Cargando…

Benzene-mediated protein kinase C activation.

Extracellular ligands transfer information into the cell through several pathways that operate in an integrated fashion. Protein kinase C, and enzyme that plays a pivotal role in signal transduction, is the molecular target for tumor promoters from the series of phorbol esters. A number of structura...

Descripción completa

Detalles Bibliográficos
Autores principales: Da Silva, C, Fan, X T, Castagna, M
Formato: Texto
Lenguaje:English
Publicado: 1989
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1568131/
https://www.ncbi.nlm.nih.gov/pubmed/2676506
_version_ 1782129947472560128
author Da Silva, C
Fan, X T
Castagna, M
author_facet Da Silva, C
Fan, X T
Castagna, M
author_sort Da Silva, C
collection PubMed
description Extracellular ligands transfer information into the cell through several pathways that operate in an integrated fashion. Protein kinase C, and enzyme that plays a pivotal role in signal transduction, is the molecular target for tumor promoters from the series of phorbol esters. A number of structurally unrelated tumor promoters also enhance protein kinase C, interacting or not interacting with the phorbol ester binding site. Evidence is provided that benzene potently activate protein kinase C in vitro, as well as in intact platelets. The drug does not compete for the phorbol ester binding site and probably affects the hydrophobic environment requires for full enzyme activation. Toluene is equally active. The relevance of the presented findings in the carcinogenic effects of benzene is discussed.
format Text
id pubmed-1568131
institution National Center for Biotechnology Information
language English
publishDate 1989
record_format MEDLINE/PubMed
spelling pubmed-15681312006-09-18 Benzene-mediated protein kinase C activation. Da Silva, C Fan, X T Castagna, M Environ Health Perspect Research Article Extracellular ligands transfer information into the cell through several pathways that operate in an integrated fashion. Protein kinase C, and enzyme that plays a pivotal role in signal transduction, is the molecular target for tumor promoters from the series of phorbol esters. A number of structurally unrelated tumor promoters also enhance protein kinase C, interacting or not interacting with the phorbol ester binding site. Evidence is provided that benzene potently activate protein kinase C in vitro, as well as in intact platelets. The drug does not compete for the phorbol ester binding site and probably affects the hydrophobic environment requires for full enzyme activation. Toluene is equally active. The relevance of the presented findings in the carcinogenic effects of benzene is discussed. 1989-07 /pmc/articles/PMC1568131/ /pubmed/2676506 Text en
spellingShingle Research Article
Da Silva, C
Fan, X T
Castagna, M
Benzene-mediated protein kinase C activation.
title Benzene-mediated protein kinase C activation.
title_full Benzene-mediated protein kinase C activation.
title_fullStr Benzene-mediated protein kinase C activation.
title_full_unstemmed Benzene-mediated protein kinase C activation.
title_short Benzene-mediated protein kinase C activation.
title_sort benzene-mediated protein kinase c activation.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1568131/
https://www.ncbi.nlm.nih.gov/pubmed/2676506
work_keys_str_mv AT dasilvac benzenemediatedproteinkinasecactivation
AT fanxt benzenemediatedproteinkinasecactivation
AT castagnam benzenemediatedproteinkinasecactivation