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Volumn 581, Issue 18, 2007, Pages 3415-3421

Regulation of various proteolytic pathways by insulin and amino acids in human fibroblasts

Author keywords

Amino acids; Human fibroblasts; Insulin; Intracellular protein degradation; Lysosomes; mTOR; Proteasomes

Indexed keywords

AMINO ACID; ARGININE; CYSTEINE; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN; METHIONINE; PHENYLALANINE; TRYPTOPHAN; TYROSINE;

EID: 34447260075     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.06.043     Document Type: Article
Times cited : (15)

References (39)
  • 3
    • 22044442015 scopus 로고    scopus 로고
    • Autophagosomes: biogenesis from scratch?
    • Reggiori F., and Klionsky D.J. Autophagosomes: biogenesis from scratch?. Curr. Opin. Cell Biol. 17 (2005) 415-422
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 415-422
    • Reggiori, F.1    Klionsky, D.J.2
  • 4
    • 33745023775 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in aging and disease
    • Massey A.C., Zhang C., and Cuervo A.M. Chaperone-mediated autophagy in aging and disease. Curr. Top. Dev. Biol. 73 (2006) 205-235
    • (2006) Curr. Top. Dev. Biol. , vol.73 , pp. 205-235
    • Massey, A.C.1    Zhang, C.2    Cuervo, A.M.3
  • 8
    • 33749052075 scopus 로고    scopus 로고
    • Signalling and autophagy regulation in health, aging and disease
    • Meijer A.J., and Codogno P. Signalling and autophagy regulation in health, aging and disease. Mol Aspects Med. 27 (2006) 411-425
    • (2006) Mol Aspects Med. , vol.27 , pp. 411-425
    • Meijer, A.J.1    Codogno, P.2
  • 9
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes
    • Tassa A., Roux M.P., Attaix D., and Bechet D.M. Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem. J. 376 (2003) 577-586
    • (2003) Biochem. J. , vol.376 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 12
    • 0037401773 scopus 로고    scopus 로고
    • Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions
    • Fuertes G., Villarroya A., and Knecht E. Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions. Int. J. Biochem. Cell Biol. 35 (2003) 651-664
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 651-664
    • Fuertes, G.1    Villarroya, A.2    Knecht, E.3
  • 13
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes G., Marti{dotless}́n de Llano J.J., Villarroya A., Rivett A.J., and Knecht E. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem. J. 375 (2003) 75-86
    • (2003) Biochem. J. , vol.375 , pp. 75-86
    • Fuertes, G.1    Martín de Llano, J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 14
    • 33646191861 scopus 로고    scopus 로고
    • A single point mutation in the low-density lipoprotein receptor switches the degradation of its mature protein from the proteasome to the lysosome
    • Marti{dotless}́n de Llano J.J., Fuertes G., Andreu E.J., Puig O., Chaves F.J., Soutar A.K., Armengod M.E., and Knecht E. A single point mutation in the low-density lipoprotein receptor switches the degradation of its mature protein from the proteasome to the lysosome. Int. J. Biochem. Cell Biol. 38 (2006) 1340-1351
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1340-1351
    • Martín de Llano, J.J.1    Fuertes, G.2    Andreu, E.J.3    Puig, O.4    Chaves, F.J.5    Soutar, A.K.6    Armengod, M.E.7    Knecht, E.8
  • 15
    • 0021175877 scopus 로고
    • Regulation of lysosomal autophagy in transformed and non-transformed mouse fibroblasts under several growth conditions
    • Knecht E., Hernández-Yago J., and Grisoli{dotless}́a S. Regulation of lysosomal autophagy in transformed and non-transformed mouse fibroblasts under several growth conditions. Exp. Cell Res. 154 (1984) 224-232
    • (1984) Exp. Cell Res. , vol.154 , pp. 224-232
    • Knecht, E.1    Hernández-Yago, J.2    Grisolía, S.3
  • 16
    • 22144433385 scopus 로고    scopus 로고
    • Differentiation stage-dependent preferred uptake of basolateral (systemic) glutamine into Caco-2 cells results in its accumulation in proteins with a role in cell-cell interaction
    • Lenaerts K., Mariman E., Bouwman F., and Renes J. Differentiation stage-dependent preferred uptake of basolateral (systemic) glutamine into Caco-2 cells results in its accumulation in proteins with a role in cell-cell interaction. FEBS J. 272 (2005) 3350-3364
    • (2005) FEBS J. , vol.272 , pp. 3350-3364
    • Lenaerts, K.1    Mariman, E.2    Bouwman, F.3    Renes, J.4
  • 17
  • 18
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation
    • Munafó D.B., and Colombo M.I. A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation. J. Cell Sci. 114 (2001) 3619-3629
    • (2001) J. Cell Sci. , vol.114 , pp. 3619-3629
    • Munafó, D.B.1    Colombo, M.I.2
  • 19
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida I., Minematsu-Ikeguchi N., Ueno T., and Kominami E. Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 1 (2005) 84-91
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 20
    • 1542289063 scopus 로고    scopus 로고
    • Amino acids and insulin control autophagic proteolysis through different signaling pathways in relation to mTOR in isolated hepatocytes
    • Kanazawa T., Taneike I., Akaishi R., Yoshizawa F., Furuya N., Fujimura S., and Kadowaki M. Amino acids and insulin control autophagic proteolysis through different signaling pathways in relation to mTOR in isolated hepatocytes. J. Biol. Chem. 279 (2004) 8452-8459
    • (2004) J. Biol. Chem. , vol.279 , pp. 8452-8459
    • Kanazawa, T.1    Taneike, I.2    Akaishi, R.3    Yoshizawa, F.4    Furuya, N.5    Fujimura, S.6    Kadowaki, M.7
  • 21
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart E.F., Luiken J.J., Blommaart P.J., van Woerkom G.M., and Meijer A.J. Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J. Biol. Chem. 270 (1995) 2320-2326
    • (1995) J. Biol. Chem. , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1    Luiken, J.J.2    Blommaart, P.J.3    van Woerkom, G.M.4    Meijer, A.J.5
  • 22
    • 33646548305 scopus 로고    scopus 로고
    • The amino acid sensitive TOR pathway from yeast to mammals
    • Dann S.G., and Thomas G. The amino acid sensitive TOR pathway from yeast to mammals. FEBS Lett. 580 (2006) 2821-2829
    • (2006) FEBS Lett. , vol.580 , pp. 2821-2829
    • Dann, S.G.1    Thomas, G.2
  • 23
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S., Davies J.E., Huang Z., Tunnacliffe A., and Rubinsztein D.C. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J. Biol. Chem. 282 (2007) 5641-5652
    • (2007) J. Biol. Chem. , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 25
    • 33646559999 scopus 로고    scopus 로고
    • Role of amino acids in insulin signaling in adipocytes and their potential to decrease insulin resistance of adipose tissue
    • Hinault C., van Obberghen E., and Mothe-Satney I. Role of amino acids in insulin signaling in adipocytes and their potential to decrease insulin resistance of adipose tissue. J. Nutr. Biochem. 17 (2006) 374-378
    • (2006) J. Nutr. Biochem. , vol.17 , pp. 374-378
    • Hinault, C.1    van Obberghen, E.2    Mothe-Satney, I.3
  • 26
    • 20344376194 scopus 로고    scopus 로고
    • The role of leucine in the regulation of protein metabolism
    • Garlick P.J. The role of leucine in the regulation of protein metabolism. J. Nutr. 135 (2005) 1553S-1556S
    • (2005) J. Nutr. , vol.135
    • Garlick, P.J.1
  • 28
    • 31544458134 scopus 로고    scopus 로고
    • Branched-chain amino acids: enzyme and substrate regulation
    • Brosnan J.T., and Brosnan M.E. Branched-chain amino acids: enzyme and substrate regulation. J. Nutr. 136 1 (2006) 207S-211S
    • (2006) J. Nutr. , vol.136 , Issue.1
    • Brosnan, J.T.1    Brosnan, M.E.2
  • 30
    • 23944474593 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Cell Death Differ. 12 (2005) 1178-1190
    • (2005) Cell Death Differ. , vol.12 , pp. 1178-1190
    • Ciechanover, A.1
  • 31
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa Jr. N.E., Odessey R., and Goldberg A.L. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J. Clin. Invest. 100 (1997) 197-203
    • (1997) J. Clin. Invest. , vol.100 , pp. 197-203
    • Tawa Jr., N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 33
    • 0043092316 scopus 로고    scopus 로고
    • Inhibition of proteasome activity by selected amino acids
    • Hamel F.G., Upward J.L., Siford G.L., and Duckworth W.C. Inhibition of proteasome activity by selected amino acids. Metabolism 52 (2003) 810-814
    • (2003) Metabolism , vol.52 , pp. 810-814
    • Hamel, F.G.1    Upward, J.L.2    Siford, G.L.3    Duckworth, W.C.4
  • 34
    • 34047212021 scopus 로고    scopus 로고
    • Amino acids and insulin act additively to regulate components of the ubiquitin-proteasome pathway in C2C12 myotubes
    • Sadiq F., Hazlerigg D.G., and Lomax M.A. Amino acids and insulin act additively to regulate components of the ubiquitin-proteasome pathway in C2C12 myotubes. BMC Mol. Biol. 8 (2007) 23
    • (2007) BMC Mol. Biol. , vol.8 , pp. 23
    • Sadiq, F.1    Hazlerigg, D.G.2    Lomax, M.A.3
  • 35
    • 0033997045 scopus 로고    scopus 로고
    • The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe
    • Niemann A., Takatsuki A., and Elsässer H.-P. The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe. J. Histochem. Cytochem. 48 (2000) 251-258
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 251-258
    • Niemann, A.1    Takatsuki, A.2    Elsässer, H.-P.3
  • 36
    • 21844440290 scopus 로고    scopus 로고
    • Ketone bodies stimulate chaperone-mediated autophagy
    • Finn P.F., and Dice J.F. Ketone bodies stimulate chaperone-mediated autophagy. J. Biol. Chem. 280 (2005) 25864-25870
    • (2005) J. Biol. Chem. , vol.280 , pp. 25864-25870
    • Finn, P.F.1    Dice, J.F.2
  • 37
    • 33748066654 scopus 로고    scopus 로고
    • Akt and mammalian target of rapamycin regulate separate systems of proteolysis in renal tubular cells
    • Shen W., Brown N.S., Finn P.F., Dice J.F., and Franch H.A. Akt and mammalian target of rapamycin regulate separate systems of proteolysis in renal tubular cells. J. Am. Soc. Nephrol. 17 (2006) 2414-2423
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 2414-2423
    • Shen, W.1    Brown, N.S.2    Finn, P.F.3    Dice, J.F.4    Franch, H.A.5
  • 38
    • 34248594926 scopus 로고    scopus 로고
    • Collaboration of proteolytic systems
    • Mizushima N. Collaboration of proteolytic systems. Autophagy 3 (2007) 179-180
    • (2007) Autophagy , vol.3 , pp. 179-180
    • Mizushima, N.1


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