PubMed · 4119414
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R H Dowling, G D Bell. 1973-02-03. Gallstone dissolution by chenodeoxycholic acid.. https://doi.org/10.1016/s0140-6736(73)90110-4
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Clostridium scindens is a keystone bacterial species in the mammalian gut that, while low in abundance, has a significant impact on bile acid and steroid metabolism. Numerous studies indicate that the two most studied strains of C. scindens (i.e. ATCC 35704 and VPI 12708) are important for a myriad of physiological processes in the host. We focus on both historical and current microbiological and molecular biology work on the Hylemon-Björkhem pathway and the steroid-17,20-desmolase pathway that were first discovered in C. scindens. Our most recent analysis now calls into question whether strains currently defined as C. scindens represent two separate taxonomic groups. Future directions include developing genetic tools to further explore the physiological role of bile acid and steroid metabolism by strains of C. scindens and the causal role of these pathways in host physiology and disease.
Stress tolerance and cross-protection in Enterococcus faecalis ATCC19433 were examined after exposure to bile salts, acid or heat shock. Bile salts and heat adapted cells demonstrated induced homologous tolerance and cross-resistance. No cross-protection of heat adapted cells against acid stress is observed and pretreatment with bile salts even sensitized the cells to this challenge. Whole-cell protein extract analysis revealed that each treatment induced a battery of stress proteins. Some of these polypeptides are induced by more than one treatment. The greatest overlap is observed between bile salts and heat treatments. Eighteen stress proteins, including DnaK and GroEL, are common between these stresses.
The effects of pH and of the bile salts, sodium cholate, chenodeoxycholate, taurocholate, deoxycholate and glycodeoxycholate on the adsorption of the heterocyclic aromatic amine mutagen and carcinogen 2-amino-3,8-dimethylimidazo[4,5-f]-quinoxaline (MeIQx) onto wheat bran cell wall material have been examined. The highest binding affinity of MeIQx for bran was at pH 5.5. Binding affinity declined more rapidly with pH > 5.5 than with pH < 5.5. Bile salts in solution did not appreciably affect the binding of MeIQx to bran, but where the bile salts formed a suspension then the adsorption was reduced. Where precipitation of bile salts occurred then the free concentration of MeIQx was also reduced, indicating that MeIQx binding/immobilization could be enhanced through interaction with bile salts.