Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships
Autor(a) principal: | |
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Data de Publicação: | 1993 |
Outros Autores: | , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.6/554 |
Resumo: | Subcellular targeting of the components of the cAMPdependent pathway is thought to be essential for intracellular signaling. Here we have identified a novel protein, named myomegalin, that interacts with the cyclic nucleotide phosphodiesterase PDE4D, thereby targeting it to particulate structures. Myomegalin is a large 2,324-amino acid protein mostly composed of a-helical and coiled-coil structures, with domains shared with microtubule-associated proteins, and a leucine zipper identical to that found in the Drosophila centrosomin. Transcripts of 7.5–8 kilobases were present in most tissues, whereas a short mRNA of 2.4 kilobases was detected only in rat testis. A third splicing variant was expressed predominantly in rat heart. Antibodies against the deduced sequence recognized particulate myomegalin proteins of 62 kDa in testis and 230–250 kDa in heart and skeletal muscle. Immunocytochemistry and transfection studies demonstrate colocalization of PDE4D and myomegalin in the Golgi/centrosomal area of cultured cells, and in sarcomeric structures of skeletal muscle. Myomegalin expressed in COS-7 cells coimmunoprecipitated with PDE4D3 and sequestered it to particulate structures. These findings indicate that myomegalin is a novel protein that functions as an anchor to localize components of the cAMP-dependent pathway to the Golgi/centrosomal region of the cell. |
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Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity RelationshipsSubcellular targeting of the components of the cAMPdependent pathway is thought to be essential for intracellular signaling. Here we have identified a novel protein, named myomegalin, that interacts with the cyclic nucleotide phosphodiesterase PDE4D, thereby targeting it to particulate structures. Myomegalin is a large 2,324-amino acid protein mostly composed of a-helical and coiled-coil structures, with domains shared with microtubule-associated proteins, and a leucine zipper identical to that found in the Drosophila centrosomin. Transcripts of 7.5–8 kilobases were present in most tissues, whereas a short mRNA of 2.4 kilobases was detected only in rat testis. A third splicing variant was expressed predominantly in rat heart. Antibodies against the deduced sequence recognized particulate myomegalin proteins of 62 kDa in testis and 230–250 kDa in heart and skeletal muscle. Immunocytochemistry and transfection studies demonstrate colocalization of PDE4D and myomegalin in the Golgi/centrosomal area of cultured cells, and in sarcomeric structures of skeletal muscle. Myomegalin expressed in COS-7 cells coimmunoprecipitated with PDE4D3 and sequestered it to particulate structures. These findings indicate that myomegalin is a novel protein that functions as an anchor to localize components of the cAMP-dependent pathway to the Golgi/centrosomal region of the cell.uBibliorumVerde, IgnacioLoza, IsabelFerreiro, T. G.Sanz, F.Lozoya, E.Rodriguez, J.Manaut, F.Castro, ElenaFontenla, José AngelCadavid, IsabelHonrubia, M.Fueyo, J.Ravina, Enrique2010-04-28T10:06:48Z19931993-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.6/554enginfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-12-15T09:35:46Zoai:ubibliorum.ubi.pt:10400.6/554Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:42:36.066988Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
title |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
spellingShingle |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships Verde, Ignacio |
title_short |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
title_full |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
title_fullStr |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
title_full_unstemmed |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
title_sort |
Antiserotoninergic activity of 2-aminoethylbenzocyclanones in rat aorta: Structure-activity Relationships |
author |
Verde, Ignacio |
author_facet |
Verde, Ignacio Loza, Isabel Ferreiro, T. G. Sanz, F. Lozoya, E. Rodriguez, J. Manaut, F. Castro, Elena Fontenla, José Angel Cadavid, Isabel Honrubia, M. Fueyo, J. Ravina, Enrique |
author_role |
author |
author2 |
Loza, Isabel Ferreiro, T. G. Sanz, F. Lozoya, E. Rodriguez, J. Manaut, F. Castro, Elena Fontenla, José Angel Cadavid, Isabel Honrubia, M. Fueyo, J. Ravina, Enrique |
author2_role |
author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
uBibliorum |
dc.contributor.author.fl_str_mv |
Verde, Ignacio Loza, Isabel Ferreiro, T. G. Sanz, F. Lozoya, E. Rodriguez, J. Manaut, F. Castro, Elena Fontenla, José Angel Cadavid, Isabel Honrubia, M. Fueyo, J. Ravina, Enrique |
description |
Subcellular targeting of the components of the cAMPdependent pathway is thought to be essential for intracellular signaling. Here we have identified a novel protein, named myomegalin, that interacts with the cyclic nucleotide phosphodiesterase PDE4D, thereby targeting it to particulate structures. Myomegalin is a large 2,324-amino acid protein mostly composed of a-helical and coiled-coil structures, with domains shared with microtubule-associated proteins, and a leucine zipper identical to that found in the Drosophila centrosomin. Transcripts of 7.5–8 kilobases were present in most tissues, whereas a short mRNA of 2.4 kilobases was detected only in rat testis. A third splicing variant was expressed predominantly in rat heart. Antibodies against the deduced sequence recognized particulate myomegalin proteins of 62 kDa in testis and 230–250 kDa in heart and skeletal muscle. Immunocytochemistry and transfection studies demonstrate colocalization of PDE4D and myomegalin in the Golgi/centrosomal area of cultured cells, and in sarcomeric structures of skeletal muscle. Myomegalin expressed in COS-7 cells coimmunoprecipitated with PDE4D3 and sequestered it to particulate structures. These findings indicate that myomegalin is a novel protein that functions as an anchor to localize components of the cAMP-dependent pathway to the Golgi/centrosomal region of the cell. |
publishDate |
1993 |
dc.date.none.fl_str_mv |
1993 1993-01-01T00:00:00Z 2010-04-28T10:06:48Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.6/554 |
url |
http://hdl.handle.net/10400.6/554 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799136326775209984 |