Short-chain
fatty acids (SCFAs), including propionate, are major
metabolites of intestinal microorganisms and play an essential role
in regulating intestinal epithelial integrity. Heat shock proteins
(HSPs) promote cellular homeostasis under physiological and stressed
conditions. This study aimed to investigate the regulation of intestinal
HSP70 by propionate in human intestinal Caco-2 cells and the colon
of fermentable dietary fiber (DF)-fed mice and germ-free mice. The
results showed that propionate increased Hspa1a (HSP70
mRNA) level in Caco-2 cells, upregulated HSP70 protein, and phosphorylation
of heat shock factor 1; however, the latter two were reduced by mitogen-activated
protein kinases and the mechanistic target of rapamycin inhibitors.
Feeding fermentable DFs, such as guar gum (GG) and partially hydrolyzed
GG, increased both cecal SCFAs and colonic HSP70 expression, both
of which were reduced in germ-free mice than in specific-pathogen-free
mice. Collectively, the propionate-induced HSP70 expression was shown
to be possibly involved in intestinal homeostasis.
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