Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC
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 under...
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todo:paper_03636143_v275_n144-1_pC113_Castro2023-10-03T15:27:31Z Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC Castro, A.F. Amorena, C. Müller, A. Ottaviano, G. Tellez-Iñon, M.T. Taquini, A.C. 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 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03636143_v275_n144-1_pC113_Castro |
| institution |
Universidad de Buenos Aires |
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I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 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 |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Castro, A.F. Amorena, C. Müller, A. Ottaviano, G. Tellez-Iñon, M.T. Taquini, A.C. |
| author_facet |
Castro, A.F. Amorena, C. Müller, A. Ottaviano, G. Tellez-Iñon, M.T. Taquini, A.C. |
| author_sort |
Castro, A.F. |
| title |
Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC |
| title_short |
Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC |
| title_full |
Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC |
| title_fullStr |
Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC |
| title_full_unstemmed |
Extracellular ATP and bradykinin increase cGMP in vascular endothelial cells via activation of PKC |
| title_sort |
extracellular atp and bradykinin increase cgmp in vascular endothelial cells via activation of pkc |
| url |
http://hdl.handle.net/20.500.12110/paper_03636143_v275_n144-1_pC113_Castro |
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