Navegar

Colección

Datos Estadísticas

Artículo

Castro, A.F.; Amorena, C.; Müller, A.; Ottaviano, G.; Tellez-Iñon, M.T.; Taquini, A.C. "Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC" (1998) American Journal of Physiology - Cell Physiology. 275(1 44-1):C113-C119
Estamos trabajando para incorporar este artículo al repositorio
Consulte la política de Acceso Abierto del editor

Abstract:

Vasodilation by agents such as bradykinin and ATP is dependent on nitric oxide, the endothelium-dependent relaxing factor (EDRF). The release of EDRF results in elevation of cGMP in endothelial and smooth muscle cells (9). The signaling pathway that leads to increases in cGMP is not completely understood. The role of protein kinase C (PKC) in the elevation of cGMP induced by ATP and bradykinin was studied in cultured porcine aortic endothelial cells, by measuring PKC phosphorylation of a substrate and by measuring cGMP levels by radioimmunoassay. Extracellular ATP and bradykinin simultaneously elevated cGMP levels and PKC activity. The PKC inhibitors staurosporine, calphostin C, and Cremophor EL (T. Tamaoki and H. Nakano. Bio/Technology 8: 732-735, 1990; F. K. Zhao, L. F. Chuang, M. Israel, and R. Y. Chuang. Biochem. Biophys. Res. Commun. 159: 1359-1367, 1989) prevented the elevation of cGMP elicited by ATP and reduced that produced by bradykinin. Cremophor did not affect the elevation of cGMP by nitroprusside, an agent that directly increases guanylate cyclase activity (9). The PKC activator phorbol 12-myristate 13-acetate, but not a phorbol ester analog inactive on PKC, also elevated cGMP levels. These results suggest that EDRF agonists elevate cGMP in endothelial cells via PKC stimulation.

Registro:

Documento: Artículo
Título:Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC
Autor:Castro, A.F.; Amorena, C.; Müller, A.; Ottaviano, G.; Tellez-Iñon, M.T.; Taquini, A.C.
Filiación:Inst. de Invest. Cardiologicas, Facultad de Medicina, Universidad de Buenos Aires, 1122 Buenos Aires, Argentina
Inst. de Ing. Genet. y Biol. Molec., 1428 Buenos Aires, Argentina
Escuela de Ciencia y Tecnologia, Univ. Nacional de General San Martin, Buenos Aires, Argentina
Dept. of Physiology and Biophysics, Univ. of Texas Medical Branch, Galveston, TX 77555-0641, United States
Palabras clave:Endothelium-dependent relaxing factor; Phorbol ester; Protein kinase C inhibitors; adenosine triphosphate; bradykinin; calphostin c; cremophor; cyclic gmp; guanylate cyclase; nitric oxide; nitroprusside sodium; phorbol 13 acetate 12 myristate; phorbol ester derivative; protein kinase c; protein kinase c inhibitor; staurosporine; animal cell; article; controlled study; endothelium cell; enzyme activation; enzyme activity; immunoblotting; nonhuman; polyacrylamide gel electrophoresis; priority journal; protein phosphorylation; radioimmunoassay; swine; vascular endothelium; Adenosine Triphosphate; Animals; Aorta, Thoracic; Bradykinin; Cells, Cultured; Cyclic GMP; Endothelium, Vascular; Enzyme Activation; Enzyme Inhibitors; Fetus; Kinetics; Naphthalenes; NG-Nitroarginine Methyl Ester; Nitric Oxide; Phorbol Esters; Polyethylene Glycols; Protein Kinase C; Staurosporine; Swine; Tetradecanoylphorbol Acetate; Time Factors; Vasodilator Agents; Animalia; Suidae; Sus scrofa
Año:1998
Volumen:275
Número:1 44-1
Página de inicio:C113
Página de fin:C119
Título revista:American Journal of Physiology - Cell Physiology
Título revista abreviado:Am. J. Physiol. Cell Physiol.
ISSN:03636143
CODEN:AJPCD
CAS:Adenosine Triphosphate, 56-65-5; Bradykinin, 58-82-2; calphostin complex; cremophor, 39279-69-1; Cyclic GMP, 7665-99-8; Enzyme Inhibitors; Naphthalenes; NG-Nitroarginine Methyl Ester, 50903-99-6; Nitric Oxide, 10102-43-9; Phorbol Esters; phorbol-12,13-didecanoate, 24928-17-4; Polyethylene Glycols; Protein Kinase C, EC 2.7.1.37; Staurosporine, 62996-74-1; Tetradecanoylphorbol Acetate, 16561-29-8; Vasodilator Agents
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03636143_v275_n144-1_pC113_Castro

Referencias:

  • Amorena, C., Castro, A., Müller, A., Villamil, M.F., Direct vascular effects in the rat of the vehicles used for the intravenous and oral administration of cyclosporin A (1990) Clin. Sci. (Colch.), 79, pp. 149-154
  • Bredt, D.S., Ferris, C.D., Snyder, S.H., Nitric oxide synthase regulatory sites (1992) J. Biol. Chem., 267, pp. 10976-10981
  • Brown, C.A., Patel, V., Wilkinson, G., Boarder, M., P2 purinoceptor-stimulated conversion of arginine to citrulline in bovine endothelial cells is reduced by inhibition of protein kinase G (1996) Biochem. Pharmacol., 52, pp. 1849-1854
  • Buckley, B., Barchowsky, A., Dolor, R., Whorton, R., Regulation of arachidonic acid release in vascular endothelium (1991) Biochem. J., 280, pp. 281-287
  • Chuang, L.F., Israel, M., Chuang, R.Y., Cremophor EL inhibits 12-o-tetradecanoylphorbol-13-acetate (TPA)-induced protein phosphorylation in human myeloblastic leukemia ML-1 cells (1991) Anticancer Res., 11, pp. 1517-1521
  • Davda, R.K., Chandler, L.J., Guzman, N.J., Protein kinase C modulates receptor-independent activation of endothelial nitric oxide synthase (1994) Eur. J. Pharmacol., 266, pp. 237-244
  • Dekker, L.V., Parker, P.J., Protein kinase C - A question of specificity (1994) Trends Biochem. Sci., 19, pp. 73-77
  • De Nucci, G., Gryglewski, R.J., Warner, T.D., Vane, J.R., Receptor-mediated release of endothelium-derived relaxing factor and prostacyclin from bovine aortic endothelial cells is coupled (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 2334-2338
  • Furchgott, R.F., Introduction to EDRF research (1993) J. Cardiovasc. Pharmacol., 22 (7 SUPPL.), pp. S1-S2
  • Gomez, M.L., Medrano, E.E., Cafferatta, E.G.A., Tellez-Iñón, M.T., Protein kinase C is differentially regulated by thrombin, insulin, and epidermal growth factor in human mammary tumor cells (1988) Exp. Cell Res., 175, pp. 74-80
  • Guyton, J.R., Rosenberg, R.D., Clowes, A.W., Karnovsky, M.J., Inhibition of rat arterial smooth muscle cell proliferation by heparin (1980) Circ. Res., 46, pp. 625-634
  • Hecker, M., Luckhoff, A., Busse, R., Modulation of endothelial autacoid release by protein kinase C: Feedback inhibition or non specific attenuation of receptor-dependent cell activation? (1993) J. Cell. Physiol., 156, pp. 571-578
  • Hirata, K., Kuroda, R., Sakoda, T., Katayama, M., Nobutaka, I., Suematsu, M., Kawashima, S., Yokoyama, M., Inhibition of endothelial nitric oxide synthase activity by protein kinase C (1995) Hypertension, 25, pp. 180-185
  • Hortelano, S., Genaro, A.M., Bosca, L., Phorbol esters induce nitric oxide synthase and increase arginine influx in cultured peritoneal macrophages (1993) FEBS Lett., 320, pp. 135-139
  • Huang, K.-P., Chan, K.-F.J., Singh, T.J., Nakabayashi, H., Huang, F.L., Autophosphorylation of rat brain Ca 2+ -activated and phospholipid-dependent protein kinase (1986) J. Biol. Chem., 261, pp. 12134-12140
  • Jaffe, E.A., Nachman, R.N., Becker, C.G., Minick, C.R., Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria (1973) J. Clin. Invest., 52, pp. 2745-2756
  • Kraft, A.S., Anderson, W.B., Phorbol esters increase the amount of Ca 2+ , phospholipid- dependent protein kinase associated with plasma membrane (1983) Nature, 301, pp. 621-623
  • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head bacteriophage (1970) Nature, 227, pp. 680-685
  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275
  • Martin, W., White, D.G., Henderson, A.H., Endothelium-derived relaxing factor and atriopeptin II elevate cyclic GMP levels in pig aortic endothelial cells (1988) Br. J. Pharmacol., 93, pp. 229-239
  • Nakane, M., Mitchell, J., Förstermann, U., Murad, F., Phosphorylation by calcium calmodulin-dependent protein kinase II and protein kinase C modulates the activity of nitric oxide synthase (1991) Biochem. Biophys. Res. Commun., 180, pp. 1396-1402
  • Ohara, Y., Sayegh, H.S., Yamin, J.J., Harrison, D., Regulation of endothelial constitutive nitric oxide synthase by protein kinase C (1995) Hypertension, 25, pp. 415-420
  • Pirotton, S., Communi, D., Motte, S., Janssens, R., Boeynaems, J.M., Endothelial P2-purinoceptors: Subtypes and signal transduction (1996) J. Auton. Pharmacol., 16, pp. 353-356
  • Sakata, K., Karaki, H., Phorbol ester-induced release of endothelium-derived relaxing factor (1990) Eur. J. Pharmacol., 179, pp. 207-210
  • Smith, J.A., Lang, D., Release of endothelium-derived relaxing factor from pig cultured aortic endothelial cells, as assessed by changes in endothelial cell cyclic GMP content, is inhibited by a phorbol ester (1990) Br. J. Pharmacol., 99, pp. 565-571
  • Shimokawa, H., Flavahan, N.A., Lorenz, R.R., Vanhoutte, P.M., Prostacyclin releases endothelium-derived relaxing factor and potentiates its action in coronary arteries of the pig (1995) Br. J. Pharmacol., 95, pp. 1197-1203
  • Schwartz, S.M., Selection and characterization of bovine aortic endothelial cells (1978) In Vitro (Rockville), 14, pp. 966-980
  • Smith, C.D., Uhing, R.J., Snyderman, R., Nucleotide regulatory protein-mediated activation of phospholipase C in human polymorphonuclear leukocytes is disrupted by phorbol esters (1987) J. Biol. Chem., 262, pp. 6121-6127
  • Tamaoki, T., Nakano, H., Potent and specific inhibitors of protein kinase C of microbial origin (1990) Bio/Technology, 8, pp. 732-735
  • Tang, E.K.Y., Houslay, M.D., Glucagon, vasopressin and angiotensin all elicit a rapid, transient increase in hepatocyte protein kinase C activity (1992) Biochem. J., 283, pp. 341-346
  • Uratsuji, Y., Dicorleto, P.E., Growth-dependent subcellular redistribution of protein kinase C in cultured porcine aortic endothelial cells (1988) J. Cell. Physiol., 136, pp. 431-438
  • Zhao, F.K., Chuang, L.F., Israel, M., Chuang, R.Y., Cremophor EL, a widely used parenteral vehicle, is a potent inhibitor of protein kinase C (1989) Biochem. Biophys. Res. Commun., 159, pp. 1359-1367

Citas:

---------- APA ----------
Castro, A.F., Amorena, C., Müller, A., Ottaviano, G., Tellez-Iñon, M.T. & Taquini, A.C. (1998) . Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC. American Journal of Physiology - Cell Physiology, 275(1 44-1), C113-C119.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03636143_v275_n144-1_pC113_Castro [ ]
---------- CHICAGO ----------
Castro, A.F., Amorena, C., Müller, A., Ottaviano, G., Tellez-Iñon, M.T., Taquini, A.C. "Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC" . American Journal of Physiology - Cell Physiology 275, no. 1 44-1 (1998) : C113-C119.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03636143_v275_n144-1_pC113_Castro [ ]
---------- MLA ----------
Castro, A.F., Amorena, C., Müller, A., Ottaviano, G., Tellez-Iñon, M.T., Taquini, A.C. "Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC" . American Journal of Physiology - Cell Physiology, vol. 275, no. 1 44-1, 1998, pp. C113-C119.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03636143_v275_n144-1_pC113_Castro [ ]
---------- VANCOUVER ----------
Castro, A.F., Amorena, C., Müller, A., Ottaviano, G., Tellez-Iñon, M.T., Taquini, A.C. Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC. Am. J. Physiol. Cell Physiol. 1998;275(1 44-1):C113-C119.
Available from: https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03636143_v275_n144-1_pC113_Castro [ ]