Excretion of Histidine and Histidine Derivatives by Human Subjects Ingesting Protein from Different Sources

Block, Walter D.; Hubbard, Richard W.; Steele, Betty F.

doi:10.1093/jn/85.4.419

Cited by 40 publications

(19 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Block et al 1965;Perry et al 1967), to our Tsuji, 1987). The brush-border transport of carnosine is said to be regulated by dietary levels of amino acids, peptides and/or proteins (Ferraris, Diamond & Kwan, 1988).…”

Section: Discussionmentioning

confidence: 77%

Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose.

Gardner

Illingworth

Kelleher

et al. 1991

The Journal of Physiology

139

107

View full text Add to dashboard Cite

SUMMARY Healthy humans ingested the dipeptide carnosine (L-/I-alanyl-L-histidine).Their plasma levels and urinary outputs of carnosine and ,8-alanine were monitored over the following 5 h.2. Large amounts of intact carnosine (up to 14 % of the ingested dose) were recovered in the urine over the 5 h after ingestion. However, carnosine was undetectable in the plasma unless precautions were taken to inhibit blood carnosinase activity ex vivo during and after blood collection.3. The amount of carnosine recovered in urine varied substantially between subjects. It correlated negatively with carnosinase enzymic activity in the plasma. Highest carnosinase activities were observed in those subjects who regularly underwent physical training.4. Urinary recovery of the disaccharide lactulose also varied considerably between subjects, but was substantially lower than that of carnosine. There was no significant correlation between the recoveries of carnosine and lactulose. 5. When lactulose was ingested with a hypertonic solution, the urinary recovery of lactulose was generally increased. When carnosine was ingested with a hypertonic solution, the urinary recovery of carnosine was reduced: hence the paracellular route probably is not dominant for absorption of intact carnosine.6. Intact carnosine must have crossed the intestine to an extent much greater than hitherto recognized. Rapid post-absorptive hydrolysis is a severe obstacle to quantification of intact peptide absorption.

show abstract

Section: Discussionmentioning

confidence: 77%

Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose.

Gardner

Illingworth

Kelleher

et al. 1991

The Journal of Physiology

139

107

View full text Add to dashboard Cite

show abstract

“…Carnosinase activity of jejunal mucosa by weight is therefore approximately 200 to 400 times that of normal human plasma. Carnosine and anserine are found in minimal amounts (2 to 3 mg and 5 to 7 mg per day respectively) in the urine of healthy subjects (Westall, 1955), but the excretion strongly depends on the intake of animal flesh in the diet (Block, Hubbard, and Steele, 1965). The hydrolytic capacity of the intestinal enzyme for carnosine and anserine can therefore be easily saturated in healthy adults by giving sufficient beef steak (which contains 0 03 % carnosine by weight) or chicken breast (which contains both dipeptides).…”

Section: Range Of Meanmentioning

confidence: 99%

Carnosinase activity of human gastrointestinal mucosa.

Sadikali¹,

Darwish²,

Watson³

1975

Gut

View full text Add to dashboard Cite

SUMMARY Carnosinase, the dipeptidase which hydrolyses carnosine and other histidine-containing dipeptides, was assayed in mucosal tissues of the human and of the rat gut. Kinetic properties of the intestinal enzyme were found to be similar to carnosinase of other animal tissues. Little or no activity was detected in human gastric or colonic mucosa, and the levels were lower in duodenal than jejunal mucosa. The distribution of carnosinase is similar to that of the disaccharidases. Mean carnosinase activity was 8'8 units/g weight in 15 patients with histologically normal mucosa compared with 5-7 units in five with villous atrophy. The enzyme levels increased with histological improvement of the mucosa in patients with coeliac disease on a gluten-free diet. Tolerance curves for carnosine and its constitutent amino acids showed malabsorption of the dipeptide in a patient with carnosinase deficiency. It is concluded that the intestinal mucosa has much less hydrolase activity for carnosine than for glycylglycine and other dipeptidases, and the relatively slow hydrolysis appears to be the rate-limiting step in the total absorptive process.

show abstract

“…These authors had previously found that 3-methylhistidine, unlike other amino acids, released from muscle during protein depletion, was not reutilized in protein synthesis (7). For 1-methylhistidine Block et al (8) have suggested that the urinary excretion tended to reflect its dietary intake. This explanation does not seem tenable for 3-methylhistidine since it has not been found in any of the foods analyzed, yet it was recovered from the urine of the subjects.…”

Section: Introductionmentioning

confidence: 99%

Levels of Histidine and Histidine Derivatives in Breast Muscle of Protein-Depleted and Repleted Adult Cockerels

Fisher

Konlande

Strumeyer³

1975

Ann Nutr Metab

View full text Add to dashboard Cite

Four groups of adult cockerels, consisting of a control group given adequate protein, a protein-depleted group, and two groups that had been given, respectively, a low and a higher nitrogen-containing diet following protein depletion, were killed after appropriate time intervals and histidine and histidine derivatives analyzed in breast muscle extract. The concentration of 1-methylhistidine increased more than 12-fold during protein depletion and returned to near control levels during repletion. Carnosine decreased during depletion to less than 1/20 of the concentration in controls, yet increased more rapidly during repletion in the group fed a low-nitrogen diet free of histidine compared to the group fed a high-nitrogen diet containing histidine. Depleted cocks showed an elevation in the concentration of free histidine which decreased toward control levels after repletion. Levels of 3-methylhistidine were highest in the cocks fed diets containing histidine. Evidence for an accumulation in the breast muscle of adult cocks of 3-methylhistidine consisted of unusually high ratios of this derivative to muscle protein in all experimental groups. It was suggested that both 3-methylhistidine and 1-methylhistidine might serve as useful indices for assessing protein depletion in the adult cockerel, but that consideration should be given to the possibility of species differences in the metabolism of histidine derivatives during protein depletion and repletion.

show abstract

Excretion of Histidine and Histidine Derivatives by Human Subjects Ingesting Protein from Different Sources

Cited by 40 publications

References 12 publications

Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose.

Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose.

Carnosinase activity of human gastrointestinal mucosa.

Levels of Histidine and Histidine Derivatives in Breast Muscle of Protein-Depleted and Repleted Adult Cockerels

Contact Info

Product

Resources

About