메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages

The amino-terminus of Nitric oxide sensitive guanylyl cyclase α 1 does not affect dimerization but influences subcellular localization

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; LYASE; NITRIC OXIDE SENSITIVE QUANYLYL CYCLASE ALPHA1; UNCLASSIFIED DRUG; GUANYLATE CYCLASE;

EID: 80053585971     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025772     Document Type: Article
Times cited : (15)

References (34)
  • 1
    • 0031473770 scopus 로고    scopus 로고
    • Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis
    • Liu Y, Ruoho AE, Rao VD, Hurley JH, (1997) Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis. Proc Natl Acad Sci U S A 94: 13414-13419.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13414-13419
    • Liu, Y.1    Ruoho, A.E.2    Rao, V.D.3    Hurley, J.H.4
  • 2
    • 24044514657 scopus 로고    scopus 로고
    • Dimerization of nitric oxide-sensitive guanylyl cyclase requires the alpha 1 N terminus
    • Wagner C, Russwurm M, Jager R, Friebe A, Koesling D, (2005) Dimerization of nitric oxide-sensitive guanylyl cyclase requires the alpha 1 N terminus. J Biol Chem 280: 17687-17693.
    • (2005) J Biol Chem , vol.280 , pp. 17687-17693
    • Wagner, C.1    Russwurm, M.2    Jager, R.3    Friebe, A.4    Koesling, D.5
  • 3
    • 0037809223 scopus 로고    scopus 로고
    • A functional domain of the alpha1 subunit of soluble guanylyl cyclase is necessary for activation of the enzyme by nitric oxide and YC-1 but is not involved in heme binding
    • Koglin M, Behrends S, (2003) A functional domain of the alpha1 subunit of soluble guanylyl cyclase is necessary for activation of the enzyme by nitric oxide and YC-1 but is not involved in heme binding. J Biol Chem 278: 12590-12597.
    • (2003) J Biol Chem , vol.278 , pp. 12590-12597
    • Koglin, M.1    Behrends, S.2
  • 4
    • 47249162105 scopus 로고    scopus 로고
    • Alpha1 soluble guanylyl cyclase (sGC) splice forms as potential regulators of human sGC activity
    • Sharina IG, Jelen F, Bogatenkova EP, Thomas A, Martin E, et al. (2008) Alpha1 soluble guanylyl cyclase (sGC) splice forms as potential regulators of human sGC activity. J Biol Chem 283: 15104-15113.
    • (2008) J Biol Chem , vol.283 , pp. 15104-15113
    • Sharina, I.G.1    Jelen, F.2    Bogatenkova, E.P.3    Thomas, A.4    Martin, E.5
  • 5
    • 79959835838 scopus 로고    scopus 로고
    • Nitric Oxide Receptor Soluble Guanylyl Cyclase Undergoes Splicing Regulation in Differentiating Human Embryonic Cells
    • Sharin VG, Mujoo K, Kots AY, Martin E, Murad F, et al. (2011) Nitric Oxide Receptor Soluble Guanylyl Cyclase Undergoes Splicing Regulation in Differentiating Human Embryonic Cells. Stem Cells and Development 20: 1287-1293.
    • (2011) Stem Cells and Development , vol.20 , pp. 1287-1293
    • Sharin, V.G.1    Mujoo, K.2    Kots, A.Y.3    Martin, E.4    Murad, F.5
  • 6
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • Meyer AJ, Dick TP, (2010) Fluorescent protein-based redox probes. Antioxid Redox Signal 13: 621-650.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 7
    • 80053894077 scopus 로고    scopus 로고
    • RNA splicing in regulation of nitric oxide receptor soluble guanylyl cyclase
    • Nitric Oxide
    • Sharina IG, Cote GJ, Martin E, Doursout MF, Murad F, (2011) RNA splicing in regulation of nitric oxide receptor soluble guanylyl cyclase. Nitric Oxide.
    • (2011)
    • Sharina, I.G.1    Cote, G.J.2    Martin, E.3    Doursout, M.F.4    Murad, F.5
  • 8
    • 0037146488 scopus 로고    scopus 로고
    • Highly Sensitive and Fast Protein Detection with Coomassie Brilliant Blue in Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis
    • Kang D, Gho YS, Suh M, Kang C, (2002) Highly Sensitive and Fast Protein Detection with Coomassie Brilliant Blue in Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis. Bull Korean Chem Soc 23: 1511-1512.
    • (2002) Bull Korean Chem Soc , vol.23 , pp. 1511-1512
    • Kang, D.1    Gho, Y.S.2    Suh, M.3    Kang, C.4
  • 9
    • 77955402749 scopus 로고    scopus 로고
    • Fluorescent fusion proteins of soluble guanylyl cyclase indicate proximity of the heme nitric oxide domain and catalytic domain
    • Haase T, Haase N, Kraehling JR, Behrends S, (2010) Fluorescent fusion proteins of soluble guanylyl cyclase indicate proximity of the heme nitric oxide domain and catalytic domain. PLoS One 5: e11617.
    • (2010) PLoS One , vol.5
    • Haase, T.1    Haase, N.2    Kraehling, J.R.3    Behrends, S.4
  • 10
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • Truong K, Ikura M, (2001) The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr Opin Struct Biol 11: 573-578.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 11
    • 0023731036 scopus 로고
    • Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines MD, (1988) Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J 2: 2557-2568.
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 13
    • 24044445562 scopus 로고    scopus 로고
    • Amphipathic alpha-helix mediates the heterodimerization of soluble guanylyl cyclase
    • Shiga T, Suzuki N, (2005) Amphipathic alpha-helix mediates the heterodimerization of soluble guanylyl cyclase. Zoolog Sci 22: 735-742.
    • (2005) Zoolog Sci , vol.22 , pp. 735-742
    • Shiga, T.1    Suzuki, N.2
  • 14
    • 35548977224 scopus 로고    scopus 로고
    • Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo
    • Rothkegel C, Schmidt PM, Atkins DJ, Hoffmann LS, Schmidt HH, et al. (2007) Dimerization region of soluble guanylate cyclase characterized by bimolecular fluorescence complementation in vivo. Mol Pharmacol 72: 1181-1190.
    • (2007) Mol Pharmacol , vol.72 , pp. 1181-1190
    • Rothkegel, C.1    Schmidt, P.M.2    Atkins, D.J.3    Hoffmann, L.S.4    Schmidt, H.H.5
  • 15
    • 14844344676 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic domains of soluble guanylate cyclase: interaction with the heme domain
    • Winger JA, Marletta MA, (2005) Expression and characterization of the catalytic domains of soluble guanylate cyclase: interaction with the heme domain. Biochemistry 44: 4083-4090.
    • (2005) Biochemistry , vol.44 , pp. 4083-4090
    • Winger, J.A.1    Marletta, M.A.2
  • 16
    • 34547135735 scopus 로고    scopus 로고
    • Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress
    • Lin Q, Weis S, Yang G, Weng YH, Helston R, et al. (2007) Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress. J Biol Chem 282: 20621-20633.
    • (2007) J Biol Chem , vol.282 , pp. 20621-20633
    • Lin, Q.1    Weis, S.2    Yang, G.3    Weng, Y.H.4    Helston, R.5
  • 17
    • 79952808113 scopus 로고    scopus 로고
    • Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum
    • Appenzeller-Herzog C, (2011) Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum. J Cell Sci 124: 847-855.
    • (2011) J Cell Sci , vol.124 , pp. 847-855
    • Appenzeller-Herzog, C.1
  • 18
    • 44449090114 scopus 로고    scopus 로고
    • Real-time imaging of the intracellular glutathione redox potential
    • Gutscher M, Pauleau AL, Marty L, Brach T, Wabnitz GH, et al. (2008) Real-time imaging of the intracellular glutathione redox potential. Nat Methods 5: 553-559.
    • (2008) Nat Methods , vol.5 , pp. 553-559
    • Gutscher, M.1    Pauleau, A.L.2    Marty, L.3    Brach, T.4    Wabnitz, G.H.5
  • 19
    • 39649123028 scopus 로고    scopus 로고
    • LPS-induced down-regulation of NO-sensitive guanylyl cyclase in astrocytes occurs by proteasomal degradation in clastosomes
    • Baltrons MA, Pifarre P, Berciano MT, Lafarga M, Garcia A, (2008) LPS-induced down-regulation of NO-sensitive guanylyl cyclase in astrocytes occurs by proteasomal degradation in clastosomes. Mol Cell Neurosci 37: 494-506.
    • (2008) Mol Cell Neurosci , vol.37 , pp. 494-506
    • Baltrons, M.A.1    Pifarre, P.2    Berciano, M.T.3    Lafarga, M.4    Garcia, A.5
  • 20
    • 67349195437 scopus 로고    scopus 로고
    • NO-sensitive guanylyl cyclase beta1 subunit is peripherally associated to chromosomes during mitosis. Novel role in chromatin condensation and cell cycle progression
    • Pifarre P, Baltrons MA, Foldi I, Garcia A, (2009) NO-sensitive guanylyl cyclase beta1 subunit is peripherally associated to chromosomes during mitosis. Novel role in chromatin condensation and cell cycle progression. Int J Biochem Cell Biol 41: 1719-1730.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1719-1730
    • Pifarre, P.1    Baltrons, M.A.2    Foldi, I.3    Garcia, A.4
  • 22
    • 77956256451 scopus 로고    scopus 로고
    • Iron and porphyrin trafficking in heme biogenesis
    • Schultz IJ, Chen C, Paw BH, Hamza I, (2010) Iron and porphyrin trafficking in heme biogenesis. J Biol Chem 285: 26753-26759.
    • (2010) J Biol Chem , vol.285 , pp. 26753-26759
    • Schultz, I.J.1    Chen, C.2    Paw, B.H.3    Hamza, I.4
  • 23
    • 84655167703 scopus 로고    scopus 로고
    • A novel insight into the heme and NO/CO binding mechanism of the alpha subunit of human soluble guanylate cyclase
    • Zhong F, Pan J, Liu X, Wang H, Ying T, et al. (2011) A novel insight into the heme and NO/CO binding mechanism of the alpha subunit of human soluble guanylate cyclase. J Biol Inorg Chem.
    • (2011) J Biol Inorg Chem
    • Zhong, F.1    Pan, J.2    Liu, X.3    Wang, H.4    Ying, T.5
  • 24
    • 0029938767 scopus 로고    scopus 로고
    • Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanylyl cyclase
    • Schrammel A, Behrends S, Schmidt K, Koesling D, Mayer B, (1996) Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanylyl cyclase. Mol Pharmacol 50: 1-5.
    • (1996) Mol Pharmacol , vol.50 , pp. 1-5
    • Schrammel, A.1    Behrends, S.2    Schmidt, K.3    Koesling, D.4    Mayer, B.5
  • 25
    • 70350145165 scopus 로고    scopus 로고
    • Distinct molecular requirements for activation or stabilization of soluble guanylyl cyclase upon haem oxidation-induced degradation
    • Hoffmann LS, Schmidt PM, Keim Y, Schaefer S, Schmidt HH, et al. (2009) Distinct molecular requirements for activation or stabilization of soluble guanylyl cyclase upon haem oxidation-induced degradation. Br J Pharmacol 157: 781-795.
    • (2009) Br J Pharmacol , vol.157 , pp. 781-795
    • Hoffmann, L.S.1    Schmidt, P.M.2    Keim, Y.3    Schaefer, S.4    Schmidt, H.H.5
  • 26
    • 67949105076 scopus 로고    scopus 로고
    • Nitric oxide-independent vasodilator rescues heme-oxidized soluble guanylate cyclase from proteasomal degradation
    • Meurer S, Pioch S, Pabst T, Opitz N, Schmidt PM, et al. (2009) Nitric oxide-independent vasodilator rescues heme-oxidized soluble guanylate cyclase from proteasomal degradation. Circ Res 105: 33-41.
    • (2009) Circ Res , vol.105 , pp. 33-41
    • Meurer, S.1    Pioch, S.2    Pabst, T.3    Opitz, N.4    Schmidt, P.M.5
  • 27
    • 77957906338 scopus 로고    scopus 로고
    • Direct fusion of subunits of heterodimeric nitric oxide sensitive guanylyl cyclase leads to functional enzymes with preserved biochemical properties: evidence for isoform specific activation by ciguates
    • Haase N, Haase T, Kraehling JR, Behrends S, (2010) Direct fusion of subunits of heterodimeric nitric oxide sensitive guanylyl cyclase leads to functional enzymes with preserved biochemical properties: evidence for isoform specific activation by ciguates. Biochem Pharmacol 80: 1676-1683.
    • (2010) Biochem Pharmacol , vol.80 , pp. 1676-1683
    • Haase, N.1    Haase, T.2    Kraehling, J.R.3    Behrends, S.4
  • 28
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M, (1987) An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res 15: 8125-8148.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 30
    • 77954074555 scopus 로고    scopus 로고
    • A rapid method for titrating baculovirus stocks using the Sf-9 Easy Titer cell line
    • Hopkins R, Esposito D, (2009) A rapid method for titrating baculovirus stocks using the Sf-9 Easy Titer cell line. Biotechniques 47: 785-788.
    • (2009) Biotechniques , vol.47 , pp. 785-788
    • Hopkins, R.1    Esposito, D.2
  • 31
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt TG, Skerra A, (2007) The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat Protoc 2: 1528-1535.
    • (2007) Nat Protoc , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 32
    • 0000745994 scopus 로고
    • Isolierung und Kristallisation des Gärungsferments Enolase
    • Warburg O, Christian W, (1941) Isolierung und Kristallisation des Gärungsferments Enolase. Biochem Z 310: 384-421.
    • (1941) Biochem Z , vol.310 , pp. 384-421
    • Warburg, O.1    Christian, W.2
  • 33
    • 0001406574 scopus 로고
    • Methods of Enzymatic Analysis
    • In: Bergmeyer HU, Bergmeyer J, Grassel M, editors, Weinheim, Germany
    • Schultz G, Böhme E, (1984) Methods of Enzymatic Analysis. In: Bergmeyer HU, Bergmeyer J, Grassel M, editors. 3rd ed: Verlag Chemie Weinheim, Germany pp. 379-389.
    • (1984) 3rd Ed: Verlag Chemie , pp. 379-389
    • Schultz, G.1    Böhme, E.2
  • 34
    • 61749091614 scopus 로고    scopus 로고
    • Biochemistry of soluble guanylate cyclase
    • Handb Exp Pharmacol
    • Derbyshire ER, Marletta MA, (2009) Biochemistry of soluble guanylate cyclase. Handb Exp Pharmacol pp. 17-31.
    • (2009) , pp. 17-31
    • Derbyshire, E.R.1    Marletta, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.