medigraphic.com
ISSN 0016-3813 (Print)

2018, Number 2

<< Back Next >>

Gac Med Mex 2018; 154 (2)

Complejos moleculares de la señalización adrenérgica

Alcántara-Hernández R, Hernández-Méndez A

Language: Spanish
References: 69
Page: 223-235
PDF size: 417.19 Kb.


ABSTRACT

Adrenaline and noradrenaline bind to membrane receptors of the superfamily of G protein-coupled receptors (GPCR) in target cells, where they modulate physiological responses such as metabolism, vasoconstriction, vasodilation and proliferation. Alteration in their function is associated with conditions such as hypertension, benign prostatic hyperplasia and cardiac hypertrophy. In response to adrenaline, receptors form signaling complexes, which enables adrenergic action to be specific, rapid and efficient. These signaling complexes or signalosomes are composed of kinases, phosphatases, and adapter and scaffold proteins, which together modulate the receptor function. Manipulation of each protein-protein interaction of the adrenergic signaling complex emerges as a promising therapeutic strategy for the design of drugs that modulate adrenergic action and help to define its pathophysiological significance. An important biological model to perform these investigations is the heart, since it expresses all adrenergic receptors; to date, several heart signalosomes have been described. Mass spectrometry (proteomics), genetic manipulation and biochemical assays, such as two-hybrid and co-immunoprecipitation assays, are tools that are used in these studies.


REFERENCES

  1. Lymperopoulos A, Brill A, McCrink KA. GPCRs of adrenal chromaffin cells and catecholamines: The plot thickens. Int J Biochem Cell Biol. 2016;77(Pt B):213-219.

  2. Cotecchia S. The α1-edrenergic receptors diversity of signaling networks and regulation. J Recept Signal Transduct Res. 2010;30(6):410-419.

  3. Forster C. Agonistas de los adrenorreceptores. En: Kalant H, Roschlau WHE (eds.). Principios de farmacología médica. México: Oxford; 2003.

  4. Forster C. Antagonistas de los adrenorreceptores. En: Kalant H, Roschlau WHE, editores. Principios de farmacología médica. México: Oxford; 2003.

  5. Mitchell J. Transducción de señales y segundos mensajeros. En: Kalant H, Roschlau WHE, editores. Principios de farmacología médica. México: Oxford; 2003.

  6. Mycek MJ, Harvey RA, Champe PC. Agonistas adrenérgicos. En: Harvey RA, Champe PC, editors. Farmacología. México: McGrawHill; 2007.

  7. Mycek MJ, Harvey RA, Champe PC. Antagonistas adrenérgicos. En: Harvey RA, Champe PC, editores. Farmacología. México: McGrawHill; 2007.

  8. García-Sáinz JA. Hormonas: mensajeros químicos y comunicación celular. México: Fondo de Cultura Económica; 2016.

  9. Carniegie KM, Means CK, Scott JD. A-kinase anchoring proteins: from protein complexes to physiology and disease. IUBMB Life. 2009; 61(4):394-406.

  10. Dombrádi V, Krieglstein J, Klumpp S. Regulating the regulators. EMBO Rep. 2002;3(2):120-124.

  11. Groves JT, Kuriyan J. Molecular mechanisms in signal transduction at the membrane. Nat Struct Mol Biol. 2010;17(6):659-665.

  12. Bauman AL, Michel JJ, Henson E, Dodge-Kafka KL, Kapiloff MS. The mAKAP signalosome and cardiac myocyte hypertrophy. IUBMB Life. 2007;59(3):163-169.

  13. Pawson CT, Scott JD. Signal interaction through blending, bolstering and bifurcating of intracellular information. Nat Struct Mol Biol. 2010;17(6):653-658.

  14. Cotecchia S, Stanasila L, Diviani D. Protein-protein interaction at adrenergic receptors. Curr Drug Targets. 2012;13(1):15-27.

  15. Diviani D, Reggi E, Arambasic C, Caso S, Maric D. Emerging roles of A-kinase anchoring proteins in cardiovascular pathophysiology. Biochim Biophys Acta. 2016;18637(7 Pt B):1926-1936.

  16. Malbon CC, Tao J, Wang HY. AKAPs (A-kinase anchoring proteins) and molecules that composes their G-protein-coupled receptor signaling complexes. Biochem J. 2004;379(Pt 1):1-9.

  17. Logue JS, Scott JD. Organizing signal transduction through A-kinase Anchoring proteins (AKAPs). 2010;277(21):4370-4375.

  18. Vázquez-Prado J, Casas-González P, García-Sáinz JA. G protein-coupled receptor cross-talk: pivotal roles of protein phosphorylation and protein-protein interactions. Cell Signal. 2003;15(6) 549-557.

  19. Tao J, Shumay E, McLaughlin S, Wang HY, Malbon CC. Regulation of AKAP-membrane interactions by calcium. J Biol Chem. 2006;281(33):23932-23944.

  20. Perino A, Ghigo A, Scott JD, Hirsch E. Anchoring proteins as regulators of signaling pathways. Circ Res. 2012;111(4):482-492.

  21. Fu Y, Westenbroek RE, Yu FH, Clark JP, Marshall MR, Scheuer T, et al. Deletion of the distal C terminus of Cav1.2 channels leads to loss of b-adrenergic regulation and heart failure in vivo. J Biol Chem. 2011;286(14):12617-12626.

  22. Redden JM, Dodge-Kafka KL. AKAP phosphatases complexes in the heart. J Cardiovasc Pharmacol. 2011;58(4):354-362.

  23. Shi T, Papay RS, Pérez DM. α1A-adrenergic receptor prevents cardiac ischemic damage through PKC/GLUT1/4-mediated glucose uptake. J Recept Signal Transduct Res. 2016;36(3):261-270.

  24. Östman-Smith I. Beta-blockers in pediatric hypertrophic cardiomyopathies. Rev Recent Clin Trials. 2014;9(2):82-85.

  25. Hamada M, lkeda S, Shigematsu Y. Advances in medical treatment of hypertrophic cardiomyopathy. J Cardiol. 2014;64(1):1-10.

  26. DeFilipps EM, Givertz MM. Treating diabetes in pacients with heart failure: moving from risk to benefit. Curr Heart Fail Rep. 2016;13(3):111-118.

  27. Hinson JT, Chopra A, Nafissi N, Polacheck WJ, Benson CC, Swist S, et al. Titin mutations in iPS cells define sarcomere insufficiency as a cause of dilated cardiomyopathy. Science. 2015;349(6251):982-986.

  28. Ahlquist RP. A study of adrenotropic receptors. Am J Physiol. 1948;153(3):586-600.

  29. Sutherland EW, Rall TW. Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J Biol Chem. 1958;232(2):1077-1091.

  30. Galitzky J, Vermorel M, Lafontan M, Mantastruc P, Berlan M. Termogenetic and lipolytic effect of yohimbine in the dog. Br J Pharmacol. 1991; 104(2):514-518.

  31. Alcántara-Hernández R, Casas-González P, García-Sáinz JA. Signal transduction pathway cross-talk. Role of protein kinases, protein phosphatases and reactive oxygen species. Curr Trends Endocrinol. 2005;1:19-30.

  32. García-Sáinz JA. Robert Lefkowitz y Brian Kobilka: premios Nobel 2012. Rev Fac Med UNAM. 2013;56(1) 59-63.

  33. Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, et. al. Crystal structure of the human b2 adrenergic G-protein- coupled receptor. Nature. 2007;450(7168):383-388.

  34. Rasmussen SG, DeVree BT, Zou Y, Kuse AC, Chung KY, Kobilka TS, et al. Crystal structure of the b2 adrenergic receptor-Gs protein complex. Nature. 2011;477(7366):549-555.

  35. Kruse AC, Hu J, Pan AC, Arlow DH, Rosenbaum DM, Rosemond E, et al. Structure and dynamics of the M3 muscarinic acetylcholine receptor. Nature. 2012;482(7386):552-556.

  36. Granier S, Manglik A, Kruse AC, Kobilka TS, Thian FS, Weiss WI, Kobilka BK. Structure of the d-opioid receptor bound to naltrindole. Nature. 2012;485(7398):400-404.

  37. Okada T, Le Trong I, Fox BA, Behnke CA, Stenkamp RE, Palczewski K. X-Ray diffraction analysis of the three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. J Struct Biol. 2000; 130(1):73-80.

  38. Pawson CT, Scott JD. Signal integration blending, bolstering and bifurcating of intracellular information. Nat Struct Mol Biol. 2010;17(6) 653-658

  39. Welch JEJ, Jones BW, Scott JD. Networking with AKAPs: context-dependent regulation of anchored enzymes. Mol Interv. 2010;10(2):86-97.

  40. Zentella-Dehesa A, Alcántara-Hernández R. Importancia de los dominios de interacción proteica en la formación de complejos en los sistemas de transducción. Rev Educ Bioq. 2003;22(3):117-129.

  41. Huber T, Sakmar TP. Escaping the flatlands: new approaches to study dynamic assembly and activation of GPCRs signaling complexes. Trends Pharmacol Sci. 2011;32(7):410-419.

  42. Pawson T. New impressions of Src and Hck. Nature. 1997;385(6617):582-609.

  43. Roskoski R. Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun. 2004;324(4):1155-1164.

  44. Foster-Barber A, Bishop JM. Src interact with dynamin and synapsin in neuronal cells. Proc Natl Acad Sci U S A. 1998;95(8):4673-4677.

  45. Ponting CP, Phillips Ch, Davies KE, Blake DJ. PDZ domains: targeting signaling molecules to sub-membranous sites. Bioessays. 1997;19(6):469-479.

  46. Tao J, Wang H-yu, Malbon CC. Protein kinase A regulates AKAP250 (gravin) scaffold binding to the b2-adrenergic receptor. EMBO J. 2003;22(24):6419-6429.

  47. Lin F, Wang HY, Malbon CC. Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization. J Biol Chem. 2000;275(25):19025-19034.

  48. García-Sáinz JA, Romero-Ávila T, Alcántara-Hernández R. Mechanisms involved in α1B-adrenoceptor desensitization. IUBMB Life. 2011; 63(10):811-815.

  49. Tao J, Wang HY, Malbon CC. Src docks to A-kinase anchoring protein gravin, regulating beta2-adrenergic receptor resensitization and recycling. J Biol Chem. 2007;282(9):6597-6608.

  50. Willoughby D, Wong W, Shaack J, Scott JD, Cooper DM. An anchored PKA and PDE4 complex regulates subplasmalemmal cAMP dynamics. EMBO J. 2006;25(10):2051-2061.

  51. Laporte SA, Oakley RH, Holt JA, Barak LS, Caron MG. The interaction of beta-arrestin with AP-2 adaptor is required for the clustering of beta2- adrenergic receptor into clathrin-coated pits. J Biol Chem. 2000;275(30):23120-23126.

  52. Azzi M, Charest PG, Rousseau G, Kohout T, Bouvier M, Piñeyro G, et al. b-arrestin-mediated activation of MAPK by inverse agonists revels distinct active conformations for G protein-coupled receptors. Proc Natl Acad Sci U S A. 2003;100(20):11406-11411.

  53. Shenoy SK, Xiao K, Weissman AM, Venkataramanan V, Snyder PM, Freedman NJ. Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the b2-adrenergic receptor. J Biol Chem. 2008;283(32):22166-22176.

  54. Wnorowski A, Jozwiak K. Homo- and hetero-oligomerization of b2-adrenergic receptor in receptor trafficking, signaling pathways and receptor pharmacology. Cell Signal. 2014;26(10):2259-2265.

  55. Salahpour A, Angers S, Mercier JF, Lagacé M, Marullo S, Bouvier M. Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting. J Biol Chem. 2004;279(32):33390-33397.

  56. Tam J, Trembovier V, DiMarzo V, Petrosino S, Leo G, Alexandrovich A, et. al. The cannabinoid CB1 receptor regulates bone formation by modulating adrenergic signaling. FASEB J. 2008;22(1):285-294.

  57. Hudson BD, Hébert TE, Kelly ME. Physical and functional interaction between CB1 cannabinoid receptors and beta2-adrenoceptors. Br J Pharmacol. 2010;160(3) 627-642.

  58. Prasanna X, Chattopadhvay A, Sengupta D. Cholesterol modulates the dimer interface of the b2-adrenergic receptor via colesterol occupancy sites. Biophys J. 2014;106(6):1290-1300.

  59. Shukla AK, Westfield GH, Xiao K, Reis RI, Huang LY, Shukla PT, et. al. Visualization of arrestin recruitment by a G protein-coupled receptor. Nature. 2014;512(7513):218-222.

  60. Luttrell LM, Lefkowitz RJ. The role of b-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci. 2002;115(Pt 3):455-465.

  61. Nelson CD, Kovacs JJ, Nobles KN, Whalen EJ, Lefkowitz RJ. Beta-arrestin scaffolding of phosphoinositol 4-phsphate 5-kinase Ialpha promotes agonist-stimulated sequestration of the b2-adrenergic receptor. J Biol Chem. 2008;283(30):21093-21101.

  62. Nobles KN, Xiao K, Ahn S, Shukla AK, Lam ChM, Rajagopal S, et. al. Distinct phosphorylation sites on the b2-adrenergic receptor establish a barcode that encodes differential functions of b-arrestin. Sci Signal. 2011;4(185):ra51.

  63. Shenoy SK, Lefkowitz RJ. b-arrestin-mediated receptor trafficking and signal transduction. Trends Pharmacol Sci. 2011;32(9):521-533.

  64. Tao J, Malbon CC. G-protein-coupled receptor-associated A-kinase anchoring proteins AKAP5 and AKAP12: differential signaling to MAPK and GPCR recycling. J Mol Signal. 2008;3:19.

  65. Gao S, Wang HY, Malbon CC. AKAP12 and AKAP5 form higher-order hetero-oligomers. J Mol Signal. 2011;6:8.

  66. Vanotis G, Del-Duca D, Trieu P, Rohlicek CV, Hébert TE, Allen BG. Nuclear b-adrenergic receptors modulate gene expression in adult rat heart. Cell Signal. 2011;23(1):89-98.

  67. Wright CD, Chen Q, Baye NL, Huang Y, Healy CL, Kasinathan S, et al. Nuclear α1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes. Circ Res. 2008;103(9):992-1000.

  68. Lyssand JS, Whiting JL, Lee K-S, Kastl R, Wacker JL, Bruchas MR, Miyatake M, Langeberg LK, Chavkin Ch, Scott JD, Gardner RG, Adams ME, Hague Ch. α-dystrobrevin-1 recruits α-catulin to the α1D adrenergic receptor/dystrophin-associated protein complex signalosome. Proc Natl Acad Sci U S A. 2010;107(50):21854-21859.

  69. De-La-Torre Russis V, Valles A, Gómez R, Chinea G, Pons T. Interacciones proteína-proteína: bases de datos y métodos teóricos de predicción. Biotecnología Aplicada. 2003;20(3):201-208.




2020     |     www.medigraphic.com