Skip to main content
NCBI home page
The Journal of Physiology logoLink to The Journal of Physiology
. 1976 Nov;262(2):459–476. doi: 10.1113/jphysiol.1976.sp011605

The role of some small peptides in the transfer of amino nitrogen across the wall of vascularly perfused intestine.

C I Cheeseman, D S Parsons
PMCID: PMC1307653  PMID: 1086903

Abstract

The characteristics have been investigated of the transfer into the vascular bed of L-leucine and glycine from free amino acids or peptides in the intestinal lumen of Rana pipiens. Over the concentration range 0-5-10 mM the transfer of L-leucine is but little affected by the presence of equimolar concentrations of glycine but the transfer of glycine, in contrast, is greatly inhibited by the presence of L-leucine. 2. With glycyl-L-leucine in the intestinal lumen, the rate of transfer of glycine into the vascular bed is much greater than from the mixture of the two amino acids and is equal to that of the L-leucine. From L-leucyl-glycine the rates of transfer of leucine and of glycine are also higher than from the mixture of the two amino acids but the rate of transfer of glycine is somewhat lower than that of leucine. There is no evidence of the presence of the dipeptides in the effluent from the portal vein. 3. When the peptide glycyl-L-leucine is added to the lumen in the presence of 10 mM concentrations of the free amino acids, additional amounts of L-leucine and of glycine are transferred in approximately equimolar quantities into the vascular bed. This additional transfer exhibits saturation with respect to concentration of peptide in the intestinal lumen. An additional transfer of amino acids was also found when L-leucyl-glycine was added to the lumen in the presence of saturating concentrations of the two amino acids. 4. Evidence is presented that the presence of the dipeptides in the intestinal lumen had little effect on the transfer of free amino acids from the lumen into the vascular bed. Although the transfer of free amino acids from the lumen into the vascular bed is significantly, but not completely, abolished when the Na in the intestinal lumen is replaced by K, the transfer of the amino acids from the dipeptides is but little affected. 5. The findings are discussed in relation to the view that the dipeptides are transported into the mucosal epithelium by a process that is distinct from those promoting uptake of the individual amino acids. Being completely hydrolysed, there is no evidence for an accumulative uptake of the peptides; it is suggested that this may be related to the fact that the peptide uptake occurs in the absence of Na in the intestinal lumen.

Full text

PDF
459

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adibi S. A., Soleimanpour M. R. Functional characterization of dipeptide transport system in human jejunum. J Clin Invest. 1974 May;53(5):1368–1374. doi: 10.1172/JCI107685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Boyd C. A., Cheeseman C. I., Parsons D. S. Amino acid movements across the wall of anuran small intestine perfused through the vascular bed. J Physiol. 1975 Sep;250(2):409–429. doi: 10.1113/jphysiol.1975.sp011062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boyd C. A., Cheeseman C. I., Parsons D. S. Effects of sodium on solute transport between compartments in intestinal mucosal epithelium. Nature. 1975 Aug 28;256(5520):747–749. doi: 10.1038/256747a0. [DOI] [PubMed] [Google Scholar]
  4. Carter G. W., Van Dyke K. A superior counting solution for water-soluble tritiated compounds. Clin Chem. 1971 Jul;17(7):576–580. [PubMed] [Google Scholar]
  5. Cheeseman C. I., Parsons D. S. Intestinal absorption of peptides. Peptide uptake by small intestine of Rana pipiens. Biochim Biophys Acta. 1974 Dec 24;373(3):523–526. doi: 10.1016/0005-2736(74)90034-0. [DOI] [PubMed] [Google Scholar]
  6. FISHER R. B., PARSONS D. S. Glucose movements across the wall of the rat small intestine. J Physiol. 1953 Feb 27;119(2-3):210–223. doi: 10.1113/jphysiol.1953.sp004839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fujita M., Parsons D. S., Wojnarowska F. Oligopeptidases of brush border membranes of rat small intestinal mucosal cells. J Physiol. 1972 Dec;227(2):377–394. doi: 10.1113/jphysiol.1972.sp010038. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hanes C. S. Studies on plant amylases: The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem J. 1932;26(5):1406–1421. doi: 10.1042/bj0261406. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hellier M. D., Holdsworth C. D., McColl I., Perrett D. Dipeptide absorption in man. Gut. 1972 Dec;13(12):965–969. doi: 10.1136/gut.13.12.965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. MILNE M. D., CRAWFORD M. A., GIRAO C. B., LOUGHRIDGE L. W. The metabolic disorder in Hartnup disease. Q J Med. 1960 Jul;29:407–421. [PubMed] [Google Scholar]
  11. Malathi P., Ramaswamy K., Caspary W. F., Crane R. K. Studies on the transport of glucose from disaccharides by hamster small intestine in vitro. I. Evidence for a disaccharidase-related transport system. Biochim Biophys Acta. 1973 May 25;307(3):613–626. doi: 10.1016/0005-2736(73)90306-4. [DOI] [PubMed] [Google Scholar]
  12. Matthews D. M., Addison J. M., Burston D. Evidence for active transport of the dipeptide carnosine (beta-alanyl-L-histidine) by hamster jejunum in vitro. Clin Sci Mol Med. 1974 Jun;46(6):693–705. doi: 10.1042/cs0460693. [DOI] [PubMed] [Google Scholar]
  13. Matthews D. M., Craft I. L., Geddes D. M., Wise I. J., Hyde C. W. Absorption of glycine and glycine peptides from the small intestine of the rat. Clin Sci. 1968 Dec;35(3):415–424. [PubMed] [Google Scholar]
  14. Matthews D. M. Intestinal absorption of peptides. Physiol Rev. 1975 Oct;55(4):537–608. doi: 10.1152/physrev.1975.55.4.537. [DOI] [PubMed] [Google Scholar]
  15. Matthews D. M., Lis M. T., Cheng B., Crampton R. F. Observations on the intestinal absorption of some oligopeptides of methionine and glycine in the rat. Clin Sci. 1969 Dec;37(3):751–764. [PubMed] [Google Scholar]
  16. NEWEY H., SMYTH D. H. Intracellular hydrolysis of dipeptides during intestinal absorption. J Physiol. 1960 Jul;152:367–380. doi: 10.1113/jphysiol.1960.sp006493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rubino A., Field M., Shwachman H. Intestinal transport of amino acid residues of dipeptides. I. Influx of the glycine residue of glycyl-L-proline across mucosal border. J Biol Chem. 1971 Jun 10;246(11):3542–3548. [PubMed] [Google Scholar]
  18. Sardesai V. M., Provido H. S. The determination of glycine in biological fluids. Clin Chim Acta. 1970 Jul;29(1):67–71. doi: 10.1016/0009-8981(70)90222-6. [DOI] [PubMed] [Google Scholar]
  19. Winne D. Unstirred layer, source of biased Michaelis constant in membrane transport. Biochim Biophys Acta. 1973 Feb 27;298(1):27–31. doi: 10.1016/0005-2736(73)90005-9. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Physiology are provided here courtesy of The Physiological Society

RESOURCES