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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Characteristics of glycyl-L-proline transport in intestinal brush-border membrane vesicles.

A proton-peptide symport mechanism has been postulated for transport of dipeptides in rabbit intestinal and renal brush-border membrane vesicles (BBMV). We have investigated the effects of a transmembrane potential (in mouse) and an inwardly directed proton gradient (in mouse, rabbit, and human) on the transport of glycyl-L-proline in intestinal BBMV. Membrane potential alterations, induced by permeant anions or generated by a K+-diffusion potential in the presence of valinomycin, did not accelerate the uptake of glycyl-L-proline. In contrast, in parallel experiments the uptake of D-glucose, whose cotransport system is electrogenic, was markedly increased by an interior negative membrane potential. Thus the transport of glycyl-L-proline in mouse intestinal BBMV is not electrogenic. Further studies on the effect of a proton gradient (extravesicular pH 5.5; intravesicular pH 7.5) on transport of glycyl-L-proline revealed an absence of stimulation of glycyl-L-proline transport and lower uptake rates in the presence of a proton gradient. The simultaneous presence of an interior negative membrane potential and an inwardly directed proton gradient did not accelerate the transport of glycyl-L-proline. These results demonstrate that the transport of glycyl-L-proline in mouse intestinal BBMV is neither electrogenic nor energized by an inwardly directed proton gradient. Likewise, pH gradients do not stimulate glycyl-L-proline uptake in either rabbit or human BBMV.[1]

References

  1. Characteristics of glycyl-L-proline transport in intestinal brush-border membrane vesicles. Rajendran, V.M., Harig, J.M., Ramaswamy, K. Am. J. Physiol. (1987) [Pubmed]
 
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