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Volumn 2, Issue 78, 2009, Pages

Oxygen-regulated β2-Adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETA ARRESTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; HYPOXIA INDUCIBLE FACTOR; PROLINE DERIVATIVE; RADIOLIGAND; UBIQUITIN PROTEIN LIGASE E3; VON HIPPEL LINDAU PROTEIN; DIOXYGENASE; EGLN3 PROTEIN, HUMAN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; OXYGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROLINE;

EID: 70249122059     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2000444     Document Type: Article
Times cited : (127)

References (45)
  • 1
    • 0037050009 scopus 로고    scopus 로고
    • Seven-transmembrane-spanning receptors and heart function
    • H. A. Rockman, W. J. Koch, R. J. Lefkowitz, Seven-transmembrane-spanning receptors and heart function. Nature 415, 206-212 (2002).
    • (2002) Nature , vol.415 , pp. 206-212
    • Rockman, H.A.1    Koch, W.J.2    Lefkowitz, R.J.3
  • 3
    • 0033535942 scopus 로고    scopus 로고
    • Progressive hypertrophy and heart failure in b1-adrenergic receptor transgenic mice
    • S. Engelhardt, L. Hein, F. Wiesmann, M. J. Lohse, Progressive hypertrophy and heart failure in b1-adrenergic receptor transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 96, 7059-7064 (1999).
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7059-7064
    • Engelhardt, S.1    Hein, L.2    Wiesmann, F.3    Lohse, M.J.4
  • 6
    • 20444445949 scopus 로고    scopus 로고
    • The role of β-adrenergic receptor signaling in cardioprotection
    • H. Tong, D. Bernstein, E. Murphy, C. Steenbergen, The role of β-adrenergic receptor signaling in cardioprotection. FASEB J. 19, 983-985 (2005).
    • (2005) FASEB J. , vol.19 , pp. 983-985
    • Tong, H.1    Bernstein, D.2    Murphy, E.3    Steenbergen, C.4
  • 11
    • 34548667496 scopus 로고    scopus 로고
    • Cardiovascular adjustments for life at high altitude
    • R. Hainsworth, M. J. Drinkhill, Cardiovascular adjustments for life at high altitude. Respir. Physiol. Neurobiol. 158, 204-211 (2007).
    • (2007) Respir. Physiol. Neurobiol. , vol.158 , pp. 204-211
    • Hainsworth, R.1    Drinkhill, M.J.2
  • 13
    • 15444374449 scopus 로고    scopus 로고
    • Inhibition of NGF deprivation-induced death by low oxygen involves suppression of BIMEL and activation of HIF-1
    • L. Xie, R. S. Johnson, R. S. Freeman, Inhibition of NGF deprivation-induced death by low oxygen involves suppression of BIMEL and activation of HIF-1. J. Cell Biol. 168, 911-920 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 911-920
    • Xie, L.1    Johnson, R.S.2    Freeman, R.S.3
  • 16
    • 16644373473 scopus 로고    scopus 로고
    • Role of VHL gene mutation in human cancer
    • W. Y. Kim, W. G. Kaelin, Role of VHL gene mutation in human cancer. J. Clin. Oncol. 22, 4991-5004 (2004).
    • (2004) J. Clin. Oncol. , vol.22 , pp. 4991-5004
    • Kim, W.Y.1    Kaelin, W.G.2
  • 17
    • 35148828429 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1) pathway
    • G. L. Semenza, Hypoxia-inducible factor 1 (HIF-1) pathway. Sci. STKE 2007, cm8 (2007).
    • (2007) Sci. STKE 2007
    • Semenza, G.L.1
  • 19
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • R. K. Bruick, S. L. McKnight, A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294, 1337-1340 (2001).
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 22
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-a chains activated by prolyl hydroxylation
    • N. Masson, C. Willam, P. H. Maxwell, C. W. Pugh, P. J. Ratcliffe, Independent function of two destruction domains in hypoxia-inducible factor-a chains activated by prolyl hydroxylation. EMBO J. 20, 5197-5206 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 23
    • 0037131159 scopus 로고    scopus 로고
    • Sequence determinants in hypoxiainducible factor-1a for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3
    • J. Huang, Q. Zhao, S. M. Mooney, F. S. Lee, Sequence determinants in hypoxiainducible factor-1a for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3. J. Biol. Chem. 277, 39792-39800 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39792-39800
    • Huang, J.1    Zhao, Q.2    Mooney, S.M.3    Lee, F.S.4
  • 24
    • 11244279649 scopus 로고    scopus 로고
    • Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation
    • D. Li, M. Hirsilä, P. Koivunen, M. C. Brenner, L. Xu, C. Yang, K. I. Kivirikko, J. Myllyharju, Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation. J. Biol. Chem. 279, 55051-55059 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 55051-55059
    • Li, D.1    Hirsilä, M.2    Koivunen, P.3    Brenner, M.C.4    Xu, L.5    Yang, C.6    Kivirikko, K.I.7    Myllyharju, J.8
  • 26
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB EGL-9 and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • RESEARCH0007
    • L. Aravind, E. V. Koonin, The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases. Genome Biol. 2, RESEARCH0007 (2001).
    • (2001) Genome Biol. , vol.2
    • Aravind, L.1    Koonin, E.V.2
  • 29
    • 48649098334 scopus 로고    scopus 로고
    • PVHL: A multipurpose adaptor protein
    • I. J. Frew, W. Krek, pVHL: A multipurpose adaptor protein. Sci. Signal. 1, pe30 (2008).
    • (2008) Sci. Signal. , vol.1
    • Frew, I.J.1    Krek, W.2
  • 31
    • 42449163874 scopus 로고    scopus 로고
    • Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure
    • Y. A. Minamishima, J. Moslehi, N. Bardeesy, D. Cullen, R. T. Bronson, W. G. Kaelin Jr., Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure. Blood 111, 3236-3244 (2008).
    • (2008) Blood , vol.111 , pp. 3236-3244
    • Minamishima, Y.A.1    Moslehi, J.2    Bardeesy, N.3    Cullen, D.4    Bronson, R.T.5    Kaelin Jr., W.G.6
  • 32
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolylhydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia
    • E. Berra, E. Benizri, A. Ginouves, V. Volmat, D. Roux, J. Pouysségur, HIF prolylhydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia. EMBO J. 22, 4082-4090 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouysségur, J.6
  • 33
    • 1842627462 scopus 로고    scopus 로고
    • SM-20 EGL-9 and the EGLN family of hypoxia-inducible factor prolyl hydroxylases
    • R. S. Freeman, D. M. Hasbani, E. A. Lipscomb, J. A. Straub, L. Xie, SM-20, EGL-9, and the EGLN family of hypoxia-inducible factor prolyl hydroxylases. Mol. Cells 16, 1-12 (2003).
    • (2003) Mol. Cells , vol.16 , pp. 1-12
    • Freeman, R.S.1    Hasbani, D.M.2    Lipscomb, E.A.3    Straub, J.A.4    Xie, L.5
  • 34
    • 0036433394 scopus 로고    scopus 로고
    • Mammalian EGLN genes have distinct patterns of mRNA expression and regulation
    • M. E. Lieb, K. Menzies, M. C. Moschella, R. Ni, M. B. Taubman, Mammalian EGLN genes have distinct patterns of mRNA expression and regulation. Biochem. Cell Biol. 80, 421-426 (2002).
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 421-426
    • Lieb, M.E.1    Menzies, K.2    Moschella, M.C.3    Ni, R.4    Taubman, M.B.5
  • 35
    • 0034636080 scopus 로고    scopus 로고
    • Catecholamines, cardiac β-adrenergic receptors, and heart failure
    • R. J. Lefkowitz, H. A. Rockman, W. J. Koch, Catecholamines, cardiac β-adrenergic receptors, and heart failure. Circulation 101, 1634-1637 (2000).
    • (2000) Circulation , vol.101 , pp. 1634-1637
    • Lefkowitz, R.J.1    Rockman, H.A.2    Koch, W.J.3
  • 37
    • 24744472029 scopus 로고    scopus 로고
    • 2 adrenergic receptor enhances cardioprotective effects of ischemic preconditioning in rat hearts after myocardial infarction. Interact
    • 2 adrenergic receptor enhances cardioprotective effects of ischemic preconditioning in rat hearts after myocardial infarction. Interact. Cardiovasc. Thorac. Surg. 4, 163-167 (2005).
    • (2005) Cardiovasc. Thorac. Surg. , vol.4 , pp. 163-167
    • Mieno, S.1    Watanabe, F.2    Sawa, Y.3    Horimoto, H.4
  • 40
    • 23644461909 scopus 로고    scopus 로고
    • Age-dependent increase of prolyl-4-hydroxylase domain (PHD) 3 expression in human and mouse heart
    • S. Rohrbach, A. Simm, R. Pregla, C. Franke, D. M. Katschinski, Age-dependent increase of prolyl-4-hydroxylase domain (PHD) 3 expression in human and mouse heart. Biogerontology 6, 165-171 (2005).
    • (2005) Biogerontology , vol.6 , pp. 165-171
    • Rohrbach, S.1    Simm, A.2    Pregla, R.3    Franke, C.4    Katschinski, D.M.5
  • 41
    • 33750976389 scopus 로고    scopus 로고
    • Placental but not heart defects are associated with elevated hypoxia-inducible factor a levels in mice lacking prolyl hydroxylase domain protein 2
    • K. Takeda, V. C. Ho, H. Takeda, L. J. Duan, A. Nagy, G. H. Fong, Placental but not heart defects are associated with elevated hypoxia-inducible factor a levels in mice lacking prolyl hydroxylase domain protein 2. Mol. Cell. Biol. 26, 8336-8346 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8336-8346
    • Takeda, K.1    Ho, V.C.2    Takeda, H.3    Duan, L.J.4    Nagy, A.5    Fong, G.H.6
  • 45
    • 77953655871 scopus 로고    scopus 로고
    • This work was supported by P01-HL075443, U19-ES012496, RO1-NS034400 and an RJL Award for Scientific Innovation. We thank D. T. Hess for discussion, advice, and assistance with the manuscript and L. A. Desouza for technical help. The authors have no conflicting financial interests
    • This work was supported by P01-HL075443, U19-ES012496, RO1-NS034400 and an RJL Award for Scientific Innovation. We thank D. T. Hess for discussion, advice, and assistance with the manuscript and L. A. Desouza for technical help. The authors have no conflicting financial interests.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.