메뉴 건너뛰기




Volumn 278, Issue 24, 2011, Pages 4943-4954

Rate, affinity and calcium dependence of nitric oxide synthase isoform binding to the primary physiological regulator calmodulin

Author keywords

calmodulin; kinase; nitric oxide synthase; optical biosensing; protein kinase C

Indexed keywords

CALCIUM ION; CALMODULIN; ENDOTHELIAL NITRIC OXIDE SYNTHASE; ISOPROTEIN; MUTANT PROTEIN; NEURONAL NITRIC OXIDE SYNTHASE; PROTEIN KINASE C;

EID: 82755189778     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08395.x     Document Type: Article
Times cited : (31)

References (39)
  • 1
    • 0025296139 scopus 로고
    • Calcium-dependent nitric oxide synthesis in endothelial cytosol is mediated by calmodulin
    • DOI 10.1016/0014-5793(90)80902-U
    • Busse R, &, Mulsch A, (1990) Calcium-dependent nitric oxide synthesis in endothelial cytosol is mediated by calmodulin. FEBS Lett 265, 133-136. (Pubitemid 20189413)
    • (1990) FEBS Letters , vol.265 , Issue.1-2 , pp. 133-136
    • Busse, R.1    Mulsch, A.2
  • 2
    • 0023676959 scopus 로고
    • Endothelium-derived relaxing factor and nitric oxide possess identical pharmacologic properties as relaxants of bovine arterial and venous smooth muscle
    • Ignarro LJ, Buga GM, Byrns RE, Wood KS, &, Chaudhuri G, (1988) Endothelium-derived relaxing factor and nitric oxide possess identical pharmacologic properties as relaxants of bovine arterial and venous smooth muscle. J Pharmacol Exp Ther 246, 218-226.
    • (1988) J Pharmacol Exp Ther , vol.246 , pp. 218-226
    • Ignarro, L.J.1    Buga, G.M.2    Byrns, R.E.3    Wood, K.S.4    Chaudhuri, G.5
  • 3
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • DOI 10.1038/327524a0
    • Palmer RM, Ferrige AG, &, Moncada S, (1987) Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327, 524-526. (Pubitemid 17085822)
    • (1987) Nature , vol.327 , Issue.6122 , pp. 524-526
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 5
    • 0029933799 scopus 로고    scopus 로고
    • Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform expressed in differentiated skeletal muscle
    • Silvagno F, Xia H, &, Bredt DS, (1996) Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform expressed in differentiated skeletal muscle. J Biol Chem 271, 11204-11208.
    • (1996) J Biol Chem , vol.271 , pp. 11204-11208
    • Silvagno, F.1    Xia, H.2    Bredt, D.S.3
  • 6
    • 0025685395 scopus 로고
    • Inhibition of insulin secretion by interleukin-1 beta and tumour necrosis factor-alpha via an l-arginine-dependent nitric oxide generating mechanism
    • Southern C, Schulster D, &, Green IC, (1990) Inhibition of insulin secretion by interleukin-1 beta and tumour necrosis factor-alpha via an l-arginine-dependent nitric oxide generating mechanism. FEBS Lett 276, 42-44.
    • (1990) FEBS Lett , vol.276 , pp. 42-44
    • Southern, C.1    Schulster, D.2    Green, I.C.3
  • 8
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt DS, Hwang PM, Glatt CE, Lowenstein C, Reed RR, &, Snyder SH, (1991) Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature 351, 714-718. (Pubitemid 21896670)
    • (1991) Nature , vol.351 , Issue.6329 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 10
    • 47249100332 scopus 로고    scopus 로고
    • 2+ concentrations required for calmodulin to bind and activate the enzyme
    • DOI 10.1021/bi8003186
    • 2+ concentrations required for calmodulin to bind and activate the enzyme. Biochemistry 47, 7557-7566. (Pubitemid 351991032)
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7557-7566
    • Tran, Q.-K.1    Leonard, J.2    Black, D.J.3    Persechini, A.4
  • 11
    • 18844362885 scopus 로고    scopus 로고
    • Regulation of endothelial derived nitric oxide in health and disease
    • Sessa WC, (2005) Regulation of endothelial derived nitric oxide in health and disease. Mem Inst Oswaldo Cruz 100 (Suppl 1), 15-18. (Pubitemid 40685434)
    • (2005) Memorias do Instituto Oswaldo Cruz , vol.100 , Issue.SUPPL. 1 , pp. 15-18
    • Sessa, W.C.1
  • 12
    • 0037207099 scopus 로고    scopus 로고
    • Site-specific dephosphorylation of endothelial nitric oxide synthase by protein phosphatase 2A: Evidence for crosstalk between phosphorylation sites
    • DOI 10.1021/bi026732g
    • Greif DM, Kou R, &, Michel T, (2002) Site-specific dephosphorylation of endothelial nitric oxide synthase by protein phosphatase 2A: evidence for crosstalk between phosphorylation sites. Biochemistry 41, 15845-15853. (Pubitemid 36062490)
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15845-15853
    • Greif, D.M.1    Kou, R.2    Michel, T.3
  • 15
    • 33747335659 scopus 로고    scopus 로고
    • Electron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements
    • Roman LJ, &, Masters BS, (2006) Electron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements. J Biol Chem 281, 23111-23118.
    • (2006) J Biol Chem , vol.281 , pp. 23111-23118
    • Roman, L.J.1    Masters, B.S.2
  • 16
    • 0008632745 scopus 로고    scopus 로고
    • Autoinhibition of endothelial nitric-oxide synthase. Identification of an electron transfer control element
    • Nishida CR, &, Ortiz de Montellano PR, (1999) Autoinhibition of endothelial nitric-oxide synthase. Identification of an electron transfer control element. J Biol Chem 274, 14692-14698.
    • (1999) J Biol Chem , vol.274 , pp. 14692-14698
    • Nishida, C.R.1    Ortiz De Montellano, P.R.2
  • 17
    • 33751049930 scopus 로고    scopus 로고
    • Centrin isoforms in mammals. Relation to calmodulin
    • DOI 10.1007/s11033-006-9004-z
    • Friedberg F, (2006) Centrin isoforms in mammals. Relation to calmodulin. Mol Biol Rep 33, 243-252. (Pubitemid 44760393)
    • (2006) Molecular Biology Reports , vol.33 , Issue.4 , pp. 243-252
    • Friedberg, F.1
  • 18
    • 24644460439 scopus 로고    scopus 로고
    • 2+-binding proteins in the functional regulation of TRP channels
    • DOI 10.1007/s00424-005-1427-1
    • 2+-binding proteins in the functional regulation of TRP channels. Pflugers Arch 451, 105-115. (Pubitemid 41424913)
    • (2005) Pflugers Archiv European Journal of Physiology , vol.451 , Issue.1 , pp. 105-115
    • Zhu, M.X.1
  • 19
    • 0034856516 scopus 로고    scopus 로고
    • Evolutionary aspects of calmodulin
    • DOI 10.1080/152165401753311753
    • Friedberg F, &, Rhoads AR, (2001) Evolutionary aspects of calmodulin. IUBMB Life 51, 215-221. (Pubitemid 32848152)
    • (2001) IUBMB Life , vol.51 , Issue.4 , pp. 215-221
    • Friedberg, F.1    Rhoads, A.R.2
  • 22
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads AR, &, Friedberg F, (1997) Sequence motifs for calmodulin recognition. FASEB J 11, 331-340. (Pubitemid 27193937)
    • (1997) FASEB Journal , vol.11 , Issue.5 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 25
    • 0029441693 scopus 로고
    • Control of electron transfer in neuronal nitric oxide synthase by calmodulin, substrate, substrate analogs, and nitric oxide
    • Stuehr DJ, Abu-Soud HM, Rousseau DL, Feldman PL, &, Wang J, (1995) Control of electron transfer in neuronal nitric oxide synthase by calmodulin, substrate, substrate analogs, and nitric oxide. Adv Pharmacol 34, 207-213.
    • (1995) Adv Pharmacol , vol.34 , pp. 207-213
    • Stuehr, D.J.1    Abu-Soud, H.M.2    Rousseau, D.L.3    Feldman, P.L.4    Wang, J.5
  • 26
    • 0029671422 scopus 로고    scopus 로고
    • 2+ dissociation from complexes of calmodulin with nitric oxide synthase or myosin light chain kinase
    • 2+ dissociation from complexes of calmodulin with nitric oxide synthase or myosin light chain kinase. J Biol Chem 271, 62-67.
    • (1996) J Biol Chem , vol.271 , pp. 62-67
    • Persechini, A.1    White, H.D.2    Gansz, K.J.3
  • 27
    • 0027954427 scopus 로고
    • Characterization of the calmodulin-binding domain of rat cerebellar nitric oxide synthase
    • Zhang M, &, Vogel HJ, (1994) Characterization of the calmodulin-binding domain of rat cerebellar nitric oxide synthase. J Biol Chem 269, 981-985. (Pubitemid 24032473)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.2 , pp. 981-985
    • Zhang, M.1    Vogel, H.J.2
  • 28
    • 77449150569 scopus 로고    scopus 로고
    • Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer
    • Guan ZW, Haque MM, Wei CC, Garcin ED, Getzoff ED, &, Stuehr DJ, (2010) Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer. J Biol Chem 285, 3064-3075.
    • (2010) J Biol Chem , vol.285 , pp. 3064-3075
    • Guan, Z.W.1    Haque, M.M.2    Wei, C.C.3    Garcin, E.D.4    Getzoff, E.D.5    Stuehr, D.J.6
  • 29
    • 11144356896 scopus 로고    scopus 로고
    • Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane: A pentabasic amino acid sequence in the autoinhibitory domain of eNOS targets a proteinase K-cleavable peptide on the cytoplasmic face of mitochondria
    • DOI 10.1074/jbc.M308504200
    • Gao S, Chen J, Brodsky SV, Huang H, Adler S, Lee JH, Dhadwal N, Cohen-Gould L, Gross SS, &, Goligorsky MS, (2004) Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane: a pentabasic amino acid sequence in the autoinhibitory domain of eNOS targets a proteinase K-cleavable peptide on the cytoplasmic face of mitochondria. J Biol Chem 279, 15968-15974. (Pubitemid 38509285)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 15968-15974
    • Gao, S.1    Chen, J.2    Brodsky, S.V.3    Huang, H.4    Adler, S.5    Lee, J.H.6    Dhadwal, N.7    Cohen-Gould, L.8    Gross, S.S.9    Goligorsky, M.S.10
  • 30
    • 0037166321 scopus 로고    scopus 로고
    • Disabling a C-terminal autoinhibitory control element in endothelial nitric-oxide synthase by phosphorylation provides a molecular explanation for activation of vascular NO synthesis by diverse physiological stimuli
    • DOI 10.1074/jbc.M200258200
    • Lane P, &, Gross SS, (2002) Disabling a C-terminal autoinhibitory control element in endothelial nitric-oxide synthase by phosphorylation provides a molecular explanation for activation of vascular NO synthesis by diverse physiological stimuli. J Biol Chem 277, 19087-19094. (Pubitemid 34952474)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 19087-19094
    • Lane, P.1    Gross, S.S.2
  • 31
    • 0242666181 scopus 로고    scopus 로고
    • Phosphorylation of Threonine 497 in Endothelial Nitric-oxide Synthase Coordinates the Coupling of L-Arginine Metabolism to Efficient Nitric Oxide Production
    • DOI 10.1074/jbc.M302836200
    • Lin MI, Fulton D, Babbitt R, Fleming I, Busse R, Pritchard KA Jr, &, Sessa WC, (2003) Phosphorylation of threonine 497 in endothelial nitric-oxide synthase coordinates the coupling of l-arginine metabolism to efficient nitric oxide production. J Biol Chem 278, 44719-44726. (Pubitemid 37377229)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44719-44726
    • Lin, M.I.1    Fulton, D.2    Babbitt, R.3    Fleming, I.4    Busse, R.5    Pritchard Jr., K.A.6    Sessa, W.C.7
  • 32
    • 0035947574 scopus 로고    scopus 로고
    • Coordinated control of endothelial nitric-oxide synthase phosphorylation by protein kinase C and the cAMP-dependent protein kinase
    • Michell BJ, Chen Z, Tiganis T, Stapleton D, Katsis F, Power DA, Sim AT, &, Kemp BE, (2001) Coordinated control of endothelial nitric-oxide synthase phosphorylation by protein kinase C and the cAMP-dependent protein kinase. J Biol Chem 276, 17625-17628.
    • (2001) J Biol Chem , vol.276 , pp. 17625-17628
    • Michell, B.J.1    Chen, Z.2    Tiganis, T.3    Stapleton, D.4    Katsis, F.5    Power, D.A.6    Sim, A.T.7    Kemp, B.E.8
  • 33
    • 43049120226 scopus 로고    scopus 로고
    • Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet
    • Abdiche Y, Malashock D, Pinkerton A, &, Pons J, (2008) Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Anal Biochem 377 (2), 209-217.
    • (2008) Anal Biochem , vol.377 , Issue.2 , pp. 209-217
    • Abdiche, Y.1    Malashock, D.2    Pinkerton, A.3    Pons, J.4
  • 34
    • 42049103019 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase: Prototype for pulsed enzymology
    • Salerno JC, (2008) Neuronal nitric oxide synthase: prototype for pulsed enzymology. FEBS Lett 582, 1395-1399.
    • (2008) FEBS Lett , vol.582 , pp. 1395-1399
    • Salerno, J.C.1
  • 35
    • 70350450411 scopus 로고    scopus 로고
    • Space, time and nitric oxide-neuronal nitric oxide synthase generates signal pulses
    • Salerno JC, &, Ghosh DK, (2009) Space, time and nitric oxide-neuronal nitric oxide synthase generates signal pulses. FEBS J 276, 6677-6688.
    • (2009) FEBS J , vol.276 , pp. 6677-6688
    • Salerno, J.C.1    Ghosh, D.K.2
  • 36
    • 0041810555 scopus 로고    scopus 로고
    • Regulation of endothelial nitric oxide synthase by protein kinase C
    • DOI 10.1093/jb/mvg099
    • Matsubara M, Hayashi N, Jing T, &, Titani K, (2003) Regulation of endothelial nitric oxide synthase by protein kinase C. J Biochem 133, 773-781. (Pubitemid 36898649)
    • (2003) Journal of Biochemistry , vol.133 , Issue.6 , pp. 773-781
    • Matsubara, M.1    Hayashi, N.2    Jing, T.3    Titani, K.4
  • 37
    • 0029048347 scopus 로고
    • Neuronal nitric oxide synthase. Expression in Escherichia coli, irreversible inhibition by phenyldiazene, and active site topology
    • Gerber NC, &, Ortiz de Montellano PR, (1995) Neuronal nitric oxide synthase. Expression in Escherichia coli, irreversible inhibition by phenyldiazene, and active site topology. J Biol Chem 270, 17791-17796.
    • (1995) J Biol Chem , vol.270 , pp. 17791-17796
    • Gerber, N.C.1    Ortiz De Montellano, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.