메뉴 건너뛰기




Volumn 285, Issue 2 54-2, 2003, Pages

Novel complexes of guanylate cyclase with heat shock protein 90 and nitric oxide synthase

Author keywords

Bradykinin; cGMP accumulation; Endothelium; Smooth muscle cells; Vascular endothelial growth factor

Indexed keywords

CYCLIC GMP; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GELDANAMYCIN; GLUTATHIONE TRANSFERASE; GUANYLATE CYCLASE; HEAT SHOCK PROTEIN 90; HYBRID PROTEIN; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PEROXYNITRITE; SOLUBLE GUANYLATE CYCLASE; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 0037962212     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.01025.2002     Document Type: Article
Times cited : (110)

References (30)
  • 1
    • 0033567065 scopus 로고    scopus 로고
    • Enzymatic function of nitric oxide synthases
    • Andrew PJ and Mayer B. Enzymatic function of nitric oxide synthases. Cardiovasc Res 43: 521-531, 1999.
    • (1999) Cardiovasc Res , vol.43 , pp. 521-531
    • Andrew, P.J.1    Mayer, B.2
  • 2
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, and Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 277: 39858-39866, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 3
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide superoxide and peroxynitrite: The good, the bad, and ugly
    • Beckman JS and Koppenod WH. Nitric oxide superoxide and peroxynitrite: the good, the bad, and ugly. Am J Physiol Cell Physiol 271: C1424-C1437, 1996.
    • (1996) Am J Physiol Cell Physiol , vol.271
    • Beckman, J.S.1    Koppenod, W.H.2
  • 4
    • 0034680878 scopus 로고    scopus 로고
    • Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein
    • Bell DR and Poland A. Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein. J Biol Chem 275: 36407-36414, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 36407-36414
    • Bell, D.R.1    Poland, A.2
  • 6
    • 0035957984 scopus 로고    scopus 로고
    • Direct interaction between endothelial nitric-oxide synthase and dynamin-2
    • Cao S, Yao J, McCabe TJ, Yao Q, Katusic ZS, Sessa WC, and Shah V. Direct interaction between endothelial nitric-oxide synthase and dynamin-2. J Biol Chem 276: 14249-14256, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 14249-14256
    • Cao, S.1    Yao, J.2    McCabe, T.J.3    Yao, Q.4    Katusic, Z.S.5    Sessa, W.C.6    Shah, V.7
  • 8
    • 0037067712 scopus 로고    scopus 로고
    • Geldanamycin leads to superoxide formation and non-enzymatic redox cycling: Implications for studies of Hsp90 and eNOS
    • Dikalov S, Landmesser U, and Harrison DG. Geldanamycin leads to superoxide formation and non-enzymatic redox cycling: implications for studies of Hsp90 and eNOS. J Biol Chem 277: 25480-25485, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 25480-25485
    • Dikalov, S.1    Landmesser, U.2    Harrison, D.G.3
  • 9
    • 0032488818 scopus 로고    scopus 로고
    • The endothelial nitric-oxide synthase caveolin regulatory cycle
    • Feron O, Saldana F, Michel JB, and Michel T. The endothelial nitric-oxide synthase caveolin regulatory cycle. J Biol Chem 273: 3125-3128, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 3125-3128
    • Feron, O.1    Saldana, F.2    Michel, J.B.3    Michel, T.4
  • 10
    • 0037013152 scopus 로고    scopus 로고
    • Domain mapping studies reveal that the M domain of Hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release
    • Fontana J, Fulton D, Chen Y, Fairchild TA, McCabe TJ, Fujita N, Tsuruo T, and Sessa WC. Domain mapping studies reveal that the M domain of Hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release. Circ Res 90: 866-873, 2002.
    • (2002) Circ Res , vol.90 , pp. 866-873
    • Fontana, J.1    Fulton, D.2    Chen, Y.3    Fairchild, T.A.4    McCabe, T.J.5    Fujita, N.6    Tsuruo, T.7    Sessa, W.C.8
  • 11
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni JV and Neel BG. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal Biochem 210: 179-187, 1993.
    • (1993) Anal Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 13
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the NOS caveolin binding domain in vivo
    • Garcia-Cardeña G, Martasek P, Masters BSS, Skidd PM, Couet J, Li S, Lisanti MP, and Sessa WC. Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: functional significance of the NOS caveolin binding domain in vivo. J Biol Chem 272: 25437-25440, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 25437-25440
    • Garcia-Cardeña, G.1    Martasek, P.2    Masters, B.S.S.3    Skidd, P.M.4    Couet, J.5    Li, S.6    Lisanti, M.P.7    Sessa, W.C.8
  • 15
    • 0022640297 scopus 로고
    • Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor
    • Gryglewski RJ, Palmer RMJ, and Moncada S. Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor. Nature 320: 454-456, 1986.
    • (1986) Nature , vol.320 , pp. 454-456
    • Gryglewski, R.J.1    Palmer, R.M.J.2    Moncada, S.3
  • 16
    • 0024706628 scopus 로고
    • Biological actions and properties of endothelium-derived nitric oxide formed and released from artery and vein
    • Ignarro LJ. Biological actions and properties of endothelium-derived nitric oxide formed and released from artery and vein. Circ Res 65: 1-21, 1989.
    • (1989) Circ Res , vol.65 , pp. 1-21
    • Ignarro, L.J.1
  • 18
    • 0032508575 scopus 로고    scopus 로고
    • Inhibitory interactions of the bradykinin B2 receptor with endothelial nitric-oxide synthase
    • Ju H, Venema VJ, Marrero MB, and Venema RC. Inhibitory interactions of the bradykinin B2 receptor with endothelial nitric-oxide synthase. J Biol Chem 273: 24025-24029, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 24025-24029
    • Ju, H.1    Venema, V.J.2    Marrero, M.B.3    Venema, R.C.4
  • 19
    • 0030853953 scopus 로고    scopus 로고
    • Direct interaction of endothelial nitric oxide synthase and caveolin-I inhibits synthase activity
    • Ju H, Zou R, Venema VJ, and Venema RC. Direct interaction of endothelial nitric oxide synthase and caveolin-I inhibits synthase activity. J Biol Chem 272: 18522-18525, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 18522-18525
    • Ju, H.1    Zou, R.2    Venema, V.J.3    Venema, R.C.4
  • 20
    • 0034009135 scopus 로고    scopus 로고
    • Protein-protein interactions controlling nitric oxide synthases
    • Kone BC. Protein-protein interactions controlling nitric oxide synthases. Acta Physiol Scand 168: 27-31, 2000.
    • (2000) Acta Physiol Scand , vol.168 , pp. 27-31
    • Kone, B.C.1
  • 25
    • 0032512822 scopus 로고    scopus 로고
    • Nitric oxide is an upstream signal of vascular endothelial growth factor-induced extracellular signal-regulated kinase 1/2 activation in postcapillary endothelium
    • Parenti A, Morbidelli L, Cui XL, Douglas JG, Hood JD, Granger HJ, Ledda F, and Ziche M. Nitric oxide is an upstream signal of vascular endothelial growth factor-induced extracellular signal-regulated kinase 1/2 activation in postcapillary endothelium. J Biol Chem 273: 4220-4226, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 4220-4226
    • Parenti, A.1    Morbidelli, L.2    Cui, X.L.3    Douglas, J.G.4    Hood, J.D.5    Granger, H.J.6    Ledda, F.7    Ziche, M.8
  • 26
    • 0034681429 scopus 로고    scopus 로고
    • Estrogen stimulates heat shock protein 90 binding to endothelial nitric oxide synthase in human vascular endothelial cells: Effects on calcium sensitivity and NO release
    • Russell KS, Haynes MP, Caulin-Glaser T, Rosneck J, Sessa WC, and Bender JR. Estrogen stimulates heat shock protein 90 binding to endothelial nitric oxide synthase in human vascular endothelial cells: effects on calcium sensitivity and NO release. J Biol Chem 275: 5026-5030, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 5026-5030
    • Russell, K.S.1    Haynes, M.P.2    Caulin-Glaser, T.3    Rosneck, J.4    Sessa, W.C.5    Bender, J.R.6
  • 28
    • 0031054517 scopus 로고    scopus 로고
    • The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
    • Stancato LF, Silverstein AM, Owens-Grillo JX, Chow YH, Jove R, and Pratt WB. The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase. J Biol Chem 272: 4013-4020, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 4013-4020
    • Stancato, L.F.1    Silverstein, A.M.2    Owens-Grillo, J.X.3    Chow, Y.H.4    Jove, R.5    Pratt, W.B.6
  • 29
    • 0029003452 scopus 로고
    • Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase
    • Venema RC, Sayegh HS, Arnal JF, and Harrison DG. Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase. J Biol Chem 270: 14705-14711, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 14705-14711
    • Venema, R.C.1    Sayegh, H.S.2    Arnal, J.F.3    Harrison, D.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.