Propionate absorption associated with bicarbonate secretion in vitro in the mouse cecum.

Short-chain fatty acids (SCFAs) produced by the microbial fermentation of undigested polysaccharide are rapidly absorbed in the large intestine. One proposed mechanism for this SCFA absorption is SCFA/HCO(-)3 exchange. To provide factual evidence for the operation of SCFA/HCO(-)3 exchange, we mounted an isolated mouse cecum in the Ussing chamber and measured the rates of propionate absorption (J(prop(ms))), alkaline secretion (J(OH(sm))) and total CO2 (HCO(-)3+CO2) secretion (J(tCO2(sm))), and the short-circuit current (I(sc)) with the mucosal side bathed with a Cl- and HCO(-)3-free solution. In the presence of propionate only on the mucosal but not in the serosal solution, J(prop(ms)) was larger when the serosal side was bathed with a HCO(-)3/CO2-containing solution than with a HCO(-)3/CO2-free solution. The addition of propionate to the mucosal side caused an increase in J(OH(sm)) and J(tCO2(sm)), the magnitude of these increases both being much greater with the serosal side bathed with the HCO(-)3/CO2-containing solution than with the HCO(-)3/CO2-free solution. Acetazolamide, a carbonic anhydrase inhibitor, largely suppressed HCO(-)3-dependent components of J(prop(ms)), propionate-induced J(OH(sm)), and propionate-induced J(tCO2(sm)). Acetazolamide, however, did not affect I(sc). The HCO(-)3-dependent component of J(prop(ms)) was not inhibited by either lactate or alpha-cyano-4-hydroxycinnamate, a typical substrate and an inhibitor of the monocarboxylate transporter (MCT1), respectively. It is concluded that an electroneutral, carbonic anhydrase-dependent SCFA/HCO(-)3 exchange mechanism was involved in SCFA absorption. The apical membrane protein for this pathway is not MCT1 and remains to be determined.