Sulforaphane activates heat shock response and enhances proteasome activity through up-regulation of Hsp27
Gan N, Wu YC, Brunet M, Garrido C, Chung FL, Dai C, Mi L
The Journal of biological chemistry · 103 citas
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Solo mecanismosDatos neutrales que nuestra revisión registró sobre cómo se hizo este estudio. Describen el método, nunca si nos gusta el resultado.
Cómo se estudió
- Diseño
- Estudio in vitro o de mecanismos (clasificado por nuestro filtro de IA)
- Estudiado en
- Células o muestras de laboratorio
- Resultado principal
- Solo mecanismos
Quién lo pagó
- Financiación
- Financiación independiente
- Gobierno
- U.S. Environmental Protection Agency
- Universidad u hospital
- Northwestern University
- Universidad u hospital
- University of Minnesota
- Gobierno
- Institut National de la Santé et de la Recherche Médicale
- Universidad u hospital
- Universitair Medisch Centrum Groningen
- Universidad u hospital
- Universität zu Köln
- Gobierno
- National Institutes of Health
- Gobierno
- National Cancer Institute
- Gobierno
- NCI NIH HHS
- Subvenciones
- National Cancer Institute (R01 CA100853); National Cancer Institute (CA100853); National Institutes of Health (CA100853)
Según 9 financiadores declarados.
Publicación
- Publicado
- 2010-09-11 · J Biol Chem · vol. 285 · número 46 · págs. 35528–35536
- Editorial
- Elsevier BV
- Citado
- 141 citas · más que el 92% de estudios similares · 3.2× el promedio de su campo
- Impacto
- Entre el 10 % más citado de su campo
- Referencias
- 49 trabajos
- Acceso
- Acceso abierto (revista híbrida) · CC-BY
- Áreas de investigación
- Genomics, phytochemicals, and oxidative stress · Heat shock proteins research · Selenium in Biological Systems
- Palabras clave
- Sulforaphane, Hsp27, Proteasome, Heat shock protein, Cell biology, KEAP1, Cruciferous vegetables, Cytotoxicity, Heat shock, Chemistry, Heat shock factor, Hsp70, Biology, Biochemistry, Transcription factor, Cancer, In vitro, Genetics
- MeSH
- cos cells, cell line, tumor, hela cells, animals, humans, thiocyanates, isothiocyanates, sulfoxides, proteasome endopeptidase complex, leupeptins, dna-binding proteins, transcription factors, anticarcinogenic agents, cysteine proteinase inhibitors, immunoblotting, reverse transcriptase polymerase chain reaction, protein biosynthesis, rna interference, up-regulation, enzyme activation, heat-shock response, dose-response relationship, drug, hot temperature, hsp27 heat-shock proteins, proteasome inhibitors, heat shock transcription factors, chlorocebus aethiops
7 autores
- Nanqin Gan🇺🇸🇨🇳Georgetown University; Chinese Academy of Sciences; Georgetown University Medical Center; Institute of Hydrobiology
- Yu‐Chieh Wu🇺🇸Georgetown University; Georgetown University Medical Center
- Mathilde Brunet🇫🇷Inserm
- Carmen Rosa Garrido🇫🇷Inserm
- Fung‐Lung Chung🇺🇸Georgetown University; Georgetown University Medical Center
- Chengkai Dai🇺🇸Jackson Laboratory
- Lixin Mi🇺🇸 · autor de correspondenciaGeorgetown University; Georgetown University Medical Center
Resumen
El texto original del estudio, en el idioma en que se publicó.
It is conceivable that stimulating proteasome activity for rapid removal of misfolded and oxidized proteins is a promising strategy to prevent and alleviate aging-related diseases. Sulforaphane (SFN), an effective cancer preventive agent derived from cruciferous vegetables, has been shown to enhance proteasome activities in mammalian cells and to reduce the level of oxidized proteins and amyloid β-induced cytotoxicity. Here, we report that SFN activates heat shock transcription factor 1-mediated heat shock response. Specifically, SFN-induced expression of heat shock protein 27 (Hsp27) underlies SFN-stimulated proteasome activity. SFN-induced proteasome activity was significantly enhanced in Hsp27-overexpressing cells but absent in Hsp27-silenced cells. The role of Hsp27 in regulating proteasome activity was further confirmed in isogenic REG cells, in which SFN-induced proteasome activation was only observed in cells stably overexpressing Hsp27, but not in the Hsp27-free parental cells. Finally, we demonstrated that phosphorylation of Hsp27 is irrelevant to SFN-induced proteasome activation. This study provides a novel mechanism underlying SFN-induced proteasome activity. This is the first report to show that heat shock response by SFN, in addition to the antioxidant response mediated by the Keap1-Nrf2 pathway, may contribute to cytoprotection.
Resumen vía Europe PMC. Los derechos de autor siguen siendo de los autores o la editorial (CC BY).
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