Proteolytic and peptidase activities of the jejunum and ileum of the rat during postnatal development

Noack, R.; Koldovský, Otakar; Friedrich, M.; Heringová, A.; Jirsová, V.; Schenk, George H.

doi:10.1042/bj1000775

Cited by 40 publications

(15 citation statements)

References 11 publications

(7 reference statements)

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“…The oligoaminopeptidase and the y-glutamyltranspeptidase are the only brush border peptidases whose developmental pattern has been studied in human (4,18), rat (26), and guinea pig (8) intestine.…”

Section: Speculationmentioning

confidence: 99%

Development of Brush Border Peptidases in Human and Rat Small Intestine during Fetal and Neonatal Life

1981

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Pediatr. Res. 15: 991-995 (1981) SummaryThe cytosol peptidase activities hydrolyzing glycyl-L-leucine and L-leucyl-glycyl-glycine as well as the activities of the brush border peptidases (oligoaminopeptidase, aminopeptidase A, y-glutamyltranspeptidase, dipeptidyl-aminopeptidase IV, and carboxypeptidase) are present in rat fetuses during the early differentiation of the intestine (17th to 19th days of fetal life); they increase then at a different rate, reaching a maximum at various times, in the second and third wk after birth, and then decrease to the adult values during the first month of postnatal life. Only the oligoaminopeptidase activity increases steadily after birth, reaching maximal activity in the last decade of the first month.In human fetuses aged between 8 and 22 wk, the y-glutamyltranspeptidase was the only brush border peptidase found to be higher than in adults and children. On the other hand, the arninopeptidase A is remarkably reduced. The dipeptidylaminopeptidase IV and the carboxypeptidase are already at adult level in the youngest fetuses, and the oligoaminopeptidase increases during the period of fetal life studied; at the end of this period, the enzyme activity does not differ from the values found in children and adults.

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Section: Speculationmentioning

confidence: 99%

Development of Brush Border Peptidases in Human and Rat Small Intestine during Fetal and Neonatal Life

1981

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“…Although the development of several enzymes associated with intraluminal or intramucosal protein digestion has been studied [22], these enzymes are all specific for cr carboxyl-amide-linked peptides. The present report concerns the presence of a different type of intestinal peptidase, GGTP, which hydrolyzes only y carboxyl-amide bonds.…”

Section: Introductionmentioning

confidence: 99%

Gamma Glutamyl Transpeptidase: Measurement and Development in Guinea Pig Small Intestine

et al. 1969

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ExtractA modification ofa previous method for the assay ofy glutamyI transpeptidase (GGTP) was developed.Substrate solubility difficulties alluded to by other investigators were avoided by employing heating and solubilization of the chromogenic substrate y glutamyl-P-naphthylamide in a medium of carbonate 0.05 M and Tris buffer 0.1 M a t p H 9.5. The kinetics and conditions for such an assay are described. Whole intestinal homogenates of adult male guinea pigs were used as the source of the enzyme.The developmental pattern of this enzyme was determined in fetuses at 55 and 63 days of gestation and at varying times from 1 to 90 days of age. A total of 69 animals was assayed. The general pattern was that ofhigh specific activity during prenatal life, with a rapid decline during the neonatal period (3-24 days of age) and a slight increase after 55 days of age.Other guinea pig organs were studied. Liver and kidney were found to contain enzyme activity greater than that of the intestine. Subcellular fractionation of intestinal mucosa using ultracentrifugation revealed a twenty-fold enrichment of activity in jejunal brush border membrane, compared with whole jejunal homogenates when expressed as specific enzyme activity per mg of protein. The stability characteristics of GGTP disclosed no loss of specific activity when stored a t -28' for 50 days.This simple enzyme assay, stability of the enzyme when frozen, subcellular distribution in the intestinal brush border membrane, and an unusual developmental pattern made this enzyme a useful adjunct to the study of intestinal protein metabolism. SpeculationThe unique ability of GGTP to hydrolyze y glutamic acid-peptide bonds and the location of the enzyme in the intestinal brush border suggest a role for this enzyme in the metabolism of an unusual group of physiologically important peptides such as glutathione, folic acid, and gluten-gliadin. The significance of these y-bonded compounds may now be approached in order to investigate the role of this enzyme in gluten enteropathy and related disorders.

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“…The postnatal development of many pep tidase activities such as enterokinase [30], leucylnaphthylamidase [25] and tripeptidase (substrate glycylglycylglycine) [28] have been established in different intestinal segments in rats and mice. In the proximal part of the small intestine of suckling rats, Raul et al [30] have reported that enterokinase reaches its maximum activity during the 2nd week after birth, then declines towards the adult values which are established during the 4th week.…”

Section: Discussionmentioning

confidence: 99%

“…After completion of incubation at 37 °C, the activity was stopped in the reaction tubes by the addition of 1 ml of 20% acetic acid in water. In the second step of y-GT assay, the Bratton and Marshall reactions by means of which the released p-nitroanilide gives a purple color in the presence o f N-naphthylethylcne-diamine was used [28].…”

Section: Methodsmentioning

confidence: 99%

“…Brush border peptidases are the enzymes of most importance in the final digestion of proteins [29], The development of several enzymes associated with intraluminal or intramucosal protein digestion has been stud ied [28]. More recently, the developmental pattern of leucylnaphthylamidase (LNase) ac tivity in different intestinal segments of the mouse has been described [25].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Development of γ-Glutamyltranspeptidase Activity in Mouse Small Intestine: Influence of Cortisone and Thyroxine

Ménard¹,

Malo²,

Calvert³

1981

Neonatology

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The fetal and postnatal development of γ-glutamyltranspeptidase (γ-GT) activity has been examined in the different parts of the mouse small intestine. At 17 days of gestation, γ-GT is present in all intestinal thirds and a decreasing gradient of activity from the proximal to the distal segments is already established. From 17 days of gestation up to 5 days after birth, a dramatic fall of activity is observed in all segments. γ-GT activity reaches adult level before weaning in the proximal segment while it increases only during the 3rd postnatal week in the middle and distal intestinal segments. Daily administration of cortisone acetate (25 μg/g b.w./day) for 3 days to 8-day-old mice elicits a premature increase of γ-GT activity in all intestinal thirds, the maximal increase being observed in the proximal segment. On the other hand, thyroxine (1 μg/g b.w./day) has no or little effect on the normal development of γ-GT activity.

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Proteolytic and peptidase activities of the jejunum and ileum of the rat during postnatal development

Cited by 40 publications

References 11 publications

Development of Brush Border Peptidases in Human and Rat Small Intestine during Fetal and Neonatal Life

Development of Brush Border Peptidases in Human and Rat Small Intestine during Fetal and Neonatal Life

Gamma Glutamyl Transpeptidase: Measurement and Development in Guinea Pig Small Intestine

Development of γ-Glutamyltranspeptidase Activity in Mouse Small Intestine: Influence of Cortisone and Thyroxine

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