Uptake of Dipeptides Containing Basic and Acidic Amino Acids by Rat Small Intestine <i>in Vitro</i>

Burston, D.; Addison, Jill M.; Matthews, D. M.

doi:10.1042/cs0430823

Cited by 59 publications

(19 citation statements)

References 21 publications

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“…This showed that uptake of amino acids from these peptides could not be accounted for by their hydrolysis in the incubation medium followed by uptake of free amino acids. It did not exclude the possibility that uptake might be the result of hydrolysis at the surface of the mucosal cells, but previous observations (Hellier, Holdsworth, Perrett & Thirumalai, 1972 ;Burston et al, 1972) suggest that such a mechanism is unlikely to be entirely responsible for uptake of amino acids from these peptides.…”

Section: Resultsmentioning

confidence: 90%

Competition between Carnosine and other Peptides for Transport by Hamster Jejunum in Vitro

Addison¹,

Matthews²,

Burston³

1974

Clinical Science

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1. This paper reports the results of experiments on competition for transport by hamster jejunum in vitro between carnosine (8-alanyl-L-histidine) and other peptides and amino acids. Carnosine was chosen because this dipeptide is taken up intact with very little hydrolysis, which simplifies interpretation of the results.2. Jejunal uptake of carnosine was inhibited by equimolar glycylglycine, glycylglycylglycine, glycylsarcosine, glycylproline, methionylmethionine and prolylhydroxyproline but not by the equivalent free amino acids, or by a mixture of p-alanine and histidine. Inhibition of carnosine uptake by glycylproline was shown to be competitive. It is suggested that carnosine and the dipeptides inhibiting its uptake enter the mucosal cells by a common mechanism which is independent of the entry mechanisms for amino acids. Uptake of carnosine was not inhibited by N-acetylglycylglycine or by glycylglycine amide, suggesting that these substitutions prevent glycylglycine utilizing the dipeptide-uptake mechanism.3. Carnosine uptake was not inhibited by equimolar lysyllysine or a-glutamylglutamic acid, nor did lysyllysine and a-glutamylglutamic acid affect uptake of each other. Though these results are compatible with the existence of multiple dipeptideuptake systems in the intestinal mucosa, the evidence at present available is insufficient to permit any conclusion on this point.

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Section: Resultsmentioning

confidence: 90%

Competition between Carnosine and other Peptides for Transport by Hamster Jejunum in Vitro

Addison¹,

Matthews²,

Burston³

1974

Clinical Science

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“…However, it has been shown that acidic amino acids, although a marked species difference was observed (PARSONS and VOLMAN-MITCHELL, 1974), were rapidly transaminated intracellularly and changed to L-alanine (NEAME and WISEMAN, 1957;BURSTON et al, 1972). These observations indicate that the majority of acidic amino acid is then transported across the basolateral membrane by the transport carrier for neutral amino acid.…”

Section: Resultsmentioning

confidence: 83%

Rheogenic property of Na+/acidic amino acid co-transport by guinea pig intestine.

Himukai

1984

Jpn.J.Physiol

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The influx of L-glutamate or L-aspartate across the intestinal brush border membrane was absolutely dependent on the presence of Na+ in the mucosal solution and saturable. The addition of these amino acids into the mucosal solution induced a sudden and sustained increase in the transepithelial potential difference (PD J, which was found to be absolutely dependent on the presence of Na+ in the mucosal solution. The increases in PD t induced by L-glutamate or L-aspartate conformed to Michaelis-Menten kinetics against the concentration of each organic substrate. On the other hand, the relationship between the change in short-circuit current induced by acidic amino acid and Na+ concentration did not conform to Michaelis-Menten kinetics but was sigmoid. A kinetic study indicated that 2 Na+ were translocated per molecule of the acidic amino acid. The PD t was not altered by the total replacement of K+ by Na+ in the mucosal solution and showed the optimum pH at around 7. The transfer of L-glutamate from mucosal to serosal solution was examined with everted sac of ileum. A significant increase in serosal appearance was observed for L-glutamate and Lalanine after the incubation with L-glutamate. The serosal appearance of L-glutamate was unaffected by the presence or absence of HC03-.

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“…Data presented by several authors have indicated that some dipeptides may be absorbed into the enterocyte without prior hydrolysis (33)(34)(35)(36). Hence, one possible function of the cytosol peptide hydrolases may be the hydrolysis of absorbed dipeptides.…”

Section: Discussionmentioning

confidence: 99%

The Responses of Rat Intestinal Brush Border and Cytosol Peptide Hydrolase Activities to Variation in Dietary Protein Content DIETARY REGULATION OF INTESTINAL PEPTIDE HYDROLASES

Nicholson¹,

McCarthy²,

Kim³

1974

J. Clin. Invest.

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AB STR A CT The effects of variation in dietary protein content on small intestinal brush border and cytosol peptide hydrolase activities have been investigated.One group of rats was fed a high protein diet (55% casein) and another group was fed a low protein diet (10% casein). After 1 wk, brush border peptide hydrolase activity (L-leucyl-P-naphthylamide as substrate) and cytosol peptide hydrolase activity (L-prolyl-L-leucine as substrate) were determined in mucosae taken from the proximal, middle, and distal small intestine. As judged by several parameters, brush border peptide hydrolase activity was significantly greater in rats fed the high protein diet when data for corresponding segments were compared. In contrast, no significant difference was seen in cytosol peptide hydrolase activity.In a second study, brush border and cytosol peptide hydrolase activities were determined in the proximal intestine by utilizing an additional three peptide substrates: L-leucyl-L-alanine, L-phenylalanylglycine, and glyCyl-L-phenylalanine. Sucrase, maltase, and alkaline phosphatase activities were also determined. As before, brush border peptide hydrolase activities were significantly greater in rats fed the high protein diet. However, activities of the nonproteolytic brush border enzymes did not vary significantly with diet. In contrast to the results obtained with L-prolyl-L-leucine as substrate for the cytosol enzymes, cytosol activity against

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Uptake of Dipeptides Containing Basic and Acidic Amino Acids by Rat Small Intestine in Vitro

Cited by 59 publications

References 21 publications

Competition between Carnosine and other Peptides for Transport by Hamster Jejunum in Vitro

Competition between Carnosine and other Peptides for Transport by Hamster Jejunum in Vitro

Rheogenic property of Na+/acidic amino acid co-transport by guinea pig intestine.

The Responses of Rat Intestinal Brush Border and Cytosol Peptide Hydrolase Activities to Variation in Dietary Protein Content DIETARY REGULATION OF INTESTINAL PEPTIDE HYDROLASES

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