Vande Woude, G. F. (2000) Regulation of P311 expression by Met-hepatocyte growth factor/scatter factor and the ubiquitin/proteasome system. J. Biol. Chem. 275, 4215-4219
    • (2000) J. Biol. Chem. , vol.275 , pp. 4215-4219
    • Taylor, G.A.1    Hudson, E.2    Resau, J.H.3    Vande Woude, G.F.4
  • 87
    • 0036616751 scopus 로고    scopus 로고
    • Prolonged unloading of rat soleus muscle causes distinct adaptations of the gene profile
    • Wittwer, M., Fluck, M., Hoppeler, H., Muller, S., Desplanches, D., and Billeter, R. (2002) Prolonged unloading of rat soleus muscle causes distinct adaptations of the gene profile. FASEB J. 16, 884-886
    • (2002) FASEB J. , vol.16 , pp. 884-886
    • Wittwer, M.1    Fluck, M.2    Hoppeler, H.3    Muller, S.4    Desplanches, D.5    Billeter, R.6
  • 88
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., Bartel, B., and Varshavsky, A. (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature (London) 338, 394-401
    • (1989) Nature (London) , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 90
    • 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., and Goodman, M. N. (1986) Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochem. J. 234, 237-240
    • (1986) Biochem. J. , vol.234 , pp. 237-240
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 91
    • 0027176277 scopus 로고
    • Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers
    • Takahashi, H., Ishidoh, K., Muno, D., Ohwada, A., Nukiwa, T., Kominami, E., and Kira, S. (1993) Cathepsin L activity is increased in alveolar macrophages and bronchoalveolar lavage fluid of smokers. Am. Rev. Respir. Dis. 147, 1562-1568
    • (1993) Am. Rev. Respir. Dis. , vol.147 , pp. 1562-1568
    • Takahashi, H.1    Ishidoh, K.2    Muno, D.3    Ohwada, A.4    Nukiwa, T.5    Kominami, E.6    Kira, S.7
  • 92
    • 0032797384 scopus 로고    scopus 로고
    • Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism
    • Williams, A. B., Decourten-Myers, G. M., Fischer, J. E., Luo, G., Sun, X., and Hasselgren, P. O. (1999) Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism. FASEB J. 13, 1435-1443
    • (1999) FASEB J. , vol.13 , pp. 1435-1443
    • Williams, A.B.1    Decourten-Myers, G.M.2    Fischer, J.E.3    Luo, G.4    Sun, X.5    Hasselgren, P.O.6
  • 93
    • 0031196063 scopus 로고    scopus 로고
    • Nutrition and the insulin-like growth factor system
    • Estivariz, C. F., and Ziegler, T. R. (1997) Nutrition and the insulin-like growth factor system. Endocrine 7, 65-71
    • (1997) Endocrine , vol.7 , pp. 65-71
    • Estivariz, C.F.1    Ziegler, T.R.2
  • 94
    • 0026315384 scopus 로고
    • Control of myosin heavy chain expression: Interaction of hypothyroidism and hindlimb suspension
    • Diffee, G. M., Haddad, F., Herrick, R. E., and Baldwin, K. M. (1991) Control of myosin heavy chain expression: Interaction of hypothyroidism and hindlimb suspension. Am. J. Physiol. 261, C1099-C1106
    • (1991) Am. J. Physiol. , vol.261
    • Diffee, G.M.1    Haddad, F.2    Herrick, R.E.3    Baldwin, K.M.4
  • 95
    • 0033060435 scopus 로고    scopus 로고
    • Evaluation of signals activating ubiquitinproteasome proteolysis in a model of muscle wasting
    • Mitch, W. E., Bailey, J. L., Wang, X., Jurkovitz, C., Newby, D., and Price, S. R. (1999) Evaluation of signals activating ubiquitinproteasome proteolysis in a model of muscle wasting. Am. J. Physiol. 276, C1132-C1138
    • (1999) Am. J. Physiol. , vol.276
    • Mitch, W.E.1    Bailey, J.L.2    Wang, X.3    Jurkovitz, C.4    Newby, D.5    Price, S.R.6
  • 96
    • 0028412128 scopus 로고
    • Regulation of different proteolytic pathways in skeletal muscle in fasting and diabetes mellitus
    • Kettelhut, I. C., Pepato, M. T., Migliorini, R. H., Medina, R., and Goldberg, A. L. (1994) Regulation of different proteolytic pathways in skeletal muscle in fasting and diabetes mellitus. Braz. J. Med. Biol. Res. 27, 981-993
    • (1994) Braz. J. Med. Biol. Res. , vol.27 , pp. 981-993
    • Kettelhut, I.C.1    Pepato, M.T.2    Migliorini, R.H.3    Medina, R.4    Goldberg, A.L.5
  • 98
    • 0031910695 scopus 로고    scopus 로고
    • Hormonal regulation of protein metabolism in relation to nutrition and disease
    • Garlick, P. J., McNurlan, M. A., Bark, T., Lang, C. H., and Gelato, M. C. (1998) Hormonal regulation of protein metabolism in relation to nutrition and disease. J. Nutr. 128, 356S-359S
    • (1998) J. Nutr. , vol.128
    • Garlick, P.J.1    McNurlan, M.A.2    Bark, T.3    Lang, C.H.4    Gelato, M.C.5


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