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Life history of eNOS: Partners and pathways
Open accessAbstract
The complex regulation of eNOS (endothelial nitric oxide synthase) in cardiovascular physiology occurs at multiple stages. eNOS mRNA levels are controlled both at the transcriptional and post-transcriptional phases, and epigenetic mechanisms appear to modulate tissue-specific eNOS expression. The eNOS enzyme reversibly associates with a diverse family of protein partners that regulate eNOS sub-cellular localization, catalytic function, and biological activity. eNOS enzyme activity and sub-cellular localization are intimately controlled by post-translational modifications including phosphorylation, nitrosylation, and acylation. The multiple extra-cellular stimuli affecting eNOS function coordinate their efforts through these key modifications to dynamically control eNOS and NO bioactivity in the vessel wall. This review will focus on the biochemical partners and perturbations of the eNOS protein as this vital enzyme undergoes modulation by diverse signal transduction pathways in the vascular endothelium.
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“eNOS (NOS3) generates the lowest levels of NO and was originally discovered in the vascular endothelium but is also found in neurons, epithelial cells, and cardiac myocytes (28).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [28]
In the citing paper
“At the extreme of this spectrum, it is known that for inducible NOS to kill microbes, parasites, or cancer cells, high levels of NO are needed to destroy FeS centers and respiratory proteins in the target organism (28, 31, 32, 46).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [28]
In the citing paper
“NOS3 (commonly called endothelial NOS or eNOS) is expressed to highest relative abundance in the vascular endothelium, but has also been found in neurons, epithelial cells, and cardiomyocytes [66] as well as adipocytes [67, 68] and hepatocytes [69-71].”
From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [66]
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Cites
Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
Dimmeler, S., Fleming, I., Fisslthaler, B., Hermann, C., Busse, R., & Zeiher, A. M. (1999) · Nature · doi:10.1038/21224 · Cited by 3,591
Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
Fulton, D. J., Gratton, J., McCabe, T. J. D., Fontana, J. T., Fujio, Y., Walsh, K. X., Franke, T. F., Papapetropoulos, A., & Sessa, W. C. (1999) · Nature · doi:10.1038/21218 · Cited by 2,616
Caveolin, a protein component of caveolae membrane coats
Rothberg, K. G., Heuser, J. E., Donzell, W. C., Ying, Y., Glenney, J. R., & Anderson, R. G. W. (1992) · Cell · doi:10.1016/0092-8674(92)90143-z · Cited by 2,259
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice
Dráb, M., Verkade, P., Elger, M., Kasper, M. E., Löhn, M., Lauterbach, B., Menne, J., Lindschau, C., Mende, F., Luft, F. C., et al. (2001) · Science · doi:10.1126/science.1062688 · Cited by 1,555
Kureishi, Y., Luo, Z., Shiojima, I., Bialik, A., Fulton, D. J., Lefer, D. J., Sessa, W. C., & Walsh, K. X. (2000) · Nature Medicine · doi:10.1038/79510 · Cited by 1,438
Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
Simoncini, T., Hafezi‐Moghadam, A., Brazil, D. P., Ley, K. F., Chin, W. W., & Liao, J. K. (2000) · Nature · doi:10.1038/35035131 · Cited by 1,436
Steinberg, H. O., Brechtel, G., Johnson, A., Fineberg, N. S., & Baron, A. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117433 · Cited by 1,216
Dynamic activation of endothelial nitric oxide synthase by Hsp90
García‐Cardeña, G., Fan, R., Shah, V. H., Sorrentino, R., Cirino, G., Papapetropoulos, A., & Sessa, W. C. (1998) · Nature · doi:10.1038/33934 · Cited by 1,029
Modulation of Akt kinase activity by binding to Hsp90
Sato, S., Fujita, N., & Tsuruo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170276797 · Cited by 967
Phosphoinositide 3-kinases: A conserved family of signal transducers
Vanhaesebroeck, B., Leevers, S. J., Panayotou, G., & Waterfield, M. D. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01061-x · Cited by 961
Chen, Z., Yuhanna, I. S., Galcheva-Gargova, Z., Karas, R. H., Mendelsohn, M. E., & Shaul, P. W. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5347 · Cited by 924
Du, X. L., Edelstein, D., Dimmeler, S., Ju, Q., Sui, C., & Brownlee, M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11235 · Cited by 907
AMP‐activated protein kinase phosphorylation of endothelial NO synthase
Chen, Z.-P., Mitchelhill, K. I., Michell, B. J., Stapleton, D., Rodríguez‐Crespo, I., Witters, L. A., Power, D. A., de Montellano, P. R. O., & Kemp, B. E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01705-0 · Cited by 839
Acylation Targets Endothelial Nitric-oxide Synthase to Plasmalemmal Caveolae
Shaul, P. W., Smart, E. J., Robinson, L. J., German, Z., Yuhanna, I. S., Ying, Y., Anderson, R. G. W., & Michel, T. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6518 · Cited by 800
Lysophospholipid Receptors: Signaling and Biology
Ishii, I., Fukushima, N., Ye, X., & Chun, J. J. M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073731 · Cited by 771
Fleming, I., Fisslthaler, B., Dimmeler, S., Kemp, B. E., & Busse, R. (2001) · Circulation Research · doi:10.1161/hh1101.092677 · Cited by 770 · cited 1×
“Endothelial eNOS is subject to several overlappingmodes of post-translational regulatory modifications that provide mechanisms for the dynamic stimulation and inhibition of enzymatic activity in response to physiologic and pathophysiologic stimuli.”
BackgroundZeng, G., Nystrom, F. H., Ravichandran, L. V., Cong, L.-N., Kirby, M., Mostowski, H., & Quon, M. J. (2000) · Circulation · doi:10.1161/01.cir.101.13.1539 · Cited by 745
Zeng, G., & Quon, M. J. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118871 · Cited by 726
Nitric oxide and its role in the cardiovascular system
Loscalzo, J., & Welch, G. N. (1995) · Progress in Cardiovascular Diseases · doi:10.1016/s0033-0620(05)80001-5 · Cited by 613
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602
Red blood cells express a functional endothelial nitric oxide synthase
Kleinbongard, P. (2005) · Blood · doi:10.1182/blood-2005-10-3992 · Cited by 575
Michell, B. J., Chen, Z., Tiganis, T., Stapleton, D., Katsis, F., Power, D. A., Sim, A. T. R., & Kemp, B. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100122200 · Cited by 560
Montagnani, M., Chen, H., Barr, V. A., & Quon, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103702200 · Cited by 550
Regulation of Endothelial Nitric Oxide Synthase: Location, Location, Location
Shaul, P. W. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.081501.155952 · Cited by 545
Lysophospholipids--Receptor Revelations
Hla, T., Lee, M.-J., Ancellin, N., Paik, J. H., & Kluk, M. (2001) · Science · doi:10.1126/science.1065323 · Cited by 537
Identification of PSD-95 Palmitoylating Enzymes
Fukata, M., Fukata, Y., Adesnik, H., Nicoll, R. A., & Bredt, D. S. (2004) · Neuron · doi:10.1016/j.neuron.2004.12.005 · Cited by 532
Brown, D. A., & London, E. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7575 · Cited by 517
Caveolin-1 in oncogenic transformation, cancer, and metastasis
Williams, T. M., & Lisanti, M. P. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00458.2004 · Cited by 512
Fulton, D. J., Gratton, J., & Sessa, W. C. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)29198-9 · Cited by 499
He, H., Venema, V. J., Gu, X., Venema, R. C., Marrero, M. B., & Caldwell, R. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.25130 · Cited by 490
Caulin‐Glaser, T., García‐Cardeña, G., Sarrel, P. M., Sessa, W. C., & Bender, J. R. (1997) · Circulation Research · doi:10.1161/01.res.81.5.885 · Cited by 479
Cellular regulation of endothelial nitric oxide synthase
Govers, R., & Rabelink, T. J. (2001) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2001.280.2.f193 · Cited by 476
Role of plasmalemmal caveolae in signal transduction
Shaul, P. W., & Anderson, R. G. W. (1998) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1998.275.5.l843 · Cited by 465
Arthur, H. M., Ure, J. M., Smith, A. J. H., Renforth, G. L., Wilson, D. I., Torsney, E., Charlton, R., Parums, D. V., Jowett, T., Marchuk, D. A., et al. (2000) · Developmental Biology · doi:10.1006/dbio.1999.9534 · Cited by 448
THE REGULATION AND PHARMACOLOGY OF ENDOTHELIAL NITRIC OXIDE SYNTHASE
Dudzinski, D. M., Igarashi, J., Greif, D. M., & Michel, T. M. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121844 · Cited by 425
Ming, X., Viswambharan, H., Barandiér, C., Ruffieux, J., Kaibuchi, K., Rusconi, S., & Yang, Z. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8467-8477.2002 · Cited by 403
McCabe, T. J., Fulton, D., Roman, L. J., & Sessa, W. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6123 · Cited by 387 · cited 1×
“Endothelial eNOS is subject to several overlappingmodes of post-translational regulatory modifications that provide mechanisms for the dynamic stimulation and inhibition of enzymatic activity in response to physiologic and pathophysiologic stimuli.”
BackgroundThe Caveolin genes: from cell biology to medicine
Williams, T. M., & Lisanti, M. P. (2004) · Annals of Medicine · doi:10.1080/07853890410018899 · Cited by 371
Harris, M. B., Ju, H., Venema, V. J., Liang, H., Zou, R., Michell, B. J., Chen, Z.-P., Kemp, B. E., & Venema, R. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100229200 · Cited by 363
The Endothelial Nitric-oxide Synthase-Caveolin Regulatory Cycle
Féron, O., Saldaña, F., Michel, J. B., & Michel, T. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3125 · Cited by 361
Tsujita, K., Suetsugu, S., Sasaki, N., Furutani, M., Oikawa, T., & Takenawa, T. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200508091 · Cited by 360
Protein palmitoylation: a regulator of neuronal development and function
El-Husseini, A., & Bredt, D. S. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn940 · Cited by 341
Fontana, J. T., Fulton, D. J., Chen, Y., Fairchild, T. A., McCabe, T. J. D., Fujita, N., Tsuruo, T., & Sessa, W. C. (2002) · Circulation Research · doi:10.1161/01.res.0000016837.26733.be · Cited by 340
Pritchard, K. A., Ackerman, A. W., Gross, E. R., Stepp, D. W., Shi, Y., Fontana, J. T., Baker, J. E., & Sessa, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100084200 · Cited by 338
Localization of inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae.
Fujimoto, T., Nakade, S., Miyawaki, A., Mikoshiba, K., & Ogawa, K. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.6.1507 · Cited by 338
Martı́nez-Ruiz, A., Villanueva, L., de Orduña, C. G., López‐Ferrer, D., Higueras, M. Á., Tarín, C., Rodríguez‐Crespo, I., Vázquez, J., & Lamas, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407294102 · Cited by 330
Gallis, B. M., Corthals, G. L., Goodlett, D. R., Ueba, H., Kim, F., Presnell, S. R., Figeys, D., Harrison, D. G., Berk, B. C., Aebersold, R. H., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.30101 · Cited by 326
Michel, J. B., Féron, O., Sase, K., Prabhakar, P., & Michel, T. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25907 · Cited by 323
Biogenesis of caveolae: a structural model for caveolin-induced domain formation
Parton, R. G., Hanzal‐Bayer, M., & Hancock, J. F. (2006) · Journal of Cell Science · doi:10.1242/jcs.02853 · Cited by 302
Neuroprotection mediated by changes in the endothelial actin cytoskeleton
Laufs, U., Endres, M., Stagliano, N. E., Amin‐Hanjani, S., Chui, D.-S., Yang, S.-X., Simoncini, T., Yamada, M., Aïkawa, E., Allen, P. G., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9639 · Cited by 279
Cheng, C., van Haperen, R., de Waard, M., van Damme, L. C. A., Tempel, D., Hanemaaijer, L., van Cappellen, G. W. A., Bos, J., Slager, C. J., Duncker, D. J., et al. (2005) · Blood · doi:10.1182/blood-2005-06-2326 · Cited by 274
Ravi, K., Brennan, L., Levic, S., Ross, P. A., & Black, S. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0300464101 · Cited by 268
Hsp90 and Caveolin Are Key Targets for the Proangiogenic Nitric Oxide–Mediated Effects of Statins
Brouet, A., Sonveaux, P., Dessy, C., Moniotte, S., Balligand, J., & Féron, O. (2001) · Circulation Research · doi:10.1161/hh2201.100319 · Cited by 268
Toporsian, M., Gros, R., Kabir, M. G., Vera, S., Govindaraju, K., Eidelman, D. H., Husain, M., & Letarte, M. (2005) · Circulation Research · doi:10.1161/01.res.0000159936.38601.22 · Cited by 249
Conrad, P. A., Smart, E. J., Ying, Y. S., Anderson, R. G. W., & Bloom, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.6.1421 · Cited by 245
Bauer, P. M., Fulton, D. J., Boo, Y. C., Sorescu, G. P., Kemp, B. E., Jo, H., & Sessa, W. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211926200 · Cited by 243
Shear stress stimulates phosphorylation of eNOS at Ser635by a protein kinase A-dependent mechanism
Boo, Y. C., Hwang, J., Sykes, M. C., Michell, B. J., Kemp, B. E., Lum, H., & Jo, H. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00214.2002 · Cited by 240
Crystal Structures of Zinc-free and -bound Heme Domain of Human Inducible Nitric-oxide Synthase
Li, H., Raman, C. S., Glaser, C. B., Blasko, E., Young, T. A., Parkinson, J. F., Whitlow, M. D., & Poulos, T. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21276 · Cited by 240
Lin, M. I., Fulton, D. J., Babbitt, R. W., Fleming, I., Busse, R., Pritchard, K. A., & Sessa, W. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302836200 · Cited by 239
Estradiol induces the calcium-dependent translocation of endothelial nitric oxide synthase
Goetz, R. M., Thatte, H. S., Prabhakar, P., Cho, M., Michel, T. M., & Golan, D. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2788 · Cited by 234
Expression and Characterization of Recombinant Caveolin
Li, S. C., Song, K. S., & Lisanti, M. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.568 · Cited by 223
Narrative Review: Protein Degradation and Human Diseases: The Ubiquitin Connection
Reinstein, E., & Ciechanover, A. J. (2006) · Annals of Internal Medicine · doi:10.7326/0003-4819-145-9-200611070-00010 · Cited by 216
Erwin, P. A., Lin, A. J., Golan, D. E., & Michel, T. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413058200 · Cited by 215
Brouet, A., Sonveaux, P., Dessy, C., Balligand, J., & Féron, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101371200 · Cited by 213
Michell, B. J., Harris, M. B., Chen, Z.-P., Ju, H., Venema, V. J., Blackstone, M. A., Huang, W., Venema, R. C., & Kemp, B. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205144200 · Cited by 212 · cited 2×
“Phosphorylation at Ser 635 is responsive to PKA and increases eNOS activity in response to PKA dependent agonists as well as basal stimuli like shear stress [32,33].”
BackgroundSynergistic Activation of Endothelial Nitric-oxide Synthase (eNOS) by HSP90 and Akt
Takahashi, S., & Mendelsohn, M. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304471200 · Cited by 202
Murga, C., Fukuhara, S., & Gutkind, J. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12069 · Cited by 199
Igarashi, J., Erwin, P. A., Dantas, A. P., Chen, H., & Michel, T. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934494100 · Cited by 192
Dephosphorylation of Endothelial Nitric-oxide Synthase by Vascular Endothelial Growth Factor
Kou, R., Greif, D. M., & Michel, T. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204519200 · Cited by 192
Zimmermann, K., Opitz, N., Dedio, J., Renné, C., Müller‐Esterl, W., & Oess, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252345399 · Cited by 192
NOSIP, a novel modulator of endothelial nitric oxide synthase activity
Dedio, J., KÖNIG, P., Wohlfart, P., Schroeder, C., Kummer, W., & Müller‐Esterl, W. (2001) · The FASEB Journal · doi:10.1096/fj.00-0078com · Cited by 191
Bernier, S. G., Haldar, S. M., & Michel, T. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005116200 · Cited by 190
Endoglin regulates nitric oxide‐dependent vasodilatation
Jerkić, M., Rivas‐Elena, J. V., Prieto, M., Carrón, R., Sanz-Rodrı́guez, F., Pérez‐Barriocanal, F., Rodríguez‐Barbero, A., Bernabéu, C., & López-Novoa, J. M. (2004) · The FASEB Journal · doi:10.1096/fj.03-0197fje · Cited by 185
Regulation of endothelial nitric oxide synthase mRNA, protein, and activity during cell growth
Arnal, J., Yamin, J. J., Dockery, S., & Harrison, D. G. (1994) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1994.267.5.c1381 · Cited by 183
Estrogen Induces Vascular Wall Dilation
Guo, X., Razandi, M., Pedram, A., Kassab, G. S., & Levin, E. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501244200 · Cited by 180
Yeh, D. C., Duncan, J. A., Yamashita, S., & Michel, T. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.33148 · Cited by 178
Fernandez-Hernando, C. F., Fukata, M., Bernatchez, P. N., Fukata, Y., Lin, M. I., Bredt, D. S., & Sessa, W. C. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601051 · Cited by 169
Polikandriotis, J. A., Mazzella, L., Rupnow, H. L., & Hart, C. M. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000177805.65864.d4 · Cited by 168
Eto, M., Barandiér, C., Rathgeb, L., Kozai, T., Joch, H., Yang, Z., & Lüscher, T. F. (2001) · Circulation Research · doi:10.1161/hh1901.097084 · Cited by 168
Caveolins and the regulation of endothelial nitric oxide synthase in the heart
Féron, O., & Balligand, J. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.12.014 · Cited by 163
Agonist-modulated Targeting of the EDG-1 Receptor to Plasmalemmal Caveolae
Igarashi, J., & Michel, T. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003075200 · Cited by 160
Neuronal Nitric-oxide Synthase Is Regulated by the hsp90-based Chaperone System in Vivo
Bender, A. T., Silverstein, A. M., Demady, D. R., Kanelakis, K. C., Noguchi, S., Pratt, W. B., & Osawa, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1472 · Cited by 158
Receptor-regulated Translocation of Endothelial Nitric-oxide Synthase
Prabhakar, P., Thatte, H. S., Goetz, R. M., Cho, M., Golan, D. E., & Michel, T. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.42.27383 · Cited by 156
Dual Effect of Ceramide on Human Endothelial Cells
Li, H., Junk, . C., Huwiler, A., Burkhardt, C., Wallerath, T., Pfeilschifter, J. M., & Förstermann, U. (2002) · Circulation · doi:10.1161/01.cir.0000035650.05921.50 · Cited by 156
Endothelial Ca 2+ waves preferentially originate at specific loci in caveolin-rich cell edges
Isshiki, M., Ando, J., Korenaga, R., Kogo, H., Fujimoto, T., Fujita, T., & Kamiya, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5009 · Cited by 150
Sorensen, L. K., Brooke, B. S., Li, D. Y., & Urness, L. D. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00158-1 · Cited by 150
Do caveolins regulate cells by actions outside of caveolae?
Head, B. P., & Insel, P. A. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.11.008 · Cited by 143
Maniatis, N. A., Brovkovych, V. M., Allen, S. E., John, T. A., Shajahan‐Haq, A. N., Tiruppathì, C., Vogel, S. M., Skidgel, R. A., Malik, A. B., & Minshall, R. D. (2006) · Circulation Research · doi:10.1161/01.res.0000245187.08026.47 · Cited by 141
Sphingosine 1-Phosphate and Isoform-specific Activation of Phosphoinositide 3-Kinase β
Igarashi, J., & Michel, T. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105628200 · Cited by 133
Subcellular Targeting and Differential S-Nitrosylation of Endothelial Nitric-oxide Synthase
Erwin, P. A., Mitchell, D. A., Sartoretto, J. L., Marletta, M. A., & Michel, T. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510421200 · Cited by 122
Regulation of endothelial nitric oxide synthase by the actin cytoskeleton
Su, Y., Edwards-Bennett, S. M., Bubb, M., & Block, E. R. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00248.2002 · Cited by 120
Venema, V. J., Marrero, M. B., & Venema, R. C. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1417 · Cited by 115
Src Kinase Activates Endothelial Nitric-oxide Synthase by Phosphorylating Tyr-83
Fulton, D. J., Church, J. E., Ruan, L., Li, C., Sood, S. G., Kemp, B. E., Jennings, I. G., & Venema, R. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504606200 · Cited by 112
Jiang, J., Cyr, D., Babbitt, R. W., Sessa, W. C., & Patterson, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304738200 · Cited by 110
Duncan, J. A., & Gilman, A. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202505200 · Cited by 105
Greif, D. M., Kou, R., & Michel, T. M. (2002) · Biochemistry · doi:10.1021/bi026732g · Cited by 104
Zhang, Q., Church, J. E., Jagnandan, D., Catravas, J. D., Sessa, W. C., & Fulton, D. J. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000216044.49494.c4 · Cited by 100
Hypoxia increases Hsp90 binding to eNOS via PI3K-Akt in porcine coronary artery endothelium
Chen, J., & Meyrick, B. O. (2003) · Laboratory Investigation · doi:10.1038/labinvest.3700027 · Cited by 99
Gonzalez, E., Kou, R., Lin, A. J., Golan, D. E., & Michel, T. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207299200 · Cited by 96
Salt, I. P., Morrow, V. A., Brandie, F. M., Connell, J., & Petrie, J. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210618200 · Cited by 96
Gonzalez, E., Kou, R., & Michel, T. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510434200 · Cited by 95
Du, X. L., Edelstein, D., Dimmeler, S., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200111235 · Cited by 91
Functional significance of differential eNOS translocation
Sánchez, F. A., Savalia, N. B., Durán, R. G., Lal, B. K., Borić, M. P., & Durán, W. N. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00370.2006 · Cited by 88
Jagnandan, D., Sessa, W. C., & Fulton, D. J. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00162.2005 · Cited by 86
Schilling, K., Opitz, N., Wiesenthal, A., Oess, S., Tikkanen, R., Müller‐Esterl, W., & Icking, A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0709 · Cited by 86
Dreyer, J., Schleicher, M., Tappe‐Theodor, A., Schilling, K., Kuner, T., Kusumawidijaja, G., Müller‐Esterl, W., Oess, S., & Kuner, R. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2265-04.2004 · Cited by 85
Intracellular Coupling via Limiting Calmodulin
Tran, Q., Black, D. J., & Persechini, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300165200 · Cited by 84
Takahashi, S., & Mendelsohn, M. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212651200 · Cited by 80
Proteasome Inhibition Down-regulates Endothelial Nitric-oxide Synthase Phosphorylation and Function
Wei, Q., & Xia, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602105200 · Cited by 79
Posttranscriptional Regulation of Endothelial Nitric Oxide Synthase During Cell Growth
Searles, C. D., Miwa, Y., Harrison, D. G., & Ramasamy, S. (1999) · Circulation Research · doi:10.1161/01.res.85.7.588 · Cited by 78
Church, J. E., & Fulton, D. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505968200 · Cited by 78
Palmitoylation of Caveolin-1 in Endothelial Cells Is Post-translational but Irreversible
Parat, M., & Fox, P. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006722200 · Cited by 78
NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS
Icking, A., Matt, S., Opitz, N., Wiesenthal, A., Müller‐Esterl, W., & Schilling, K. (2005) · Journal of Cell Science · doi:10.1242/jcs.02620 · Cited by 76
Hutcheson, I. R., & Griffith, T. M. (1996) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1996.tb15459.x · Cited by 75
Searles, C. D., Ide, L. M., Davis, M. E., Cai, H. “., & Weber, M. (2004) · Circulation Research · doi:10.1161/01.res.0000138953.21377.80 · Cited by 74
Flowers, M. A., Wang, Y., Stewart, R. J., Patel, B., & Marsden, P. A. (1995) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1995.269.6.h1988 · Cited by 74
de Frutos, T., de Miguel, L. S., Farré, J., Rivas, J. G., Romero, J., Marcos‐Alberca, P., Nuñez, A., Rico, L., & López-Farré, A. J. (2001) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(00)01185-2 · Cited by 71
Xie, Q. W., Leung, M., Fuortes, M. G., Sassa, S., & Nathan, C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4891 · Cited by 71
Chen, P., & Wu, K. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.13155 · Cited by 65
Role of heat shock protein 90 in bradykinin-stimulated endothelial nitric oxide release
Harris, M. B., Ju, H., Venema, V. J., Blackstone, M. A., & Venema, R. C. (2000) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(01)00104-5 · Cited by 61
Cytoskeletal regulation of the l -arginine/NO pathway in pulmonary artery endothelial cells
Zharikov, S. I., Sigova, A. A., Chen, S., Bubb, M., & Block, E. R. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.280.3.l465 · Cited by 58
Calmodulin phosphorylation and modulation of endothelial nitric oxide synthase catalysis
Greif, D. M., Sacks, D. B., & Michel, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306377101 · Cited by 56
Mukhopadhyay, S., Xu, F., & Sehgal, P. B. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00990.2006 · Cited by 55
Prabhakar, P., Cheng, V., & Michel, T. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001952200 · Cited by 49
Schleicher, M., Brundin, F., Groß, S., Müller‐Esterl, W., & Oess, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.8251-8258.2005 · Cited by 47
Wei, Q., & Xia, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413607200 · Cited by 43
Schwartz, E. A., REAVEN, E. P., Topper, J. N., & Tsao, P. S. (2005) · Biochemical Journal · doi:10.1042/bj20041182 · Cited by 41
What's in a name? eNOS and anaphylactic shock
Lowenstein, C. J. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29406 · Cited by 38
Kummer, W., König, P., Dedio, J., & Müller‐Esterl, W. (2002) · Gastroenterology · doi:10.1053/gast.2002.34212 · Cited by 37
Lysophosphatidic Acid and Receptor-Mediated Activation of Endothelial Nitric-Oxide Synthase
Kou, R., Igarashi, J., & Michel, T. M. (2002) · Biochemistry · doi:10.1021/bi016017r · Cited by 36
NOSIP and Its Interacting Protein, eNOS, in the Rat Trachea and Lung
König, P., Dedio, J., Oess, S., Papadakis, T., Fischer, A., Müller‐Esterl, W., & Kummer, W. (2005) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.4a6453.2005 · Cited by 34
N-Ethylmaleimide-sensitive factor: a redox sensor in exocytosis
Lowenstein, C. J., & Tsuda, H. (2006) · Biological Chemistry · doi:10.1515/bc.2006.173 · Cited by 30
Friedman, A. D., Nimbalkar, D., & Quelle, F. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210039200 · Cited by 27
Xiang, W., Chen, H., Xu, X., Zhang, M., & Jiang, R. (2005) · International Journal of Gynecology & Obstetrics · doi:10.1016/j.ijgo.2004.12.041 · Cited by 27
Jobin, C. M., Chen, H., Lin, A. J., Yacono, P. W., Igarashi, J., Michel, T. M., & Golan, D. E. (2003) · Biochemistry · doi:10.1021/bi035066w · Cited by 24
Statin-Mediated Inhibition of Rho
Brandes, R. P. (2005) · Circulation Research · doi:10.1161/01.res.0000168040.70096.2a · Cited by 20
FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN
Icking, A., Schilling, K., Wiesenthal, A., Opitz, N., & Müller‐Esterl, W. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.078 · Cited by 19
Choi, Y., Cho, S., Kim, H.-W., Kim, J.-A., Bae, S., & Park, S. S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.079 · Cited by 18
Proliferation of regulatory mechanisms for eNOS: an emerging role for the cytoskeleton
Skidgel, R. A. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00045.2002 · Cited by 17
Harris, M. B., Bartoli, M., Sood, S. G., Matts, R. L., & Venema, R. C. (2006) · Circulation Research · doi:10.1161/01.res.0000203564.54250.0b · Cited by 16
Chen, Z., Yuhanna, I. S., Galcheva-Gargova, Z., Karas, R. H., Mendelsohn, M. E., & Shaul, P. W. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5347e1 · Cited by 12
Hypoxia increases Hsp90 binding to eNOS via PI3K-Akt in porcine coronary artery endothelium
Chen, J., & Meyrick, B. O. (2003) · Laboratory Investigation · doi:10.1038/sj.labinvest.3700027 · Cited by 8
Babbitt, R. W., Sessa, W. C., Cyr, D., et al. (2021) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/75r0-gb68 · Cited by 4
Research works printed but not linked: 3
- Dudzinski DM, Michel T. The vascular biology of nitric oxide and nitric oxide synthases. In: Colman RW, George JN, Goldhaber SZ, Marder VJ, Clowes AW, editors. Hemostasis and thrombosis: basic principles and clinical practice. 5th ed. Philadelphia: Lippincott Williams & Wilkins; 2005. p. 653-66.
- Montagnani M, Chen H, Barr VA, Quon MJ. Insulin-stimulated activation of eNOS in independent of Ca 2+ but requires phosphor- ylation by Akt at Ser 1179 . J Biol Chem 2001;276:30392-8.
- Toporsian M, Gros R, Kabir MG, Vera S, Govindaraju K, Eidelman DH, et al. A role for endoglin in coupling eNOS activity and regulating vascular tone revealed in hereditary hemorrhagic telangi- ectasia. Circ Res 2005;96:684-92.
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Metadata
- Authors
- DUDZINSKI, D., & MICHEL, T.
- Affiliations
- Harvard University (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- MICHEL, T
- Venue
- Cardiovascular Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-07-15
- Volume
- 75
- Issue
- 2
- Pages
- 247-260
- ISSN
- 0008-6363 (ISSN-L)
- PMC
- PMC2682334
- OpenAlex
- W2129195977
- Cited by
- 400
- References
- 143
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 9 · 2023: 11 · 2022: 15 · 2021: 13 · 2020: 5 · 2019: 10 · 2018: 19 · 2017: 19 · 2016: 23 · 2015: 17 · 2014: 40 · 2013: 30 · 2012: 42
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cardiovascular Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL046457, P01HL048743)
- National Institute of General Medical Sciences (R01GM036259)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Health and Disease Prevention
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Keywords
- endothelial nitric oxide synthase, nitric oxide, post-translational modification, phosphorylation, nitrosylation, acylation, subcellular localization, epigenetic regulation, transcriptional regulation, post-transcriptional regulation, signal transduction, vascular endothelium, cardiovascular physiology
- MeSH terms
- Acetylation, Animals, Endothelium, Vascular, Humans, Nitric Oxide, Phosphorylation, Protein Processing, Post-Translational, Signal Transduction, Nitrosation, Nitric Oxide Synthase Type III
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