메뉴 건너뛰기




Volumn 31, Issue 3, 2013, Pages 740-750

Nitric oxide activates intradomain disulfide bond formation in the kinase loop of Akt1/PKBα after burn injury

Author keywords

Akt1 protein kinase B ; Disulfide bond; MS MS; S nitrosylation

Indexed keywords

BIOTIN; CYSTEINE; NITRIC OXIDE; PROTEIN KINASE B; PROTEIN KINASE B ALPHA1; THREONINE; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG;

EID: 84873112613     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.2013.1241     Document Type: Article
Times cited : (13)

References (48)
  • 1
    • 0036324823 scopus 로고    scopus 로고
    • Inverse regulation of protein turnover and amino acid transport in skeletal muscle of hypercatabolic patients
    • Biolo G, Fleming RY, Maggi SP, Nguye TT, Herndon DN and Wolfe RR: Inverse regulation of protein turnover and amino acid transport in skeletal muscle of hypercatabolic patients. J Clin Endocrinol Metab 87: 3378-3384, 2002.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 3378-3384
    • Biolo, G.1    Fleming, R.Y.2    Maggi, S.P.3    Nguye, T.T.4    Herndon, D.N.5    Wolfe, R.R.6
  • 3
    • 0040973209 scopus 로고    scopus 로고
    • Differential signaling by insulin receptor substrate 1 (IRS-1) and IRS-2 in IRS-1-deficient cells
    • Bruning JC, Winnay J, Cheatham B and Kahn CR: Differential signaling by insulin receptor substrate 1 (IRS-1) and IRS-2 in IRS-1-deficient cells. Mol Cell Biol 17: 1513-1521, 1997.
    • (1997) Mol Cell Biol , vol.17 , pp. 1513-1521
    • Bruning, J.C.1    Winnay, J.2    Cheatham, B.3    Kahn, C.R.4
  • 4
    • 0034055787 scopus 로고    scopus 로고
    • Insulin resistance in fat cells from obese Zucker rats - Evidence for an impaired activation and translocation of protein kinase B and glucose transporter 4
    • Carvalho E, Rondinone C and Smith U: Insulin resistance in fat cells from obese Zucker rats - evidence for an impaired activation and translocation of protein kinase B and glucose transporter 4. Mol Cell Biochem 206: 7-16, 2000.
    • (2000) Mol Cell Biochem , vol.206 , pp. 7-16
    • Carvalho, E.1    Rondinone, C.2    Smith, U.3
  • 5
    • 0028032895 scopus 로고
    • Alternative pathway of insulin signaling in mice with targeted disruption of the IRS-1 gene
    • Araki E, Lipes MA, Patti ME, Bruning JC, Haag B, Johnson RS and Kahn CR: Alternative pathway of insulin signaling in mice with targeted disruption of the IRS-1 gene. Nature 372: 186-190, 1994.
    • (1994) Nature , vol.372 , pp. 186-190
    • Araki, E.1    Lipes, M.A.2    Patti, M.E.3    Bruning, J.C.4    Haag, B.5    Johnson, R.S.6    Kahn, C.R.7
  • 6
    • 9644304478 scopus 로고    scopus 로고
    • Glucose control by insulin for critically ill surgical patients
    • Khoury W, Klausner JM, Ben-Abraham R and Szold O: Glucose control by insulin for critically ill surgical patients. J Trauma 57: 1132-1138, 2004.
    • (2004) J Trauma , vol.57 , pp. 1132-1138
    • Khoury, W.1    Klausner, J.M.2    Ben-Abraham, R.3    Szold, O.4
  • 7
    • 16644388074 scopus 로고    scopus 로고
    • Insulin resistance in thermally-injured rats is associated with post-receptor alterations in skeletal muscle, liver and adipose tissue
    • Carter EA, Burks D, Fischman AJ, White M and Tompkins RG: Insulin resistance in thermally-injured rats is associated with post-receptor alterations in skeletal muscle, liver and adipose tissue. Int J Mol Med 14: 653-658, 2004.
    • (2004) Int J Mol Med , vol.14 , pp. 653-658
    • Carter, E.A.1    Burks, D.2    Fischman, A.J.3    White, M.4    Tompkins, R.G.5
  • 9
  • 10
    • 0344305782 scopus 로고    scopus 로고
    • Insulin signaling in health and disease
    • White MF: Insulin signaling in health and disease. Science 302: 1710-1711, 2003.
    • (2003) Science , vol.302 , pp. 1710-1711
    • White, M.F.1
  • 11
    • 26444436274 scopus 로고    scopus 로고
    • Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: Role of IRS phosphorylation
    • Zhang Q, Carter EA, Ma BY, White M, Fischman AF and Tompkins RG: Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: role of IRS phosphorylation. Life Sci 77: 3068-3077, 2005.
    • (2005) Life Sci , vol.77 , pp. 3068-3077
    • Zhang, Q.1    Carter, E.A.2    Ma, B.Y.3    White, M.4    Fischman, A.F.5    Tompkins, R.G.6
  • 12
    • 27844435600 scopus 로고    scopus 로고
    • Minireview: Recent developments in the regulation of glucose transporter-4 traffic: New signals, locations, and partners
    • Ishiki M and Klip A: Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners. Endocrinology 146: 5071-5078, 2005.
    • (2005) Endocrinology , vol.146 , pp. 5071-5078
    • Ishiki, M.1    Klip, A.2
  • 14
    • 17144395975 scopus 로고    scopus 로고
    • The activation of Akt/PKB signaling pathway and cell survival
    • Song G, Quyang G and Bao S: The activation of Akt/PKB signaling pathway and cell survival. J Cell Mol Med 9: 59-71, 2005.
    • (2005) J Cell Mol Med , vol.9 , pp. 59-71
    • Song, G.1    Quyang, G.2    Bao, S.3
  • 15
    • 33745480146 scopus 로고    scopus 로고
    • Cell signaling. A new way to burn fat
    • Neels JG and Olefsky JM: Cell signaling. A new way to burn fat. Science 312: 1756-1758, 2006.
    • (2006) Science , vol.312 , pp. 1756-1758
    • Neels, J.G.1    Olefsky, J.M.2
  • 16
    • 13444265870 scopus 로고    scopus 로고
    • Another role for celebrity: Akt and insulin resistance
    • Tian R: Another role for celebrity: Akt and insulin resistance. Circ Res 96: 139-140, 2005.
    • (2005) Circ Res , vol.96 , pp. 139-140
    • Tian, R.1
  • 17
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A key mediator of cell proliferation, survival and insulin responses?
    • Lawlor MA and Alessi DR: PKB/Akt: a key mediator of cell proliferation, survival and insulin responses? J Cell Sci 114: 2903-2910, 2001.
    • (2001) J Cell Sci , vol.114 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 18
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA and Barford D: Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol Cell 9: 1227-1240, 2002.
    • (2002) Mol Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 19
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang J, Cron P, Good VM, Thompson V, Hemmings BA and Barford D: Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat Struct Biol 9: 940-944, 2002.
    • (2002) Nat Struct Biol , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 21
    • 27844553839 scopus 로고    scopus 로고
    • Akt crystal structure and Akt-specific inhibitors
    • Kumar CC and Madison V: Akt crystal structure and Akt-specific inhibitors. Oncogene 24: 7493-7501, 2005.
    • (2005) Oncogene , vol.24 , pp. 7493-7501
    • Kumar, C.C.1    Madison, V.2
  • 23
    • 2342565881 scopus 로고    scopus 로고
    • Advances in protein kinase B signaling: AKTion on multiple fronts
    • Brazil DP, Yang ZZ and Hemmings BA: Advances in protein kinase B signaling: AKTion on multiple fronts. Trends Biochem Sci 29: 233-242, 2004.
    • (2004) Trends Biochem Sci , vol.29 , pp. 233-242
    • Brazil, D.P.1    Yang, Z.Z.2    Hemmings, B.A.3
  • 24
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins: Getting in on the Akt
    • Brazil DP, Park J and Hemmings BA: PKB binding proteins: getting in on the Akt. Cell 111: 293-303, 2002.
    • (2002) Cell , vol.111 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 25
    • 33745610132 scopus 로고    scopus 로고
    • Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry
    • Huang BX and Kim HY: Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry. Mol Cell Proteomics 5: 1045-1053, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1045-1053
    • Huang, B.X.1    Kim, H.Y.2
  • 28
    • 14844300857 scopus 로고    scopus 로고
    • S-Nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance
    • Yasukawa T, Tokunaga E, Ota H, Sugita H, Martyn JA and Kaneki M: S-Nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance. J Biol Chem 280: 7511-7518, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 7511-7518
    • Yasukawa, T.1    Tokunaga, E.2    Ota, H.3    Sugita, H.4    Martyn, J.A.5    Kaneki, M.6
  • 30
    • 1242263882 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the Pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates
    • Auguin D, Barthe P, Auge-Senegas MT, Stern MH, Noguchi M and Roumestand C: Solution structure and backbone dynamics of the Pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates. J Biomol NMR 28: 137-155, 2004.
    • (2004) J Biomol NMR , vol.28 , pp. 137-155
    • Auguin, D.1    Barthe, P.2    Auge-Senegas, M.T.3    Stern, M.H.4    Noguchi, M.5    Roumestand, C.6
  • 31
    • 0346749513 scopus 로고    scopus 로고
    • Glotaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata H, Ihara Y, Nakamura H, Yodoi J, Sumikawa K and Kondo T: Glotaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem 278: 50226-50233, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 32
    • 19544387641 scopus 로고    scopus 로고
    • A new approach for sequencing human IRS1 phosphotyrosine-containing peptides using CapLC-Q-TOF(micro)
    • Lu XM, Lu MY, Fischman AJ and Tompkins RG: A new approach for sequencing human IRS1 phosphotyrosine-containing peptides using CapLC-Q-TOF(micro). J Mass Spectrom 40: 599-607, 2005.
    • (2005) J Mass Spectrom , vol.40 , pp. 599-607
    • Lu, X.M.1    Lu, M.Y.2    Fischman, A.J.3    Tompkins, R.G.4
  • 33
    • 25144521807 scopus 로고    scopus 로고
    • Site-specific detection of S-nitrosylated PKBa/Akt1 from rat soleus muscle using CapLC-Q-TOF(micro) mass spectrometry
    • Lu XM, Lu M, Tompkins RG and Fischman AJ: Site-specific detection of S-nitrosylated PKBa/Akt1 from rat soleus muscle using CapLC-Q-TOF(micro) mass spectrometry. J Mass Spectrom 40: 1140-1148, 2005.
    • (2005) J Mass Spectrom , vol.40 , pp. 1140-1148
    • Lu, X.M.1    Lu, M.2    Tompkins, R.G.3    Fischman, A.J.4
  • 35
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for detection of S-nitrosylated proteins
    • Jaffrey SR and Snyder SH: The biotin switch method for detection of S-nitrosylated proteins. Science STKE 86: 1-9, 2001.
    • (2001) Science STKE , vol.86 , pp. 1-9
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 36
  • 37
    • 32244445145 scopus 로고    scopus 로고
    • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures
    • Hao G, Derakhshan B, Shi L, Campagne F and Gross SS: SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures. Proc Natl Acad Sci USA 103: 1012-1017, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1012-1017
    • Hao, G.1    Derakhshan, B.2    Shi, L.3    Campagne, F.4    Gross, S.S.5
  • 39
    • 1042267391 scopus 로고    scopus 로고
    • Detection and proteomic identification of S-nitrosylated proteins in endothelial cells
    • Martinez-Ruiz A and Lamas S: Detection and proteomic identification of S-nitrosylated proteins in endothelial cells. Arch Biochem Biophys 423: 192-199, 2004.
    • (2004) Arch Biochem Biophys , vol.423 , pp. 192-199
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 40
    • 17844373533 scopus 로고    scopus 로고
    • Roles of nitric oxide and prostaglandins in pathogenesis of delayed colonic transit after burn injury in rats
    • Gan HT and Chen JDZ: Roles of nitric oxide and prostaglandins in pathogenesis of delayed colonic transit after burn injury in rats. Am J Physiol Regul Integr Comp Physiol 288: R1316-R1324, 2005.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Gan, H.T.1    Chen, J.D.Z.2
  • 41
    • 3042842603 scopus 로고    scopus 로고
    • Inflammation and nitric oxide production in skeletal muscle of type 2 diabetic patients
    • Torres SH, De Sanctis JB, de L Briceno M, Hernandez N and Finol HJ: Inflammation and nitric oxide production in skeletal muscle of type 2 diabetic patients. J Endocrinol 181: 419-427, 2004.
    • (2004) J Endocrinol , vol.181 , pp. 419-427
    • Torres, S.H.1    De Sanctis, J.B.2    De L Briceno, M.3    Hernandez, N.4    Finol, H.J.5
  • 42
    • 34248998027 scopus 로고    scopus 로고
    • Nitrosative stress in the ER: A new role for S-nitrosylation in neurodegenerative diseases
    • Benhar M, Forrester MT and Stamler JS: Nitrosative stress in the ER: a new role for S-nitrosylation in neurodegenerative diseases. ACS Chem Biol 1: 355-358, 2006.
    • (2006) ACS Chem Biol , vol.1 , pp. 355-358
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 43
    • 34447513434 scopus 로고    scopus 로고
    • Regulation and specificity of S-nitrosylation and denitrosylation
    • Tannenbaum SR and White FM: Regulation and specificity of S-nitrosylation and denitrosylation. ACS Chem Biol 1: 615-618, 2006.
    • (2006) ACS Chem Biol , vol.1 , pp. 615-618
    • Tannenbaum, S.R.1    White, F.M.2
  • 44
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N: The biochemistry and physiology of S-nitrosothiols. Ann Rev Pharmacol Toxicol 42: 585-600, 2002.
    • (2002) Ann Rev Pharmacol Toxicol , vol.42 , pp. 585-600
    • Hogg, N.1
  • 45
    • 0028987969 scopus 로고
    • NO+, NO•, and NO- donation by S-nitrosothiols: Implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • Arnelle DR and Stamler JS: NO+, NO•, and NO- donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch Biochem Biophys 318: 279-285, 1995.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 46
    • 33748470543 scopus 로고    scopus 로고
    • Targeted disruption of iNOS prevents LPS-induced S-nitrosation of IRbeta/IRS-1 and Akt and insulin resistance in muscle of mice
    • Carvalho-Filho MA, Ueno M, Carvalheira JB, Velloso LA and Saad MJ: Targeted disruption of iNOS prevents LPS-induced S-nitrosation of IRbeta/IRS-1 and Akt and insulin resistance in muscle of mice. Am J Physiol Endocrinol Metab 291: E476-E482, 2006.
    • (2006) Am J Physiol Endocrinol Metab , vol.291
    • Carvalho-Filho, M.A.1    Ueno, M.2    Carvalheira, J.B.3    Velloso, L.A.4    Saad, M.J.5
  • 47
    • 77958576132 scopus 로고    scopus 로고
    • Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition
    • Wu WI, Voegtli WC, Sturgis HL, Dizon FP, Vigers GP and Brandhuber BJ: Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition. PLos One 5: e12913, 2010.
    • (2010) PLos One , vol.5
    • Wu, W.I.1    Voegtli, W.C.2    Sturgis, H.L.3    Dizon, F.P.4    Vigers, G.P.5    Brandhuber, B.J.6
  • 48
    • 80052964176 scopus 로고    scopus 로고
    • The PKB/FOXO switch in aging and cancer
    • Kloet DE and Burgering BM: The PKB/FOXO switch in aging and cancer. Biochim Biophys Acta 1813: 1926-1937, 2011.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1926-1937
    • Kloet, D.E.1    Burgering, B.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.