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Volumn 22, Issue 2, 1998, Pages 203-208

Sepsis: Stimulation of energy-dependent protein breakdown resulting in protein loss in skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYTOKINE; ENZYME INHIBITOR; GLUCOCORTICOID; INTERLEUKIN 1; MUSCLE PROTEIN; MYOSIN; PROTEASOME; TUMOR NECROSIS FACTOR; UBIQUITIN;

EID: 0031933789     PISSN: 03642313     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002689900370     Document Type: Review
Times cited : (51)

References (51)
  • 1
    • 0020699776 scopus 로고
    • Muscle proteolysis induced by a circulating peptide in patients with sepsis or trauma
    • Clowes, G.H.A., George, B.C., Villee, C.A., Saravis, C.A.: Muscle proteolysis induced by a circulating peptide in patients with sepsis or trauma. N. Engl. J. Med. 308:545, 1983
    • (1983) N. Engl. J. Med. , vol.308 , pp. 545
    • Clowes, G.H.A.1    George, B.C.2    Villee, C.A.3    Saravis, C.A.4
  • 2
    • 0022532652 scopus 로고
    • Protein metabolism in different types of skeletal muscle during early and late sepsis in rats
    • Hasselgren, P.O., Talamini, M., James, J.H., Fischer, J.E.: Protein metabolism in different types of skeletal muscle during early and late sepsis in rats. Arch. Surg. 121:918, 1986
    • (1986) Arch. Surg. , vol.121 , pp. 918
    • Hasselgren, P.O.1    Talamini, M.2    James, J.H.3    Fischer, J.E.4
  • 3
    • 0024386017 scopus 로고
    • Total and myofibrillar protein breakdown in different types of rat skeletal muscle: Effects of sepsis and regulation by insulin
    • Hasselgren, P.O., James, J.H., Benson, D.W., Hall-Angerås, M., Angerås, U., Hiyama, D.T., Li, S., Fischer, J.E.: Total and myofibrillar protein breakdown in different types of rat skeletal muscle: effects of sepsis and regulation by insulin. Metabolism 38:634, 1989
    • (1989) Metabolism , vol.38 , pp. 634
    • Hasselgren, P.O.1    James, J.H.2    Benson, D.W.3    Hall-Angerås, M.4    Angerås, U.5    Hiyama, D.T.6    Li, S.7    Fischer, J.E.8
  • 4
    • 0020687075 scopus 로고
    • Exchange of amino acids by muscle and liver in sepsis: Comparative studies in vivo and in vitro
    • Rosenblatt, S., Clowes, G.H.A., George, B.C., Hirsch, E., Lindberg, B.: Exchange of amino acids by muscle and liver in sepsis: comparative studies in vivo and in vitro. Arch. Surg. 118:167, 1983
    • (1983) Arch. Surg. , vol.118 , pp. 167
    • Rosenblatt, S.1    Clowes, G.H.A.2    George, B.C.3    Hirsch, E.4    Lindberg, B.5
  • 6
    • 0018898289 scopus 로고
    • Respiratory fuels and nitrogen metabolism in vivo in small intestine of fed rats
    • Windmueller, H.G., Spaeth, A.E.: Respiratory fuels and nitrogen metabolism in vivo in small intestine of fed rats. J. Biol. Chem. 255:107, 1980
    • (1980) J. Biol. Chem. , vol.255 , pp. 107
    • Windmueller, H.G.1    Spaeth, A.E.2
  • 7
    • 0025455556 scopus 로고
    • Properties of glutamine release from muscle and its importance for the immune system
    • Newsholme, E.A., Parry-Billings, M.: Properties of glutamine release from muscle and its importance for the immune system. J. Parenter. Ent. Nutr. 14:63S, 1990
    • (1990) J. Parenter. Ent. Nutr. , vol.14
    • Newsholme, E.A.1    Parry-Billings, M.2
  • 8
    • 0022552652 scopus 로고
    • Protein dynamics in skeletal muscle after trauma: Local and systemic effects
    • Downey, R.S., Monafo, W.W., Karl, I.E., Matthews, D.E., Bier, D.M.: Protein dynamics in skeletal muscle after trauma: local and systemic effects. Surgery 99:265, 1986
    • (1986) Surgery , vol.99 , pp. 265
    • Downey, R.S.1    Monafo, W.W.2    Karl, I.E.3    Matthews, D.E.4    Bier, D.M.5
  • 9
    • 0028854507 scopus 로고
    • Influence of burn injury on protein metabolism in different types of skeletal muscle and the role of glucocorticoids
    • Fang, C.H., James, J.H., Ogle, C.K., Fischer, J.E., Hasselgren, P.O.: Influence of burn injury on protein metabolism in different types of skeletal muscle and the role of glucocorticoids. J. Am. Coll. Surg. 180:33, 1995
    • (1995) J. Am. Coll. Surg. , vol.180 , pp. 33
    • Fang, C.H.1    James, J.H.2    Ogle, C.K.3    Fischer, J.E.4    Hasselgren, P.O.5
  • 10
    • 0022969340 scopus 로고
    • Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation
    • Lowell, B.B., Ruderman, N.B., Goodman, M.N.: Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation. Metabolism 35:1121, 1986
    • (1986) Metabolism , vol.35 , pp. 1121
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 11
    • 0023261107 scopus 로고
    • Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis
    • Kayati, A.C., Young, V.R., Goodman, M.N.: Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis. Am. J. Physiol. 252:E621, 1987
    • (1987) Am. J. Physiol. , vol.252
    • Kayati, A.C.1    Young, V.R.2    Goodman, M.N.3
  • 12
    • 0018200306 scopus 로고
    • N-Methylhistidine (3-methylhistidine) and muscle protein turnover: An overview
    • Young, V.R., Munro, H.N.: N-Methylhistidine (3-methylhistidine) and muscle protein turnover: an overview. Fed. Proc. 37:2291, 1978
    • (1978) Fed. Proc. , vol.37 , pp. 2291
    • Young, V.R.1    Munro, H.N.2
  • 13
    • 0020957875 scopus 로고
    • 3-Methylhistidine excretion and urinary 3-methylhistidine/creatinine ratio are poor indicators of skeletal muscle protein breakdown
    • Rennie, M.J., Millward, D.J.: 3-Methylhistidine excretion and urinary 3-methylhistidine/creatinine ratio are poor indicators of skeletal muscle protein breakdown. Clin. Sci. 65:217, 1983
    • (1983) Clin. Sci. , vol.65 , pp. 217
    • Rennie, M.J.1    Millward, D.J.2
  • 14
    • 0019459213 scopus 로고
    • Urinary excretion of 3-methylhistidine: An assessment of muscle protein catabolism in adult normal subjects and during malnutrition, sepsis, and skeletal trauma
    • Long, C.L., Birkhahn, R.H., Geiger, J.W., Betts, J.E., Schiller, W.R., Blakemore, W.S.: Urinary excretion of 3-methylhistidine: an assessment of muscle protein catabolism in adult normal subjects and during malnutrition, sepsis, and skeletal trauma. Metabolism 30:765, 1981
    • (1981) Metabolism , vol.30 , pp. 765
    • Long, C.L.1    Birkhahn, R.H.2    Geiger, J.W.3    Betts, J.E.4    Schiller, W.R.5    Blakemore, W.S.6
  • 15
    • 0021359050 scopus 로고
    • Urinary excretion of 3-methylhistidine before and after major surgical operation
    • Long, C.L., Birkhahn, R.H., Geiger, J.W., Blakemore, W.S.: Urinary excretion of 3-methylhistidine before and after major surgical operation. Metabolism 33:250, 1984
    • (1984) Metabolism , vol.33 , pp. 250
    • Long, C.L.1    Birkhahn, R.H.2    Geiger, J.W.3    Blakemore, W.S.4
  • 16
    • 0025284616 scopus 로고
    • The biological characteristics of cytokines and their implication in surgical injury
    • Fong, Y., Moldawer, L.L., Shires, T., Lowry, S.F.: The biological characteristics of cytokines and their implication in surgical injury. Surg. Gynecol. Obstet. 170:363, 1990
    • (1990) Surg. Gynecol. Obstet. , vol.170 , pp. 363
    • Fong, Y.1    Moldawer, L.L.2    Shires, T.3    Lowry, S.F.4
  • 17
    • 0025836449 scopus 로고
    • The effect of interleukin-1α and the glucocorticoid receptor blocker RU38486 on total and myofibrillar protein breakdown in skeletal muscle
    • Zamir, O., Hasseigren, P.O., von Allmen D., Fischer, J.E.: The effect of interleukin-1α and the glucocorticoid receptor blocker RU38486 on total and myofibrillar protein breakdown in skeletal muscle. J. Surg. Res. 50:579, 1991
    • (1991) J. Surg. Res. , vol.50 , pp. 579
    • Zamir, O.1    Hasseigren, P.O.2    Von Allmen, D.3    Fischer, J.E.4
  • 18
    • 0026793224 scopus 로고
    • Muscle protein breakdown during endotoxemia in rats and after treatment with interleukin-1 receptor antagonist (IL-1ra)
    • Zamir, O., Hasselgren, P.O., O'Brien, W., Thompson, R.C., Fischer, J.E.: Muscle protein breakdown during endotoxemia in rats and after treatment with interleukin-1 receptor antagonist (IL-1ra). Ann. Surg. 216:381, 1992
    • (1992) Ann. Surg. , vol.216 , pp. 381
    • Zamir, O.1    Hasselgren, P.O.2    O'Brien, W.3    Thompson, R.C.4    Fischer, J.E.5
  • 19
    • 0028180058 scopus 로고
    • Reduced muscle protein breakdown in septic rats following treatment with interleukin-1 receptor antagonist
    • Zamir, O., O'Brien, W., Thompson, R.C., Bloedow, D.C., Fischer, J.E., Hasselgren, P.O.: Reduced muscle protein breakdown in septic rats following treatment with interleukin-1 receptor antagonist. Int. J. Biochem. 26:943, 1994
    • (1994) Int. J. Biochem. , vol.26 , pp. 943
    • Zamir, O.1    O'Brien, W.2    Thompson, R.C.3    Bloedow, D.C.4    Fischer, J.E.5    Hasselgren, P.O.6
  • 20
    • 0026557647 scopus 로고
    • Evidence that tumor necrosis factor participates in the regulation of muscle proteolysis during sepsis
    • Zamir, O., Hasselgren, P.O., Kunkel, S.L., Frederick, J., Higashiguchi, T., Fischer, J.E.: Evidence that tumor necrosis factor participates in the regulation of muscle proteolysis during sepsis. Arch. Surg. 127: 170, 1992
    • (1992) Arch. Surg. , vol.127 , pp. 170
    • Zamir, O.1    Hasselgren, P.O.2    Kunkel, S.L.3    Frederick, J.4    Higashiguchi, T.5    Fischer, J.E.6
  • 21
    • 0023620504 scopus 로고
    • Interleukin-1 and tumor necrosis factor do not regulate protein balance in skeletal muscle
    • Moldawer, L.L., Svanoinger, G., Gelin, J., Lundholm, K.: Interleukin-1 and tumor necrosis factor do not regulate protein balance in skeletal muscle. Am. J. Physiol. 253:C766, 1987
    • (1987) Am. J. Physiol. , vol.253
    • Moldawer, L.L.1    Svanoinger, G.2    Gelin, J.3    Lundholm, K.4
  • 22
    • 0023947951 scopus 로고
    • 2 production in rat skeletal muscle in fever is signalled by a macrophage product distinct from interleukin-1 or other known monokines
    • 2 production in rat skeletal muscle in fever is signalled by a macrophage product distinct from interleukin-1 or other known monokines. J. Clin. Invest. 81:1378, 1988
    • (1988) J. Clin. Invest. , vol.81 , pp. 1378
    • Goldberg, A.L.1    Kettelhut, J.C.2    Furano, K.3    Fagan, J.M.4    Baracos, V.5
  • 24
    • 0028201322 scopus 로고
    • Interleukin-6 induces skeletal muscle protein breakdown in rats
    • Goodman, M.N.: Interleukin-6 induces skeletal muscle protein breakdown in rats. Proc. Soc. Exp. Biol. Med. 205:182, 1994
    • (1994) Proc. Soc. Exp. Biol. Med. , vol.205 , pp. 182
    • Goodman, M.N.1
  • 25
    • 0028789750 scopus 로고
    • Interleukin-6 induces proteolysis by activating intracellular proteases (cathepsins B and L, proteasome) in C2C12 myotubes
    • Ebisui, C., Tsujinaka, T., Morimoto, T., Kan, K., Iijima, S., Yano, M., Kominami, E., Tanaka, K., Monden, M.: Interleukin-6 induces proteolysis by activating intracellular proteases (cathepsins B and L, proteasome) in C2C12 myotubes. Clin. Sci. 89:431, 1995
    • (1995) Clin. Sci. , vol.89 , pp. 431
    • Ebisui, C.1    Tsujinaka, T.2    Morimoto, T.3    Kan, K.4    Iijima, S.5    Yano, M.6    Kominami, E.7    Tanaka, K.8    Monden, M.9
  • 27
    • 0028009670 scopus 로고
    • Interleukin-6 does not activate protein breakdown in rat skeletal muscle
    • Garcia-Martinez, C., Lopez-Soriano, F.J., Argiles, J.M. Interleukin-6 does not activate protein breakdown in rat skeletal muscle. Cancer Lett. 76:1, 1994
    • (1994) Cancer Lett. , vol.76 , pp. 1
    • Garcia-Martinez, C.1    Lopez-Soriano, F.J.2    Argiles, J.M.3
  • 28
    • 0025190892 scopus 로고
    • Interleukin-6 and the acute phase response
    • Heinrich, P.C., Castell, J.V., Anders, T.: Interleukin-6 and the acute phase response. Biochem. J. 265:621, 1990
    • (1990) Biochem. J. , vol.265 , pp. 621
    • Heinrich, P.C.1    Castell, J.V.2    Anders, T.3
  • 29
    • 0031032016 scopus 로고    scopus 로고
    • Treatment of endotoxemic mice with anti-IL-6 antibody paradoxically increases IL-6 levels and stimulates mucosal protein synthesis
    • Wang, Q., Fischer, J.E., Hasselgren, P.O.: Treatment of endotoxemic mice with anti-IL-6 antibody paradoxically increases IL-6 levels and stimulates mucosal protein synthesis. Arch. Surg. 132:82, 1997
    • (1997) Arch. Surg. , vol.132 , pp. 82
    • Wang, Q.1    Fischer, J.E.2    Hasselgren, P.O.3
  • 31
    • 0000863905 scopus 로고
    • Tumor necrosis factor (TNF) and interleukin-1 (IL-1) induce muscle proteolysis through different mechanisms
    • Zamir, O., Hasselgren, P.O., Higashiguchi, T., Frederick, J., Fischer, J.E.: Tumor necrosis factor (TNF) and interleukin-1 (IL-1) induce muscle proteolysis through different mechanisms. Mediat. Inflamm. 1:247, 1992
    • (1992) Mediat. Inflamm. , vol.1 , pp. 247
    • Zamir, O.1    Hasselgren, P.O.2    Higashiguchi, T.3    Frederick, J.4    Fischer, J.E.5
  • 32
    • 0023814696 scopus 로고
    • Physiological hypercortisolemia increases proteolysis, glutamine and alanine production
    • Darmann, D., Matthews, D.E., Bier, D.M.: Physiological hypercortisolemia increases proteolysis, glutamine and alanine production. Am. J. Physiol. 255:E366, 1988
    • (1988) Am. J. Physiol. , vol.255
    • Darmann, D.1    Matthews, D.E.2    Bier, D.M.3
  • 33
    • 0025761863 scopus 로고
    • Effect of the glucocorticoid receptor antagonist RU38486 on muscle protein breakdown in sepsis
    • Hall-Angerås, M., Angerås, U., Zamir, O., Hasselgren, P.O., Fischer, J.E.: Effect of the glucocorticoid receptor antagonist RU38486 on muscle protein breakdown in sepsis. Surgery 109:468, 1991
    • (1991) Surgery , vol.109 , pp. 468
    • Hall-Angerås, M.1    Angerås, U.2    Zamir, O.3    Hasselgren, P.O.4    Fischer, J.E.5
  • 35
    • 0025293425 scopus 로고
    • Corticosterone alone does not explain increased muscle proteolysis in septic rats
    • Hall-Angerås, M., Angerås, U., Hasselgren, P.O., Fischer, J.E.: Corticosterone alone does not explain increased muscle proteolysis in septic rats. J. Surg. Res. 48:368, 1990
    • (1990) J. Surg. Res. , vol.48 , pp. 368
    • Hall-Angerås, M.1    Angerås, U.2    Hasselgren, P.O.3    Fischer, J.E.4
  • 36
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg, A.L.: The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur. J. Biochem. 203:9, 1992
    • (1992) Eur. J. Biochem. , vol.203 , pp. 9
    • Goldberg, A.L.1
  • 39
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A., Ciechanover, A.: The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61:761, 1992
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761
    • Hershko, A.1    Ciechanover, A.2
  • 40
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M.: Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7:215, 1995
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215
    • Hochstrasser, M.1
  • 41
    • 0030897196 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: Review of a novel intracellular mechanism of muscle protein breakdown during sepsis and other catabolic conditions
    • Hasselgren, P.O., Fischer, J.E.: The ubiquitin-proteasome pathway: review of a novel intracellular mechanism of muscle protein breakdown during sepsis and other catabolic conditions. Ann. Surg. 225: 307, 1997
    • (1997) Ann. Surg. , vol.225 , pp. 307
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 42
    • 0029007115 scopus 로고
    • From the cradle to the grave: Ring complexes in the life of a protein
    • Weissman, J.S., Sigler, P.B., Horwich, A.L.: From the cradle to the grave: ring complexes in the life of a protein. Science 268:523, 1995
    • (1995) Science , vol.268 , pp. 523
    • Weissman, J.S.1    Sigler, P.B.2    Horwich, A.L.3
  • 43
    • 0029028065 scopus 로고
    • A new twist to the cell cycle
    • Barinaga, M.: A new twist to the cell cycle. Science 269:631, 1995
    • (1995) Science , vol.269 , pp. 631
    • Barinaga, M.1
  • 44
    • 0026524392 scopus 로고
    • A molecular model of MHC class-I-restricted antigen processing
    • Monaco, J.: A molecular model of MHC class-I-restricted antigen processing. Immunol. Today 13:173, 1992
    • (1992) Immunol. Today , vol.13 , pp. 173
    • Monaco, J.1
  • 45
    • 0028972845 scopus 로고
    • Mechanistic aspects of NFκB regulation: The emerging role of phosphorylation and proteolysis
    • Finco, T.S., Baldwin, A.S.: Mechanistic aspects of NFκB regulation: the emerging role of phosphorylation and proteolysis. Immunity 3:263, 1995
    • (1995) Immunity , vol.3 , pp. 263
    • Finco, T.S.1    Baldwin, A.S.2
  • 46
    • 0028212481 scopus 로고
    • Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes
    • Mitch, W.E., Medina, R., Grieber, S., May, R.C., England, B.K., Price, S.R., Bailey, J.L., Goldberg, A.L.: Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes. J. Clin. Invest. 93:2127, 1994
    • (1994) J. Clin. Invest. , vol.93 , pp. 2127
    • Mitch, W.E.1    Medina, R.2    Grieber, S.3    May, R.C.4    England, B.K.5    Price, S.R.6    Bailey, J.L.7    Goldberg, A.L.8
  • 47
    • 0028817382 scopus 로고
    • Burn injury stimulates multiple proteolytic pathways in skeletal muscle including the ubiquitin-energy-dependent pathway
    • Fang, C.H., Tiao, G., James, J.H., Ogle, C., Fischer, J.E., Hasselgren, P.O.: Burn injury stimulates multiple proteolytic pathways in skeletal muscle including the ubiquitin-energy-dependent pathway. J. Am. Coll. Surg. 180:161, 1995
    • (1995) J. Am. Coll. Surg. , vol.180 , pp. 161
    • Fang, C.H.1    Tiao, G.2    James, J.H.3    Ogle, C.4    Fischer, J.E.5    Hasselgren, P.O.6
  • 49
    • 0041173139 scopus 로고
    • Sepsis increases proteasome-dependent proteolysis and mRNA levels for the proteasome subunit RC3 in skeletal muscle
    • Tiao, G.M., Fagan, J., Lieberman, M., Fischer, J.E., Hasselgren, P.O.: Sepsis increases proteasome-dependent proteolysis and mRNA levels for the proteasome subunit RC3 in skeletal muscle. Surg. Forum 46:10, 1995
    • (1995) Surg. Forum , vol.46 , pp. 10
    • Tiao, G.M.1    Fagan, J.2    Lieberman, M.3    Fischer, J.E.4    Hasselgren, P.O.5
  • 50
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K.L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Huang, D., Goldberg, A.L.: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761, 1994
    • (1994) Cell , vol.78 , pp. 761
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Huang, D.7    Goldberg, A.L.8
  • 51
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., Schreiber, S.L.: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726, 1995
    • (1995) Science , vol.268 , pp. 726
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6


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