Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets

Autores
Elzagallaai, A.; Rosé, S. D.; Brandan, Nora Cristina; Trifaro, J. M.
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Stimulation of platelets by thrombin induces protein kinase C (PKC) activation, phosphorylation of pleckstrin, aggregation and serotonin release. Here, we demonstrate that, in human platelets, thrombin stimulation also induced phosphorylation of the myristoylated alanine-rich C Kinase substrate (MARCKS) and serotonine release in intact and digitonin-permeabilized platelets. MARKS is known to bind actin and cross-link actin filaments, and this is inhibited by PKC-evoqued MARKS phosphorylation. MARKS phosphorylation and serotonin release in response to increasing concentration of thrombin have a similar EC 50 and time course and, in permeabilized platelets, peptide MPSD, with an amino sequence corresponding to the phosphorylation site domain of MARKS, bloked both responses. However, pleckstrin and myosin light chain phosphorylations were not modified. Ala-MPSD, in which the four serine residues of MPSD were substituted by alanines was ineffective. The results suggest a role for MARKS in platelet secretion. The fact that pleckstrin phosphorylation has different time course and was not modified in the presence of MPSD when MARCKS phosphorylation and serotonine release were inhibited would suggest either that pleckstrin phosphorylation is unrelated to secretion or that it might only be involved upstream in the events leading to secretion.
Fil: Elzagallaai, A.. University of Ottawa; Canadá
Fil: Rosé, S. D.. University of Ottawa; Canadá
Fil: Brandan, Nora Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. University of Ottawa; Canadá
Fil: Trifaro, J. M.. University of Ottawa; Canadá
Materia
Platelets
Thrombin
Markcks
Secretion
Serotonin
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/29595

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network_name_str CONICET Digital (CONICET)
spelling Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from plateletsElzagallaai, A.Rosé, S. D.Brandan, Nora CristinaTrifaro, J. M.PlateletsThrombinMarkcksSecretionSerotoninhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Stimulation of platelets by thrombin induces protein kinase C (PKC) activation, phosphorylation of pleckstrin, aggregation and serotonin release. Here, we demonstrate that, in human platelets, thrombin stimulation also induced phosphorylation of the myristoylated alanine-rich C Kinase substrate (MARCKS) and serotonine release in intact and digitonin-permeabilized platelets. MARKS is known to bind actin and cross-link actin filaments, and this is inhibited by PKC-evoqued MARKS phosphorylation. MARKS phosphorylation and serotonin release in response to increasing concentration of thrombin have a similar EC 50 and time course and, in permeabilized platelets, peptide MPSD, with an amino sequence corresponding to the phosphorylation site domain of MARKS, bloked both responses. However, pleckstrin and myosin light chain phosphorylations were not modified. Ala-MPSD, in which the four serine residues of MPSD were substituted by alanines was ineffective. The results suggest a role for MARKS in platelet secretion. The fact that pleckstrin phosphorylation has different time course and was not modified in the presence of MPSD when MARCKS phosphorylation and serotonine release were inhibited would suggest either that pleckstrin phosphorylation is unrelated to secretion or that it might only be involved upstream in the events leading to secretion.Fil: Elzagallaai, A.. University of Ottawa; CanadáFil: Rosé, S. D.. University of Ottawa; CanadáFil: Brandan, Nora Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. University of Ottawa; CanadáFil: Trifaro, J. M.. University of Ottawa; CanadáWiley2001-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29595Elzagallaai, A.; Rosé, S. D.; Brandan, Nora Cristina; Trifaro, J. M.; Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets; Wiley; British Journal of Haematology; 112; 3; 12-2001; 593-6020007-10481365-2141CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1046/j.1365-2141.2001.02642.xinfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2141.2001.02642.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:19:09Zoai:ri.conicet.gov.ar:11336/29595instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:19:09.293CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
title Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
spellingShingle Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
Elzagallaai, A.
Platelets
Thrombin
Markcks
Secretion
Serotonin
title_short Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
title_full Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
title_fullStr Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
title_full_unstemmed Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
title_sort Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets
dc.creator.none.fl_str_mv Elzagallaai, A.
Rosé, S. D.
Brandan, Nora Cristina
Trifaro, J. M.
author Elzagallaai, A.
author_facet Elzagallaai, A.
Rosé, S. D.
Brandan, Nora Cristina
Trifaro, J. M.
author_role author
author2 Rosé, S. D.
Brandan, Nora Cristina
Trifaro, J. M.
author2_role author
author
author
dc.subject.none.fl_str_mv Platelets
Thrombin
Markcks
Secretion
Serotonin
topic Platelets
Thrombin
Markcks
Secretion
Serotonin
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Stimulation of platelets by thrombin induces protein kinase C (PKC) activation, phosphorylation of pleckstrin, aggregation and serotonin release. Here, we demonstrate that, in human platelets, thrombin stimulation also induced phosphorylation of the myristoylated alanine-rich C Kinase substrate (MARCKS) and serotonine release in intact and digitonin-permeabilized platelets. MARKS is known to bind actin and cross-link actin filaments, and this is inhibited by PKC-evoqued MARKS phosphorylation. MARKS phosphorylation and serotonin release in response to increasing concentration of thrombin have a similar EC 50 and time course and, in permeabilized platelets, peptide MPSD, with an amino sequence corresponding to the phosphorylation site domain of MARKS, bloked both responses. However, pleckstrin and myosin light chain phosphorylations were not modified. Ala-MPSD, in which the four serine residues of MPSD were substituted by alanines was ineffective. The results suggest a role for MARKS in platelet secretion. The fact that pleckstrin phosphorylation has different time course and was not modified in the presence of MPSD when MARCKS phosphorylation and serotonine release were inhibited would suggest either that pleckstrin phosphorylation is unrelated to secretion or that it might only be involved upstream in the events leading to secretion.
Fil: Elzagallaai, A.. University of Ottawa; Canadá
Fil: Rosé, S. D.. University of Ottawa; Canadá
Fil: Brandan, Nora Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. University of Ottawa; Canadá
Fil: Trifaro, J. M.. University of Ottawa; Canadá
description Stimulation of platelets by thrombin induces protein kinase C (PKC) activation, phosphorylation of pleckstrin, aggregation and serotonin release. Here, we demonstrate that, in human platelets, thrombin stimulation also induced phosphorylation of the myristoylated alanine-rich C Kinase substrate (MARCKS) and serotonine release in intact and digitonin-permeabilized platelets. MARKS is known to bind actin and cross-link actin filaments, and this is inhibited by PKC-evoqued MARKS phosphorylation. MARKS phosphorylation and serotonin release in response to increasing concentration of thrombin have a similar EC 50 and time course and, in permeabilized platelets, peptide MPSD, with an amino sequence corresponding to the phosphorylation site domain of MARKS, bloked both responses. However, pleckstrin and myosin light chain phosphorylations were not modified. Ala-MPSD, in which the four serine residues of MPSD were substituted by alanines was ineffective. The results suggest a role for MARKS in platelet secretion. The fact that pleckstrin phosphorylation has different time course and was not modified in the presence of MPSD when MARCKS phosphorylation and serotonine release were inhibited would suggest either that pleckstrin phosphorylation is unrelated to secretion or that it might only be involved upstream in the events leading to secretion.
publishDate 2001
dc.date.none.fl_str_mv 2001-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/29595
Elzagallaai, A.; Rosé, S. D.; Brandan, Nora Cristina; Trifaro, J. M.; Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets; Wiley; British Journal of Haematology; 112; 3; 12-2001; 593-602
0007-1048
1365-2141
CONICET Digital
CONICET
url http://hdl.handle.net/11336/29595
identifier_str_mv Elzagallaai, A.; Rosé, S. D.; Brandan, Nora Cristina; Trifaro, J. M.; Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets; Wiley; British Journal of Haematology; 112; 3; 12-2001; 593-602
0007-1048
1365-2141
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1046/j.1365-2141.2001.02642.x
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2141.2001.02642.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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