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Volumn 377, Issue 4, 2008, Pages 1042-1046

Phosphorylation of argininosuccinate synthase by protein kinase A

Author keywords

Argininosuccinate synthase; Nitric oxide; Phosphorylation; Protein kinase A; Vascular endothelial growth factor; Vascular endothelium

Indexed keywords

ARGININOSUCCINATE SYNTHASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; NITRIC OXIDE; VASCULOTROPIN;

EID: 56349133959     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.10.056     Document Type: Article
Times cited : (7)

References (35)
  • 1
    • 0027975453 scopus 로고
    • Nitric oxide: a physiologic messenger molecule
    • Bredt D.S., and Snyder S.H. Nitric oxide: a physiologic messenger molecule. Annu. Rev. Biochem. 63 (1994) 175-195
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 175-195
    • Bredt, D.S.1    Snyder, S.H.2
  • 2
    • 0034758378 scopus 로고    scopus 로고
    • Endothelial function and nitric oxide: clinical relevance
    • Vallance P., and Chan N. Endothelial function and nitric oxide: clinical relevance. Heart 85 (2001) 342-350
    • (2001) Heart , vol.85 , pp. 342-350
    • Vallance, P.1    Chan, N.2
  • 3
    • 0037692072 scopus 로고    scopus 로고
    • Argininosuccinate synthetase from the urea cycle to the citrulline-NO cycle
    • Husson A., Brasse-Lagnel C., Fairand A., Renouf S., and Lavoinne A. Argininosuccinate synthetase from the urea cycle to the citrulline-NO cycle. Eur. J. Biochem. 270 (2003) 1887-1899
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1887-1899
    • Husson, A.1    Brasse-Lagnel, C.2    Fairand, A.3    Renouf, S.4    Lavoinne, A.5
  • 4
    • 0034090638 scopus 로고    scopus 로고
    • The preferred source of arginine for high-output nitric oxide synthesis in blood vessels
    • Xie L., Hattori Y., Tume N., and Gross S.S. The preferred source of arginine for high-output nitric oxide synthesis in blood vessels. Semin. Perinatol. 24 (2000) 42-45
    • (2000) Semin. Perinatol. , vol.24 , pp. 42-45
    • Xie, L.1    Hattori, Y.2    Tume, N.3    Gross, S.S.4
  • 6
    • 1542652475 scopus 로고    scopus 로고
    • Nitric oxide production and regulation of endothelial nitric-oxide synthase phosphorylation by prolonged treatment with troglitazone: evidence for involvement of peroxisome proliferator-activated receptor (PPAR) gamma-dependent and PPARgamma-independent signaling pathways
    • Cho D.H., Choi Y.J., Jo S.A., and Jo I. Nitric oxide production and regulation of endothelial nitric-oxide synthase phosphorylation by prolonged treatment with troglitazone: evidence for involvement of peroxisome proliferator-activated receptor (PPAR) gamma-dependent and PPARgamma-independent signaling pathways. J. Biol. Chem. 279 (2004) 2499-2506
    • (2004) J. Biol. Chem. , vol.279 , pp. 2499-2506
    • Cho, D.H.1    Choi, Y.J.2    Jo, S.A.3    Jo, I.4
  • 7
    • 31644439543 scopus 로고    scopus 로고
    • VEGF regulation of endothelial nitric oxide synthase in glomerular endothelial cells
    • Feliers D., Chen X., Akis N., Choudhury G.G., Madaio M., and Kasinath B.S. VEGF regulation of endothelial nitric oxide synthase in glomerular endothelial cells. Kidney Int. 68 (2005) 1648-1659
    • (2005) Kidney Int. , vol.68 , pp. 1648-1659
    • Feliers, D.1    Chen, X.2    Akis, N.3    Choudhury, G.G.4    Madaio, M.5    Kasinath, B.S.6
  • 9
    • 0035844241 scopus 로고    scopus 로고
    • Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation
    • Harris M.B., Ju H., Venema V.J., Liang H., Zou R., Michell B.J., Chen Z.P., Kemp B.E., and Venema R.C. Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation. J. Biol. Chem. 276 (2001) 16587-16591
    • (2001) J. Biol. Chem. , vol.276 , pp. 16587-16591
    • Harris, M.B.1    Ju, H.2    Venema, V.J.3    Liang, H.4    Zou, R.5    Michell, B.J.6    Chen, Z.P.7    Kemp, B.E.8    Venema, R.C.9
  • 10
    • 0041355355 scopus 로고    scopus 로고
    • Direct activation of AMP-activated protein kinase stimulates nitric-oxide synthesis in human aortic endothelial cells
    • Morrow V.A., Foufelle F., Connell J.M., Petrie J.R., Gould G.W., and Salt I.P. Direct activation of AMP-activated protein kinase stimulates nitric-oxide synthesis in human aortic endothelial cells. J. Biol. Chem. 278 (2003) 31629-31639
    • (2003) J. Biol. Chem. , vol.278 , pp. 31629-31639
    • Morrow, V.A.1    Foufelle, F.2    Connell, J.M.3    Petrie, J.R.4    Gould, G.W.5    Salt, I.P.6
  • 11
    • 33846839339 scopus 로고    scopus 로고
    • AMP-activated protein kinase mediates VEGF-stimulated endothelial NO production
    • Reihill J.A., Ewart M.A., Hardie D.G., and Salt I.P. AMP-activated protein kinase mediates VEGF-stimulated endothelial NO production. Biochem. Biophys. Res. Commun. 354 (2007) 1084-1088
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 1084-1088
    • Reihill, J.A.1    Ewart, M.A.2    Hardie, D.G.3    Salt, I.P.4
  • 12
    • 0037772382 scopus 로고    scopus 로고
    • Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase
    • Bauer P.M., Fulton D., Boo Y.C., Sorescu G.P., Kemp B.E., Jo H., and Sessa W.C. Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase. J. Biol. Chem. 278 (2003) 14841-14849
    • (2003) J. Biol. Chem. , vol.278 , pp. 14841-14849
    • Bauer, P.M.1    Fulton, D.2    Boo, Y.C.3    Sorescu, G.P.4    Kemp, B.E.5    Jo, H.6    Sessa, W.C.7
  • 13
    • 0035980110 scopus 로고    scopus 로고
    • Hsp90 ensures the transition from the early Ca2+-dependent to the late phosphorylation-dependent activation of the endothelial nitric-oxide synthase in vascular endothelial growth factor-exposed endothelial cells
    • Brouet A., Sonveaux P., Dessy C., Balligand J.L., and Feron O. Hsp90 ensures the transition from the early Ca2+-dependent to the late phosphorylation-dependent activation of the endothelial nitric-oxide synthase in vascular endothelial growth factor-exposed endothelial cells. J. Biol. Chem. 276 (2001) 32663-32669
    • (2001) J. Biol. Chem. , vol.276 , pp. 32663-32669
    • Brouet, A.1    Sonveaux, P.2    Dessy, C.3    Balligand, J.L.4    Feron, O.5
  • 14
    • 0037131346 scopus 로고    scopus 로고
    • Subcellular targeting and agonist-induced site-specific phosphorylation of endothelial nitric-oxide synthase
    • Gonzalez E., Kou R., Lin A.J., Golan D.E., and Michel T. Subcellular targeting and agonist-induced site-specific phosphorylation of endothelial nitric-oxide synthase. J. Biol. Chem. 277 (2002) 39554-39560
    • (2002) J. Biol. Chem. , vol.277 , pp. 39554-39560
    • Gonzalez, E.1    Kou, R.2    Lin, A.J.3    Golan, D.E.4    Michel, T.5
  • 15
    • 0034698050 scopus 로고    scopus 로고
    • Reconstitution of an endothelial nitric-oxide synthase (eNOS), hsp90, and caveolin-1 complex in vitro. Evidence that hsp90 facilitates calmodulin stimulated displacement of eNOS from caveolin-1
    • Gratton J.P., Fontana J., O'Connor D.S., Garcia-Cardena G., McCabe T.J., and Sessa W.C. Reconstitution of an endothelial nitric-oxide synthase (eNOS), hsp90, and caveolin-1 complex in vitro. Evidence that hsp90 facilitates calmodulin stimulated displacement of eNOS from caveolin-1. J. Biol. Chem. 275 (2000) 22268-22272
    • (2000) J. Biol. Chem. , vol.275 , pp. 22268-22272
    • Gratton, J.P.1    Fontana, J.2    O'Connor, D.S.3    Garcia-Cardena, G.4    McCabe, T.J.5    Sessa, W.C.6
  • 16
    • 0031943236 scopus 로고    scopus 로고
    • VEGF upregulates ecNOS message, protein, and NO production in human endothelial cells
    • Hood J.D., Meininger C.J., Ziche M., and Granger H.J. VEGF upregulates ecNOS message, protein, and NO production in human endothelial cells. Am. J. Physiol. 274 (1998) H1054-1058
    • (1998) Am. J. Physiol. , vol.274
    • Hood, J.D.1    Meininger, C.J.2    Ziche, M.3    Granger, H.J.4
  • 17
    • 0043234527 scopus 로고    scopus 로고
    • Synergistic activation of endothelial nitric-oxide synthase (eNOS) by HSP90 and Akt: calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex
    • Takahashi S., and Mendelsohn M.E. Synergistic activation of endothelial nitric-oxide synthase (eNOS) by HSP90 and Akt: calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex. J. Biol. Chem. 278 (2003) 30821-30827
    • (2003) J. Biol. Chem. , vol.278 , pp. 30821-30827
    • Takahashi, S.1    Mendelsohn, M.E.2
  • 18
    • 0030959249 scopus 로고    scopus 로고
    • Argininosuccinate synthetase overexpression in vascular smooth muscle cells potentiates immunostimulant-induced NO production
    • Xie L., and Gross S.S. Argininosuccinate synthetase overexpression in vascular smooth muscle cells potentiates immunostimulant-induced NO production. J. Biol. Chem. 272 (1997) 16624-16630
    • (1997) J. Biol. Chem. , vol.272 , pp. 16624-16630
    • Xie, L.1    Gross, S.S.2
  • 19
    • 34848871867 scopus 로고    scopus 로고
    • Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle
    • Flam B.R., Eichler D.C., and Solomonson L.P. Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle. Nitric oxide 17 (2007) 115-121
    • (2007) Nitric oxide , vol.17 , pp. 115-121
    • Flam, B.R.1    Eichler, D.C.2    Solomonson, L.P.3
  • 20
    • 15944379598 scopus 로고    scopus 로고
    • Interaction of the endothelial nitric oxide synthase with the CAT-1 arginine transporter enhances NO release by a mechanism not involving arginine transport
    • Li C., Huang W., Harris M.B., Goolsby J.M., and Venema R.C. Interaction of the endothelial nitric oxide synthase with the CAT-1 arginine transporter enhances NO release by a mechanism not involving arginine transport. Biochem. J. 386 (2005) 567-574
    • (2005) Biochem. J. , vol.386 , pp. 567-574
    • Li, C.1    Huang, W.2    Harris, M.B.3    Goolsby, J.M.4    Venema, R.C.5
  • 21
    • 9944259578 scopus 로고    scopus 로고
    • Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline-arginine regeneration pathway
    • Shen L.J., Beloussow K., and Shen W.C. Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline-arginine regeneration pathway. Biochem. Pharmacol. 69 (2005) 97-104
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 97-104
    • Shen, L.J.1    Beloussow, K.2    Shen, W.C.3
  • 22
    • 34547912897 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha reduces argininosuccinate synthase expression and nitric oxide production in aortic endothelial cells
    • Goodwin B.L., Pendleton L.C., Levy M.M., Solomonson L.P., and Eichler D.C. Tumor necrosis factor-alpha reduces argininosuccinate synthase expression and nitric oxide production in aortic endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 293 (2007) H1115-H1121
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293
    • Goodwin, B.L.1    Pendleton, L.C.2    Levy, M.M.3    Solomonson, L.P.4    Eichler, D.C.5
  • 23
    • 0346463072 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha inhibits endothelial nitric-oxide synthase gene promoter activity in bovine aortic endothelial cells
    • Anderson H.D., Rahmutula D., and Gardner D.G. Tumor necrosis factor-alpha inhibits endothelial nitric-oxide synthase gene promoter activity in bovine aortic endothelial cells. J. Biol. Chem. 279 (2004) 963-969
    • (2004) J. Biol. Chem. , vol.279 , pp. 963-969
    • Anderson, H.D.1    Rahmutula, D.2    Gardner, D.G.3
  • 26
    • 2442618330 scopus 로고    scopus 로고
    • Argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells
    • Goodwin B.L., Solomonson L.P., and Eichler D.C. Argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells. J. Biol. Chem. 279 (2004) 18353-18360
    • (2004) J. Biol. Chem. , vol.279 , pp. 18353-18360
    • Goodwin, B.L.1    Solomonson, L.P.2    Eichler, D.C.3
  • 30
    • 4344662343 scopus 로고    scopus 로고
    • Argininosuccinate synthetase is reversibly inactivated by S-nitrosylation in vitro and in vivo
    • Hao G., Xie L., and Gross S.S. Argininosuccinate synthetase is reversibly inactivated by S-nitrosylation in vitro and in vivo. J. Biol. Chem. 279 (2004) 36192-36200
    • (2004) J. Biol. Chem. , vol.279 , pp. 36192-36200
    • Hao, G.1    Xie, L.2    Gross, S.S.3
  • 31
    • 42949170563 scopus 로고    scopus 로고
    • Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column
    • Imami K., Sugiyama N., Kyono Y., Tomita M., and Ishihama Y. Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal. Sci. 24 (2008) 161-166
    • (2008) Anal. Sci. , vol.24 , pp. 161-166
    • Imami, K.1    Sugiyama, N.2    Kyono, Y.3    Tomita, M.4    Ishihama, Y.5
  • 32
    • 0036137466 scopus 로고    scopus 로고
    • VEGF receptor signaling and endothelial function
    • Kliche S., and Waltenberger J. VEGF receptor signaling and endothelial function. IUBMB Life 52 (2001) 61-66
    • (2001) IUBMB Life , vol.52 , pp. 61-66
    • Kliche, S.1    Waltenberger, J.2
  • 34
    • 0034834395 scopus 로고    scopus 로고
    • Direct measurement of VEGF-induced nitric oxide production by choroidal endothelial cells
    • Uhlmann S., Friedrichs U., Eichler W., Hoffmann S., and Wiedemann P. Direct measurement of VEGF-induced nitric oxide production by choroidal endothelial cells. Microvasc. Res. 62 (2001) 179-189
    • (2001) Microvasc. Res. , vol.62 , pp. 179-189
    • Uhlmann, S.1    Friedrichs, U.2    Eichler, W.3    Hoffmann, S.4    Wiedemann, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.