Glycyl-L-sarcosine absorption across ovine omasal epithelium during coincubation with other peptide substrates and volatile fatty acids.

To define the interactions between the absorption of glycyl-L-sarcosine (Gly-Sar; .1 mM) and glycine, L-methionylglycine, glycyl-L-leucine, L-carnosine, or L-methionylglycyl-L-methionyl-L-methionine (each at 5 mM), ovine omasal epithelium was collected from eight wethers (average BW=69+/-8.2 kg) and mounted in parabiotic chambers. [1,2]-[14C]Glycyl-L-sarcosine was used as a marker to monitor the presence of Gly-Sar. The Gly-Sar concentration in the omasal epithelium after 60 min of incubation was greatest (P < .05; .0055 nmol/mg dry tissue) when only Gly-Sar was present. Glycine inhibited (P < .05) Gly-Sar movement through the tissue by 20%, and peptide substrates inhibited (P < .05) Gly-Sar movement by 60 to 85%. The appearance of Gly-Sar in serosal buffers increased quadratically (P < .001) with time. Numerically, Gly-Sar appearance in serosal buffers was stimulated by the presence of glycine and peptide substrates. In a second experiment, ovine omasal epithelium was collected from four lambs (average BW=47+/-6.0 kg) to determine the interactions of Gly-Sar absorption (.1 mM) alone or when coincubated with either 10 mM butyric acid, or with a mixture of VFA (50 mM acetic acid, 40 mM propionic acid, and 10 mM butyric acid). The movement of Gly-Sar through the omasal epithelium was greatest (P < .05) when only Gly-Sar was present, and the VFA mixture inhibited (P < .05) Gly-Sar movement by 84%. Results from these studies support the idea that peptides can be absorbed across omasal epithelium and that the process involves mediated as well as nonmediated mechanisms, including possibly paracellular transport.