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Titolo:
Butyrate suppression of colonocyte NF-kappa B activation and cellular proteasome activity
Autore:
Yin, L; Laevsky, G; Giardina, C;
Indirizzi:
Univ Connecticut, Dept Mol & Cellular Biol, Storrs, CT 06269 USA Univ Connecticut Storrs CT USA 06269 Cellular Biol, Storrs, CT 06269 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 48, volume: 276, anno: 2001,
pagine: 44641 - 44646
SICI:
0021-9258(20011130)276:48<44641:BSOCNB>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHAIN FATTY-ACIDS; QUIESCENT ULCERATIVE-COLITIS; COLONIC EPITHELIAL-CELLS; SODIUM-BUTYRATE; DIETARY FIBER; CANCER CELLS; WHEAT BRAN; PROTEOLYTIC PATHWAY; GENE-EXPRESSION; BETA-CATENIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
85
Recensione:
Indirizzi per estratti:
Indirizzo: Giardina, C Univ Connecticut, Dept Mol & Cell Biol, 75 N Eagleville Rd,U-125, Storrs, CT 06269 USA Univ Connecticut 75 N Eagleville Rd,U-125 Storrs CT USA 06269
Citazione:
L. Yin et al., "Butyrate suppression of colonocyte NF-kappa B activation and cellular proteasome activity", J BIOL CHEM, 276(48), 2001, pp. 44641-44646

Abstract

Butyrate is derived from the microbial metabolism of dietary fiber in the colon where it plays an important role in linking colonocyte turnover and differentiation to luminal content. In addition, butyrate appears to have both anti-inflammatory and cancer chemopreventive activities. Using confocal microscopy and cell fractionation studies, butyrate pretreatment of a humancolon cell line (HT-29 cells) inhibited the tumor necrosis factor-alpha (TNF-alpha)-induced nuclear translocation of the proinflammatory transcription factor NF-kappaB. Butyrate inhibited NF-kappaB DNA binding within 30 min of TNF-alpha stimulation, consistent with an inhibition of nuclear translocation. I kappaB.NF-kappaB complexes extracted from butyrate-treated cells were relatively resistant to in vitro dissociation by deoxycholate, suggesting a change in cellular I kappaB composition. Butyrate treatment increased p100 expression, an I kappaB that was not degraded upon TNF-alpha treatment. Butyrate also reduced the extent of TNF-alpha -induced I kappaB-alpha degradation and enhanced the presence of ubiquitin-conjugated I kappaB-alpha. The suppression of I kappaB-alpha degradation corresponded with a reductionin cellular proteasome activity as determined by in vitro proteasome assays and the increased presence of ubiquitin-conjugated proteins. The butyratesuppression of I kappaB-alpha degradation and proteasome activity may derive from its ability to inhibit histone deacetylases since the specific deacetylase inhibitor trichostatin A had similar effects. These results suggesta potential mechanism for the anti-inflammatory activity of butyrate and demonstrate the interplay between short chain fatty acids and cellular proteasome activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 11:52:58