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1
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0030222108
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Caveolae and caveolins
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1 Parton RG. Caveolae and caveolins. Curr Opin Cell Biol 1996; 8:542-548.
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(1996)
Curr Opin Cell Biol
, vol.8
, pp. 542-548
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Parton, R.G.1
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2
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0342506499
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Molecular and cellular biology of caveolae
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2 Couet J, Li S, Okamoto T, Scherer PE, Lisanti MP. Molecular and cellular biology of caveolae. Trends Cardiovasc Med 1997; 4:103-110.
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(1997)
Trends Cardiovasc Med
, vol.4
, pp. 103-110
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Couet, J.1
Li, S.2
Okamoto, T.3
Scherer, P.E.4
Lisanti, M.P.5
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3
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0032489443
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Caveolin, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane
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This review article proposes some interesting nomenclature terms such as 'caveolae-related domains' and 'precaveolae', to describe cholesterol-rich detergent-resistant membranes lacking caveolin in their mature and pre-mature forms, respectively
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3 Okamoto T, Schlegel A, Scherer P, Lisanti MP. Caveolin, a family of scaffolding proteins for organizing 'preassembled signaling complexes' at the plasma membrane. J Biol Chem 1998; 273:5419-5422. This review article proposes some interesting nomenclature terms such as 'caveolae-related domains' and 'precaveolae', to describe cholesterol-rich detergent-resistant membranes lacking caveolin in their mature and pre-mature forms, respectively.
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(1998)
J Biol Chem
, vol.273
, pp. 5419-5422
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Okamoto, T.1
Schlegel, A.2
Scherer, P.3
Lisanti, M.P.4
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4
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0029664995
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Acylation targets endotheliat nitric-oxide synthase to plasmalemmal caveolae
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4 Shaul PW, Smart EJ, Robinson LJ, German Z, Yuhanna IS, Ying Y, et al. Acylation targets endotheliat nitric-oxide synthase to plasmalemmal caveolae. J Biol Chem 1996; 271:6518-6522.
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(1996)
J Biol Chem
, vol.271
, pp. 6518-6522
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Shaul, P.W.1
Smart, E.J.2
Robinson, L.J.3
German, Z.4
Yuhanna, I.S.5
Ying, Y.6
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5
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0029787241
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Endothelial nitric-oxide synthase targeting to caveolae: Specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells
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5 Feron O, Belhassen L, Kobzik L, Smith TW, Kelly RA, Michel T. Endothelial nitric-oxide synthase targeting to caveolae: specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells. J Biol Chem 1996; 271:22810-22814.
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(1996)
J Biol Chem
, vol.271
, pp. 22810-22814
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Feron, O.1
Belhassen, L.2
Kobzik, L.3
Smith, T.W.4
Kelly, R.A.5
Michel, T.6
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6
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0030953208
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2+-calmodulin and caveolin
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The original article describing the inhibitory effect of caveolin on eNOS activity and its reversal by calmodulin
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2+-calmodulin and caveolin. J Biol Chem 1997; 272:15583-15586. The original article describing the inhibitory effect of caveolin on eNOS activity and its reversal by calmodulin.
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(1997)
J Biol Chem
, vol.272
, pp. 15583-15586
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Michel, J.B.1
Feron, O.2
Sacks, D.3
Michel, T.4
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7
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0030853953
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Direct interaction of endothelial nitric-oxide synthase and caveolin-1 inhibits synthase activity
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7 Ju H, Zou R, Venema VJ, Venema RC. Direct interaction of endothelial nitric-oxide synthase and caveolin-1 inhibits synthase activity. J Biol Chem 1997; 272:18522-18525.
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(1997)
J Biol Chem
, vol.272
, pp. 18522-18525
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Ju, H.1
Zou, R.2
Venema, V.J.3
Venema, R.C.4
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8
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0030770629
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Caveolin versus calmodulin: Counterbalancing allosteric modulators of nitric oxide synthase
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This article established by enzyme kinetic analyses that the caveolin scaffolding domain specifically mediates the inhibitory interaction with eNOS by acting as a competitive inhibitor of calmodulin; importantly, the authors have designed a useful scrambled caveolin peptide to use as a control in the experiments performed with the original caveolin-derived peptide
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8 Michel JB, Feron O, Sase K, Prabhakar P, Michel T. Caveolin versus calmodulin: counterbalancing allosteric modulators of nitric oxide synthase. J Biol Chem 1997; 272:25907-25912. This article established by enzyme kinetic analyses that the caveolin scaffolding domain specifically mediates the inhibitory interaction with eNOS by acting as a competitive inhibitor of calmodulin; importantly, the authors have designed a useful scrambled caveolin peptide to use as a control in the experiments performed with the original caveolin-derived peptide.
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(1997)
J Biol Chem
, vol.272
, pp. 25907-25912
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Michel, J.B.1
Feron, O.2
Sase, K.3
Prabhakar, P.4
Michel, T.5
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9
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0039397709
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Dissecting the interaction between nitric oxide synthase and caveolin
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These authors identify by site-directed mutagenesis the consensus caveolin binding motif in the oxygenase domain of eNOS as the site of the inhibitory interaction with the structural protein of caveolae
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9 Garcia-Cardena G, Martasek P, Siler Masters BS, Skidd PM, Couet J, Li S, et al. Dissecting the interaction between nitric oxide synthase and caveolin. J Biol Chem 1997; 272:25437-25440. These authors identify by site-directed mutagenesis the consensus caveolin binding motif in the oxygenase domain of eNOS as the site of the inhibitory interaction with the structural protein of caveolae.
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(1997)
J Biol Chem
, vol.272
, pp. 25437-25440
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Garcia-Cardena, G.1
Martasek, P.2
Siler Masters, B.S.3
Skidd, P.M.4
Couet, J.5
Li, S.6
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10
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0032488594
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Dynamic regulation of endothelial nitric oxide synthase: Complementary roles of dual acylation and caveolin interactions
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Acylation-deficient and various truncated eNOS mutants are used to demonstrate that caveolin acts as a chaperone regulating eNOS activation independently of the residence of the enzyme within the caveolae or its state of acylation; also discussed are the differential effects of detergents on the caveolin-eNOS heterocomplex
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10 Feron O, Michel JB, Sase K, Michel T. Dynamic regulation of endothelial nitric oxide synthase: complementary roles of dual acylation and caveolin interactions. Biochemistry 1998; 37:193-200. Acylation-deficient and various truncated eNOS mutants are used to demonstrate that caveolin acts as a chaperone regulating eNOS activation independently of the residence of the enzyme within the caveolae or its state of acylation; also discussed are the differential effects of detergents on the caveolin-eNOS heterocomplex.
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(1998)
Biochemistry
, vol.37
, pp. 193-200
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Feron, O.1
Michel, J.B.2
Sase, K.3
Michel, T.4
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11
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0032575496
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Interaction between caveolin-1 and the reductase domain of endothelial nitric oxide synthase
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These authors report that the interaction of caveolin with the reductase domain of eNOS is necessary and sufficient to compromise its ability to bind calmodulin and to transfer electrons to the oxygenase domain
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11 Ghosh S, Gachhui R, Crooks C, Wu C, Lisanti MP, Stuehr DJ. Interaction between caveolin-1 and the reductase domain of endothelial nitric oxide synthase. J Biol Chem 1998; 273:22267-22271. These authors report that the interaction of caveolin with the reductase domain of eNOS is necessary and sufficient to compromise its ability to bind calmodulin and to transfer electrons to the oxygenase domain.
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(1998)
J Biol Chem
, vol.273
, pp. 22267-22271
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Ghosh, S.1
Gachhui, R.2
Crooks, C.3
Wu, C.4
Lisanti, M.P.5
Stuehr, D.J.6
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12
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0031017769
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Expression and regulation of endothelial nitric oxide synthase
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12 Sase K, Michel T. Expression and regulation of endothelial nitric oxide synthase. Trends Cardiovasc Med 1997; 7:25-34.
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(1997)
Trends Cardiovasc Med
, vol.7
, pp. 25-34
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Sase, K.1
Michel, T.2
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13
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0031452440
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A caveolar complex between the cationic amino acid transporter 1 and endothelial nitric oxide synthase may explain the'arginine paradox'
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This paper documents how the caveolar location of the arginine transporter provides a mechanism for the directed delivery of substrate to eNOS and thus explains why, despite the apparent saturating intracellular arginine concentration for eNOS, exposure to extracellular arginine can increase NO production
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13 McDonald KK, Zharikov S, Block ER, Kilberg MS. A caveolar complex between the cationic amino acid transporter 1 and endothelial nitric oxide synthase may explain the'arginine paradox'. J Biol Chem 1997; 272:31213-31216. This paper documents how the caveolar location of the arginine transporter provides a mechanism for the directed delivery of substrate to eNOS and thus explains why, despite the apparent saturating intracellular arginine concentration for eNOS, exposure to extracellular arginine can increase NO production.
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(1997)
J Biol Chem
, vol.272
, pp. 31213-31216
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McDonald, K.K.1
Zharikov, S.2
Block, E.R.3
Kilberg, M.S.4
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14
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0032488818
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The endothelial nitric oxide synthase-caveolin regulatory cycle
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This article studies the relationship between intracellular calcium regulation and the dynamics of the eNOS-caveolin interaction in intact endothelial cells. These authors also clearly document the role played by eNOS palmitoylation in the reversible caveolar targeting of eNOS after muscarinic cholinergic stimulation
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14 Feron O, Saldana F, Michel JB, Michel T. The endothelial nitric oxide synthase-caveolin regulatory cycle. J Biol Chem 1998; 273:3125-3128. This article studies the relationship between intracellular calcium regulation and the dynamics of the eNOS-caveolin interaction in intact endothelial cells. These authors also clearly document the role played by eNOS palmitoylation in the reversible caveolar targeting of eNOS after muscarinic cholinergic stimulation.
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(1998)
J Biol Chem
, vol.273
, pp. 3125-3128
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Feron, O.1
Saldana, F.2
Michel, J.B.3
Michel, T.4
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15
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0030711558
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Nitric oxide synthases: Which, where, how and why?
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This review article summarizes the known post-translational modifications of eNOS in a model that integrates the cycle of activation and deactivation of the enzyme after agonist stimulation
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15 Michel T, Feron O. Nitric oxide synthases: which, where, how and why? J Clin Invest 1997; 100:2146-2152. This review article summarizes the known post-translational modifications of eNOS in a model that integrates the cycle of activation and deactivation of the enzyme after agonist stimulation.
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(1997)
J Clin Invest
, vol.100
, pp. 2146-2152
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Michel, T.1
Feron, O.2
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16
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0029914567
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Intracellular pH and tyrosine phosphorylation but not calcium determine shear stress-induced nitric oxide production in native endothelial cells
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16 Ayajiki K, Kindermann M, Hecker M, Fleming I, Busse R. Intracellular pH and tyrosine phosphorylation but not calcium determine shear stress-induced nitric oxide production in native endothelial cells. Circ Res 1996; 78:750-758.
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(1996)
Circ Res
, vol.78
, pp. 750-758
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Ayajiki, K.1
Kindermann, M.2
Hecker, M.3
Fleming, I.4
Busse, R.5
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17
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0029987385
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Phosphorylation of endothelial nitric oxide synthase in response to fluid shear stress
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17 Corson MA, James NL, Latta SE, Nerem RM, Berk BC, Harrison DG. Phosphorylation of endothelial nitric oxide synthase in response to fluid shear stress. Circ Res 1996; 79:984-991.
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(1996)
Circ Res
, vol.79
, pp. 984-991
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Corson, M.A.1
James, N.L.2
Latta, S.E.3
Nerem, R.M.4
Berk, B.C.5
Harrison, D.G.6
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18
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0032489676
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2+-independent activation of the endothelial nitric oxide synthase in response to tyrosine phosphatase inhibitors and fluid shear stress
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This study compares the effects of a protein tyrosine phosphatase inhibitor and fluid shear stress on NO-mediated relaxation of isolated carotid arteries as well as on the phosphorylation and compartmentation of eNOS and cytoskeleton-associated proteins
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2+-independent activation of the endothelial nitric oxide synthase in response to tyrosine phosphatase inhibitors and fluid shear stress. Circ Res 1998; 82:686-695. This study compares the effects of a protein tyrosine phosphatase inhibitor and fluid shear stress on NO-mediated relaxation of isolated carotid arteries as well as on the phosphorylation and compartmentation of eNOS and cytoskeleton-associated proteins.
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(1998)
Circ Res
, vol.82
, pp. 686-695
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Fleming, I.1
Bauersachs, J.2
Fisslthaler, B.3
Busse, R.4
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19
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0030600392
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Bradykinin-stimulated tyrosine phosphorylation promotes endothelial nitric oxide synthase translocation to the cytoskeleton
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19 Venema VJ, Marrero MB, Venema RC. Bradykinin-stimulated tyrosine phosphorylation promotes endothelial nitric oxide synthase translocation to the cytoskeleton. Biochem Biophys Res Commun 1996; 226:703-710.
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(1996)
Biochem Biophys Res Commun
, vol.226
, pp. 703-710
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Venema, V.J.1
Marrero, M.B.2
Venema, R.C.3
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20
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0029910141
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Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1
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20 Garcia-Cardena G, Fan R, Stern DF, Liu J, Sessa WC. Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1. J Biol Chem 1996; 271:27237-27240.
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(1996)
J Biol Chem
, vol.271
, pp. 27237-27240
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Garcia-Cardena, G.1
Fan, R.2
Stern, D.F.3
Liu, J.4
Sessa, W.C.5
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21
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0009621605
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Dynamic activation of endothelial nitric oxide synthase by Hsp90
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These authors document the agonist-and shear stress-induced formation of a heterocomplex between eNOS and Hsp90 in endothelial cells; they also present evidence for an involvement of Hsp90 in regulating the NO-dependent agonist-induced relaxation of isolated rat aorta using geldanamycin, a potentially specific inhibitor of the ATP-binding site of Hsp90
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21 Garcia-Cardena G, Fan R, Shah V, Sorrentino R, Cirino G, Papapetropoulos A, Sessa WC. Dynamic activation of endothelial nitric oxide synthase by Hsp90. Nature 1998; 392:821-824. These authors document the agonist-and shear stress-induced formation of a heterocomplex between eNOS and Hsp90 in endothelial cells; they also present evidence for an involvement of Hsp90 in regulating the NO-dependent agonist-induced relaxation of isolated rat aorta using geldanamycin, a potentially specific inhibitor of the ATP-binding site of Hsp90.
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(1998)
Nature
, vol.392
, pp. 821-824
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Garcia-Cardena, G.1
Fan, R.2
Shah, V.3
Sorrentino, R.4
Cirino, G.5
Papapetropoulos, A.6
Sessa, W.C.7
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22
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0032515154
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Modulations of the eNOS-cavelin interactions in cardiac monocytes: Implications for the autonomic regulation of heart rate
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22 Feron O, Dessy C, Opel DJ, Arstall MA, Kelly RA, Michel T. Modulations of the eNOS-cavelin interactions in cardiac monocytes: implications for the autonomic regulation of heart rate. J Biol Chem 1998; 273:30249-30254.
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(1998)
J Biol Chem
, vol.273
, pp. 30249-30254
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Feron, O.1
Dessy, C.2
Opel, D.J.3
Arstall, M.A.4
Kelly, R.A.5
Michel, T.6
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23
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0032538559
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Receptor-regulated translocation of endothelial nitric oxide synthase
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2+-dependent regulation of the subcellular distribution of eNOS in endothelial cells. These results confirm 'the eNOS-caveolin regulatory cycle paradigm' by establishing that the eNOS targeting to caveolae is labile and subject to receptor-regulated reversible translocation to perinuclear structures in the cell cytosol
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2+-dependent regulation of the subcellular distribution of eNOS in endothelial cells. These results confirm 'the eNOS-caveolin regulatory cycle paradigm' by establishing that the eNOS targeting to caveolae is labile and subject to receptor-regulated reversible translocation to perinuclear structures in the cell cytosol.
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(1998)
J Biol Chem
, vol.273
, pp. 27383-27388
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Prabhakar, P.1
Thatte, H.S.2
Goetz, R.M.3
Cho, M.R.4
Golan, D.5
Michel, T.6
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