Artículo

Musikant, D.; Ferri, G.; Durante, I.M.; Buscaglia, C.A.; Altschuler, D.L.; Edreira, M.M."Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi" (2017) Molecular and Biochemical Parasitology. 211:67-70
El editor solo permite la decarga de la versión post-print. Si usted posee dicha versión, enviela a
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Mechanistic details of the modulation by cAMP of Trypanosoma cruzi host cell invasion remain ill-defined. Here we report that activation of host's Epac1 stimulated invasion, whereas specific pharmacological inhibition or maneuvers that alter Epac1 subcellular localization significantly reduced invasion. Furthermore, while specific activation of host cell PKA showed no effect, its inhibition resulted in an increased invasion, revealing a crosstalk between the PKA and Epac signaling pathways during the process of invasion. Therefore, our data suggests that subcellular localization of Epac might be playing an important role during invasion and that specific activation of the host cell cAMP/Epac1 pathway is required for cAMP-mediated invasion. © 2016 Elsevier B.V.

Registro:

Documento: Artículo
Título:Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi
Autor:Musikant, D.; Ferri, G.; Durante, I.M.; Buscaglia, C.A.; Altschuler, D.L.; Edreira, M.M.
Filiación:IQUIBICEN-CONICET-Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad de Buenos Aires, Argentina
Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús, UNSAM-CONICET, Buenos Aires, Argentina
Department of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA, United States
Palabras clave:cAMP; Epac; Invasion; PKA; Trypanosoma cruzi; cyclic AMP; cyclic AMP dependent protein kinase; Epac1 protein; protozoal protein; unclassified drug; cyclic AMP; Epac-1 protein, rat; guanine nucleotide exchange factor; Article; cellular distribution; host cell; nonhuman; priority journal; protein localization; protein synthesis; signal transduction; Trypanosoma cruzi; animal; cell culture; host parasite interaction; metabolism; pathogenicity; physiology; protein transport; rat; Trypanosoma cruzi; Animals; Cells, Cultured; Cyclic AMP; Cyclic AMP-Dependent Protein Kinases; Guanine Nucleotide Exchange Factors; Host-Parasite Interactions; Protein Transport; Rats; Signal Transduction; Trypanosoma cruzi
Año:2017
Volumen:211
Página de inicio:67
Página de fin:70
DOI: http://dx.doi.org/10.1016/j.molbiopara.2016.10.003
Handle:http://hdl.handle.net/20.500.12110/paper_01666851_v211_n_p67_Musikant
Título revista:Molecular and Biochemical Parasitology
Título revista abreviado:Mol. Biochem. Parasitol.
ISSN:01666851
CODEN:MBIPD
CAS:cyclic AMP, 60-92-4; cyclic AMP dependent protein kinase; Cyclic AMP; Cyclic AMP-Dependent Protein Kinases; Epac-1 protein, rat; Guanine Nucleotide Exchange Factors
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v211_n_p67_Musikant

Referencias:

  • Lee, B.Y., Bacon, K.M., Bottazzi, M.E., Hotez, P.J., Global economic burden of chagas disease: a computational simulation model (2013) Lancet Infect. Dis., 13 (4), pp. 342-348
  • Andrews, N.W., Lysosome recruitment during host cell invasion by Trypanosoma cruzi (1995) Trends Cell Biol., 5 (3), pp. 133-137
  • Rodriguez, A., Martinez, I., Chung, A., Berlot, C.H., Andrews, N.W., cAMP regulates Ca2+-dependent exocytosis of lysosomes and lysosome-mediated cell invasion by trypanosomes (1999) J. Biol. Chem., 274 (24), pp. 16754-16759
  • Seino, S., Shibasaki, T., PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis (2005) Physiol. Rev., 85 (4), pp. 1303-1342
  • Pizon, V., Desjardins, M., Bucci, C., Parton, R.G., Zerial, M., Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the golgi complex (1994) J. Cell Sci., 107, pp. 1661-1670
  • Branham, M.T., Bustos, M.A., De Blas, G.A., Rehmann, H., Zarelli, V.E., Trevino, C.L., Epac activates the small G proteins Rap1 and Rab3A to achieve exocytosis (2009) J. Biol. Chem., 284 (37), pp. 24825-24839
  • Seino, S., Takahashi, H., Fujimoto, W., Shibasaki, T., Roles of cAMP signalling in insulin granule exocytosis (2009) Diabetes Obes. Metab., 11, pp. 180-188
  • Sabbatini, M.E., Chen, X., Ernst, S.A., Williams, J.A., Rap1 activation plays a regulatory role in pancreatic amylase secretion (2008) J. Biol. Chem., 283 (35), pp. 23884-23894
  • Almahariq, M., Tsalkova, T., Mei, F.C., Chen, H., Zhou, J., Sastry, S.K., A novel EPAC-specific inhibitor suppresses pancreatic cancer cell migration and invasion (2013) Mol. Pharmacol., 83 (1), pp. 122-128
  • Lochner, A., Moolman, J.A., The many faces of H89: a review (2006) Cardiovasc. Drug Rev., 24 (3-4), pp. 261-274
  • Edreira, M.M., Li, S., Hochbaum, D., Wong, S., Gorfe, A.A., Ribeiro-Neto, F., Phosphorylation-induced conformational changes in Rap1b: allosteric effects on switch domains and effector loop (2009) J. Biol. Chem., 284 (40), pp. 27480-27486
  • Wang, Z., Dillon, T.J., Pokala, V., Mishra, S., Labudda, K., Hunter, B., Rap1-mediated activation of extracellular signal-regulated kinases by cyclic AMP is dependent on the mode of Rap1 activation (2006) Mol. Cell. Biol., 26 (6), pp. 2130-2145
  • Pereira, L., Rehmann, H., Lao, D.H., Erickson, J.R., Bossuyt, J., Chen, J., Novel Epac fluorescent ligand reveals distinct Epac1 vs: epac2 distribution and function in cardiomyocytes (2015) Proc. Natl. Acad. Sci. U. S. A., 112 (13), pp. 3991-3996
  • Hochbaum, D., Hong, K., Barila, G., Ribeiro-Neto, F., Epac, A.D.L., in synergy with cAMP-dependent protein kinase (PKA), is required for cAMP-mediated mitogenesis (2008) J. Biol. Chem., 283 (8), pp. 4464-4468
  • Hochbaum, D., Barila, G., Ribeiro-Neto, F., Altschuler, D.L., Radixin assembles cAMP effectors Epac and PKA into a functional cAMP compartment: role in cAMP-dependent cell proliferation (2011) J. Biol. Chem., 286 (1), pp. 859-866
  • Gloerich, M., Ponsioen, B., Vliem, M.J., Zhang, Z., Zhao, J., Kooistra, M.R., Spatial regulation of cyclic AMP-Epac1 signaling in cell adhesion by ERM proteins (2010) Mol. Cell. Biol., 30 (22), pp. 5421-5431
  • Woolsey, A.M., Burleigh, B.A., Host cell actin polymerization is required for cellular retention of Trypanosoma cruzi and early association with endosomal/lysosomal compartments (2004) Cell. Microbiol., 6 (9), pp. 829-838
  • Mott, A., Lenormand, G., Costales, J., Fredberg, J.J., Burleigh, B.A., Modulation of host cell mechanics by Trypanosoma cruzi (2009) J. Cell. Physiol., 218 (2), pp. 315-322
  • Jeyaraj, S.C., Unger, N.T., Eid, A.H., Mitra, S., Paul El-Dahdah, N., Quilliam, L.A., Cyclic AMP-Rap1A signaling activates RhoA to induce alpha(2c)-adrenoceptor translocation to the cell surface of microvascular smooth muscle cells (2012) Am. J. Physiol. Cell Physiol., 303 (5), pp. C499-511

Citas:

---------- APA ----------
Musikant, D., Ferri, G., Durante, I.M., Buscaglia, C.A., Altschuler, D.L. & Edreira, M.M. (2017) . Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi. Molecular and Biochemical Parasitology, 211, 67-70.
http://dx.doi.org/10.1016/j.molbiopara.2016.10.003
---------- CHICAGO ----------
Musikant, D., Ferri, G., Durante, I.M., Buscaglia, C.A., Altschuler, D.L., Edreira, M.M. "Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi" . Molecular and Biochemical Parasitology 211 (2017) : 67-70.
http://dx.doi.org/10.1016/j.molbiopara.2016.10.003
---------- MLA ----------
Musikant, D., Ferri, G., Durante, I.M., Buscaglia, C.A., Altschuler, D.L., Edreira, M.M. "Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi" . Molecular and Biochemical Parasitology, vol. 211, 2017, pp. 67-70.
http://dx.doi.org/10.1016/j.molbiopara.2016.10.003
---------- VANCOUVER ----------
Musikant, D., Ferri, G., Durante, I.M., Buscaglia, C.A., Altschuler, D.L., Edreira, M.M. Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi. Mol. Biochem. Parasitol. 2017;211:67-70.
http://dx.doi.org/10.1016/j.molbiopara.2016.10.003