메뉴 건너뛰기




Volumn 8, Issue 1, 2009, Pages 104-112

Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC

Author keywords

Dynamic silac; Mass spectrometry; Protein turnover

Indexed keywords

AMINO ACID; ISOTOPE; PROTEOME; PROTEIN;

EID: 60849097304     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr800641v     Document Type: Article
Times cited : (257)

References (56)
  • 1
    • 33745539414 scopus 로고    scopus 로고
    • Doherty, M. K.; Beynon, R. J. Protein turnover on the scale of the proteome. Expert Rev. Proteomics 2006, 3 (1), 97-110.
    • Doherty, M. K.; Beynon, R. J. Protein turnover on the scale of the proteome. Expert Rev. Proteomics 2006, 3 (1), 97-110.
  • 2
    • 61849108453 scopus 로고
    • Protein turnover in mammaliar cell cultures
    • Eagle, H.; Piez, K. A.; Fleischman, R.; Oyama, V. I. Protein turnover in mammaliar cell cultures. J. Biol. Chem. 1959, 234 (3), 592-7.
    • (1959) J. Biol. Chem , vol.234 , Issue.3 , pp. 592-597
    • Eagle, H.1    Piez, K.A.2    Fleischman, R.3    Oyama, V.I.4
  • 3
    • 33745093214 scopus 로고    scopus 로고
    • Protein turnover
    • Ohsumi, Y. Protein turnover. IUBMB Life 2006, 58 (5-6), 363-9.
    • (2006) IUBMB Life , vol.58 , Issue.5-6 , pp. 363-369
    • Ohsumi, Y.1
  • 4
    • 0014874868 scopus 로고
    • Protein turnover in skeletal muscle. I. The measurement of rates of synthesis and catabolism of skeletal muscle protein using (14C)Na2C03 to label protein
    • Millward, D. J. Protein turnover in skeletal muscle. I. The measurement of rates of synthesis and catabolism of skeletal muscle protein using (14C)Na2C03 to label protein. Clin. Sci. 1970, 39 (5), 577-90.
    • (1970) Clin. Sci , vol.39 , Issue.5 , pp. 577-590
    • Millward, D.J.1
  • 5
    • 0015081684 scopus 로고
    • A simple method for measuring protein turnover in the liver: The effects of starvation and low protein feeding on liver protein metabolism in the rat
    • Millward, D. J. A simple method for measuring protein turnover in the liver: the effects of starvation and low protein feeding on liver protein metabolism in the rat. Gut 1971, 12 (6), 495.
    • (1971) Gut , vol.12 , Issue.6 , pp. 495
    • Millward, D.J.1
  • 6
    • 0015389777 scopus 로고
    • An appraisal of techniques for the determination of protein turnover in vivo
    • 1P
    • Garlick, P. J.; Millward, D. J. An appraisal of techniques for the determination of protein turnover in vivo. Biochem. J. 1972, 129 (2), 1P.
    • (1972) Biochem. J , vol.129 , Issue.2
    • Garlick, P.J.1    Millward, D.J.2
  • 7
    • 0029131988 scopus 로고
    • Whole-body protein turnover in humans-past, present, and future
    • Waterlow, J. C. Whole-body protein turnover in humans-past, present, and future. Annu. Rev. Nutr. 1995, 15, 57-92.
    • (1995) Annu. Rev. Nutr , vol.15 , pp. 57-92
    • Waterlow, J.C.1
  • 8
    • 4444256211 scopus 로고    scopus 로고
    • Differential increases in syntheses of newly identified trypsinogen 2 isoforms by dietary protein in rat pancreas
    • Hara, H.; Shiota, H. Differential increases in syntheses of newly identified trypsinogen 2 isoforms by dietary protein in rat pancreas. Exp. Biol. Med. 2004, 229 (8), 772-80.
    • (2004) Exp. Biol. Med , vol.229 , Issue.8 , pp. 772-780
    • Hara, H.1    Shiota, H.2
  • 9
    • 2942559000 scopus 로고    scopus 로고
    • Proteomic analysis of adipocyte differentiation: Evidence that alpha2 macroglobulin is involved in the adipose conversion of 3T3 LI preadipocytes
    • Choi, K. L.; Wang, Y.; Tse, C. A.; Lam, K. S.; Cooper, G. J.; Xu, A. Proteomic analysis of adipocyte differentiation: Evidence that alpha2 macroglobulin is involved in the adipose conversion of 3T3 LI preadipocytes. Proteomics 2004, 4 (6), 1840-8.
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1840-1848
    • Choi, K.L.1    Wang, Y.2    Tse, C.A.3    Lam, K.S.4    Cooper, G.J.5    Xu, A.6
  • 10
    • 6344270259 scopus 로고    scopus 로고
    • Proteomic analysis of articular cartilage shows increased type II collagen synthesis in osteoarthritis and expression of inhibin betaA (activin A), a regulatory molecule for chondrocytes
    • Hermansson, M.; Sawaji, Y.; Bolton, M.; Alexander, S.; Wallace, A.; Begum, S.; Wait, R.; Saklatvala, J. Proteomic analysis of articular cartilage shows increased type II collagen synthesis in osteoarthritis and expression of inhibin betaA (activin A), a regulatory molecule for chondrocytes. J. Biol. Chem. 2004, 279 (42), 43514-21.
    • (2004) J. Biol. Chem , vol.279 , Issue.42 , pp. 43514-43521
    • Hermansson, M.1    Sawaji, Y.2    Bolton, M.3    Alexander, S.4    Wallace, A.5    Begum, S.6    Wait, R.7    Saklatvala, J.8
  • 11
    • 17444392446 scopus 로고    scopus 로고
    • Reevaluation of amino acid stimulation of protein synthesis in murine- and human-derived skeletal muscle cells assessed by independent techniques
    • Iresjo, B. M.; Svanberg, E.; Lundholm, K. Reevaluation of amino acid stimulation of protein synthesis in murine- and human-derived skeletal muscle cells assessed by independent techniques. Am. I. Physiol. Endocrinol. Metab. 2005, 288 (5), E1028-37.
    • (2005) Am. I. Physiol. Endocrinol. Metab , vol.288 , Issue.5
    • Iresjo, B.M.1    Svanberg, E.2    Lundholm, K.3
  • 13
    • 0347361590 scopus 로고    scopus 로고
    • Synthesis/degradation ratio mass spectrometry for measuring relative dynamic protein turnover
    • Cargile, B. J.; Bundy, J. L.; Grunden, A. M.; Stephenson, J. L., Jr. Synthesis/degradation ratio mass spectrometry for measuring relative dynamic protein turnover. Anal. Chem. 2004, 76 (1), 86-97.
    • (2004) Anal. Chem , vol.76 , Issue.1 , pp. 86-97
    • Cargile, B.J.1    Bundy, J.L.2    Grunden, A.M.3    Stephenson Jr., J.L.4
  • 14
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • Doherty, M. K.; Whitehead, C; McCormack, H.; Gaskell, S. J.; Beynon, R. J. Proteome dynamics in complex organisms: using stable isotopes to monitor individual protein turnover rates. Proteomics 2005, 5 (2), 522-33.
    • (2005) Proteomics , vol.5 , Issue.2 , pp. 522-533
    • Doherty, M.K.1    Whitehead, C.2    McCormack, H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 16
    • 38349117099 scopus 로고    scopus 로고
    • Determination of global protein turnover in stressed Mycobacterium cells using hybrid-linear ion trap-Fourier transform mass spectrometry
    • Rao, P. K.; Roxas, B. A. P.; Li, Q. Determination of global protein turnover in stressed Mycobacterium cells using hybrid-linear ion trap-Fourier transform mass spectrometry. Anal. Chem. 2008, 80 (2), 396-406.
    • (2008) Anal. Chem , vol.80 , Issue.2 , pp. 396-406
    • Rao, P.K.1    Roxas, B.A.P.2    Li, Q.3
  • 18
    • 0016808917 scopus 로고
    • A statistical analysis of the relationship between degradative rates and molecular weights of proteins
    • Dice, J. F.; Goldberg, A. L. A statistical analysis of the relationship between degradative rates and molecular weights of proteins. Arch. Biochem. Biophys. 1975, 170 (1), 213-9.
    • (1975) Arch. Biochem. Biophys , vol.170 , Issue.1 , pp. 213-219
    • Dice, J.F.1    Goldberg, A.L.2
  • 19
    • 0016772784 scopus 로고
    • Relationship between in vivo degradative rates and isoelectric points of proteins
    • Dice, J. F.; Goldberg, A. L. Relationship between in vivo degradative rates and isoelectric points of proteins. Proc. Natl. Acad. Sci. U.SA. 1975, 72 (10), 3893-7.
    • (1975) Proc. Natl. Acad. Sci. U.SA , vol.72 , Issue.10 , pp. 3893-3897
    • Dice, J.F.1    Goldberg, A.L.2
  • 20
    • 0018790726 scopus 로고
    • Studies on the relationship between the degradative rates of proteins in vivo and their isoelectric points
    • Dice, J. F.; Hess, E. J.; Goldberg, A. L. Studies on the relationship between the degradative rates of proteins in vivo and their isoelectric points. Biochem. J. 1979, 178 (2), 305-12.
    • (1979) Biochem. J , vol.178 , Issue.2 , pp. 305-312
    • Dice, J.F.1    Hess, E.J.2    Goldberg, A.L.3
  • 21
    • 0016908233 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells: Part 2
    • Goldberg, A. L.; St John, A. C. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu. Rev. Biochem. 1976, 45, 747-803.
    • (1976) Annu. Rev. Biochem , vol.45 , pp. 747-803
    • Goldberg, A.L.1    St John, A.C.2
  • 22
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A.; Finley, D.; Varshavsky, A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 1986, 234 (4773), 179-86.
    • (1986) Science , vol.234 , Issue.4773 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 23
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S.; Wells, R.; Rechsteiner, M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986, 234 (4774), 364-8.
    • (1986) Science , vol.234 , Issue.4774 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 25
    • 41149125082 scopus 로고    scopus 로고
    • Structural disorder serves as a weak signal for intracellular protein degradation
    • Tompa, P.; Prilusky, J.; Silman, I.; Sussman, J. L. Structural disorder serves as a weak signal for intracellular protein degradation. Proteins 2008, 71 (2), 903-9.
    • (2008) Proteins , vol.71 , Issue.2 , pp. 903-909
    • Tompa, P.1    Prilusky, J.2    Silman, I.3    Sussman, J.L.4
  • 26
    • 0023425498 scopus 로고
    • The N-end rule of selective protein turnover: Mechanistic aspects and functional implications
    • Varshavsky, A.; Bachmair, A.; Finley, D. The N-end rule of selective protein turnover: mechanistic aspects and functional implications. Biochem. Soc. Trans. 1987, 15 (5), 815-6.
    • (1987) Biochem. Soc. Trans , vol.15 , Issue.5 , pp. 815-816
    • Varshavsky, A.1    Bachmair, A.2    Finley, D.3
  • 27
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V.; Tobias, J. W.; Bachmair, A.; Marriott, D.; Ecker, D. J.; Gonda, D. K.; Varshavsky, A. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 1989, 243 (4898), 1576-83.
    • (1989) Science , vol.243 , Issue.4898 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 30
    • 1642314524 scopus 로고    scopus 로고
    • A novel proteomic screen for peptide- protein interactions
    • Schulze, W. X.; Mann, M. A novel proteomic screen for peptide- protein interactions. J. Biol. Chem. 2004, 279 (11), 10756-64.
    • (2004) J. Biol. Chem , vol.279 , Issue.11 , pp. 10756-10764
    • Schulze, W.X.1    Mann, M.2
  • 31
    • 24044515001 scopus 로고    scopus 로고
    • Prilusky, J.; Felder, C. E.; Zeev-Ben-Mordehai, T.; Rydberg, E. H.; Man, O.; Beckmann, J. S.; Silman, I.; Sussman, J. L. Foldlndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 2005, 21 (16), 3435-8.
    • Prilusky, J.; Felder, C. E.; Zeev-Ben-Mordehai, T.; Rydberg, E. H.; Man, O.; Beckmann, J. S.; Silman, I.; Sussman, J. L. Foldlndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 2005, 21 (16), 3435-8.
  • 32
    • 0032814479 scopus 로고    scopus 로고
    • Energetics of free-ranging mammals, reptiles, and birds
    • Nagy, K. A.; Girard, I. A.; Brown, T. K. Energetics of free-ranging mammals, reptiles, and birds. Annu Rev Nutr 1999, 19, 247-77.
    • (1999) Annu Rev Nutr , vol.19 , pp. 247-277
    • Nagy, K.A.1    Girard, I.A.2    Brown, T.K.3
  • 33
    • 0035994652 scopus 로고    scopus 로고
    • Etruscan shrew muscle: The consequences of being small
    • Jurgens, K. D. Etruscan shrew muscle: the consequences of being small. J. Exp. Biol. 2002, 205 (Pt 15), 2161-6.
    • (2002) J. Exp. Biol , vol.205 , Issue.PART 15 , pp. 2161-2166
    • Jurgens, K.D.1
  • 34
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • Miller, S.; Lesk, A. M.; Janin, J.; Chothia, C. The accessible surface area and stability of oligomeric proteins. Nature 1987, 328 (6133), 834-6.
    • (1987) Nature , vol.328 , Issue.6133 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 35
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky, A. The N-end rule. Cell 1992, 69 (5), 725-35.
    • (1992) Cell , vol.69 , Issue.5 , pp. 725-735
    • Varshavsky, A.1
  • 36
    • 20444404618 scopus 로고    scopus 로고
    • Regulated protein degradation
    • Varshavsky, A. Regulated protein degradation. Trends Biochem. Sci. 2005, 30 (6), 283-6.
    • (2005) Trends Biochem. Sci , vol.30 , Issue.6 , pp. 283-286
    • Varshavsky, A.1
  • 37
    • 33845953070 scopus 로고    scopus 로고
    • Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms
    • Hu, R.-G.; Brower, C. S.; Wang, H.; Davydov, I. V.; Sheng, J.; Zhou, J.; Kwon, Y. T.; Varshavsky, A. Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms. J. Biol. Chem. 2006, 281 (43), 32559-32573.
    • (2006) J. Biol. Chem , vol.281 , Issue.43 , pp. 32559-32573
    • Hu, R.-G.1    Brower, C.S.2    Wang, H.3    Davydov, I.V.4    Sheng, J.5    Zhou, J.6    Kwon, Y.T.7    Varshavsky, A.8
  • 38
    • 39149104693 scopus 로고    scopus 로고
    • Are protein complexes made of cores, modules and attachments?
    • Pang, C. N.; Krycer, J. R.; Lek, A.; Wilkins, M. R. Are protein complexes made of cores, modules and attachments? Proteomics 2008, 8 (3), 425-34.
    • (2008) Proteomics , vol.8 , Issue.3 , pp. 425-434
    • Pang, C.N.1    Krycer, J.R.2    Lek, A.3    Wilkins, M.R.4
  • 39
    • 34249982906 scopus 로고    scopus 로고
    • Nuclear export and cytoplasmic maturation of ribosomal subunits
    • Zemp, I.; Kutay, U. Nuclear export and cytoplasmic maturation of ribosomal subunits. FEBS Lett. 2007, 581 (15), 2783-93.
    • (2007) FEBS Lett , vol.581 , Issue.15 , pp. 2783-2793
    • Zemp, I.1    Kutay, U.2
  • 40
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
    • Lam, Y. W.; Lamond, A. I.; Mann, M.; Andersen, J. S. Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr. Biol. 2007, 17 (9), 749-60.
    • (2007) Curr. Biol , vol.17 , Issue.9 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 41
    • 34548489876 scopus 로고    scopus 로고
    • Balanced production of ribosomal proteins
    • Perry, R. P. Balanced production of ribosomal proteins. Gene 2007, 401 (1-2), 1-3.
    • (2007) Gene , vol.401 , Issue.1-2 , pp. 1-3
    • Perry, R.P.1
  • 42
    • 33748567487 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • Williamson, J. R. Assembly of the 30S ribosomal subunit. Q. Rev. Biophys. 2005, 38 (4), 397-403.
    • (2005) Q. Rev. Biophys , vol.38 , Issue.4 , pp. 397-403
    • Williamson, J.R.1
  • 45
  • 46
    • 0037218838 scopus 로고    scopus 로고
    • Autoregulation in the biosynthesis of ribosomes
    • Zhao, Y.; Sohn, J. H.; Warner, J. R. Autoregulation in the biosynthesis of ribosomes. Mol. Cell. Biol. 2003, 23 (2), 699-707.
    • (2003) Mol. Cell. Biol , vol.23 , Issue.2 , pp. 699-707
    • Zhao, Y.1    Sohn, J.H.2    Warner, J.R.3
  • 47
    • 17144414925 scopus 로고    scopus 로고
    • Overexpression of proteasome betas assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates
    • Chondrogianni, N.; Tzavelas, C.; Pemberton, A. J.; Nezis, I. P.; Rivett, A. J.; Gonos, E. S. Overexpression of proteasome betas assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates. J. Biol. Chem. 2005, 280 (12), 11840-50.
    • (2005) J. Biol. Chem , vol.280 , Issue.12 , pp. 11840-11850
    • Chondrogianni, N.1    Tzavelas, C.2    Pemberton, A.J.3    Nezis, I.P.4    Rivett, A.J.5    Gonos, E.S.6
  • 48
    • 36749025650 scopus 로고    scopus 로고
    • The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum
    • Fricke, B.; Heink, S.; Steffen, J.; Moetzel, P. M.; Kruger, E. The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum. EMBO Rep. 2007, 8(12), 1170-5.
    • (2007) EMBO Rep , vol.8 , Issue.12 , pp. 1170-1175
    • Fricke, B.1    Heink, S.2    Steffen, J.3    Moetzel, P.M.4    Kruger, E.5
  • 52
    • 0035067586 scopus 로고    scopus 로고
    • 20S proteasome biogenesis
    • Kruger, E.; Kloetzel, P. M.; Enenkel, C. 20S proteasome biogenesis. Biochimie 2001, 83 (3-4), 289-93.
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 289-293
    • Kruger, E.1    Kloetzel, P.M.2    Enenkel, C.3
  • 54
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • Beynon, R. J.; Doherty, M. K.; Pratt, J. M.; Gaskell, S. J. Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Nat. Methods 2005, 2 (8), 587-9.
    • (2005) Nat. Methods , vol.2 , Issue.8 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 55
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for pro-teomics using concatenated signature peptides encoded by Qcon-CAT genes
    • Pratt, J. M.; Simpson, D. M.; Doherty, M. K.; Rivers, J.; Gaskell, S. J.; Beynon, R. J. Multiplexed absolute quantification for pro-teomics using concatenated signature peptides encoded by Qcon-CAT genes. Nat. Protoc. 2006, 1 (2), 1029-43.
    • (2006) Nat. Protoc , vol.1 , Issue.2 , pp. 1029-1043
    • Pratt, J.M.1    Simpson, D.M.2    Doherty, M.K.3    Rivers, J.4    Gaskell, S.J.5    Beynon, R.J.6
  • 56
    • 34548427053 scopus 로고    scopus 로고
    • Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT
    • Rivers, J.; Simpson, D. M.; Robertson, D. H.; Gaskell, S. J.; Beynon, R. J. Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT. Mol. Cell. Proteomics 2007, 68, 1416-27.
    • (2007) Mol. Cell. Proteomics , vol.68 , pp. 1416-1427
    • Rivers, J.1    Simpson, D.M.2    Robertson, D.H.3    Gaskell, S.J.4    Beynon, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.