In vitro and in vivo degradation of human gastrin by endopeptidase 24.11

Deschodt-Lanckman, M; Pauwels, Stanislas; Najdovski, Tomé; Dimaline, R.; Dockray, G. J.

doi:10.1016/0016-5085(88)90244-2

Cited by 41 publications

(17 citation statements)

References 27 publications

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“…Arrows above the sequence indicate bonds at which cleavage by endopeptidase 24. 11 has been demonstrated (Power et al 1987;Deschodt-Lanckman et al 1988). G6, 1-11 G17 and 1-13 G17 have been unequivocally identified in antral mucosa, and could be liberated by an enzyme with an endopeptidase 24.…”

Section: Cleavagementioning

confidence: 98%

“…Both major forms of gastrin have similar acid-stimulating potencies, but G34 is cleared from the circulation about five times less rapidly than G17, and so is more effective (Walsh, Debas & Grossman, 1974;Walsh, Isenberg, Ansfield & Maxwell, 1976;Boniface, Picone, Schebalin, Zfass & Makhlouf, 1976;Eysselein, Maxwell, Reedy, Wunsch & Walsh, 1984). (Power et al 1987;Deschodt-Lanckman et al 1988). G6, 1-11 G17 and 1-13 G17 have been unequivocally identified in antral mucosa, and could be liberated by an enzyme with an endopeptidase 24.…”

Section: Cleavagementioning

confidence: 99%

“…For example, in both man and pig, sulphated G17 is relatively resistant to degradation by endopeptidase 24. 11 compared with the unsulphated variant (Power et al 1986;Deschodt-Lanckman et al 1988 It seems likely that post-secretory processing also occurs in the case of a more recently discovered regulatory peptide, atrial natriuretic peptide (ANP). The discovery of ANP stemmed from the observation that extracts of atrial myocardium induced a marked natriuresis in rats (de Bold, Borenstein, Veress & Sonneberg, 1981).…”

Section: Post-secretory Processingmentioning

confidence: 99%

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Post‐translational Modification of Peptide Messengers in the Gut

Dimaline

1988

Exp Physiol

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Classical methods such as precursor isolation, cell-free translation and pulse-chase experiments have been of limited use in studying biosynthesis of gastrointestinal peptides, because cell populations are generally sparse and intermingled with other cell types, rates of peptide turnover are low, and levels of mRNA are generally low. However, with the advent of recombinant DNA technology, and its application in predicting precursor sequences, the opportunity has arisen for an alternative approach to the study of propeptides. The success of this approach has to some extent resulted in the eclipse of studies of post-translational processing, although they are still of considerable physiological importance. Study of gastrointestinal peptides is proving a fruitful source of information about the mechanisms involved, as is now clear from recent work on the precursors for gastrin, cholecystokinin (CCK) and vasoactive intestinal peptide (VIP).This review will focus upon these three precursors to illustrate the important features and the physiological significance of post-translational processing, and to outline the strategies currently used to identify the structural modifications which take place in the synthesis of the peptides. Examples will also be drawn where appropriate from other precursors.

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Section: Cleavagementioning

confidence: 98%

Section: Cleavagementioning

confidence: 99%

Section: Post-secretory Processingmentioning

confidence: 99%

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Post‐translational Modification of Peptide Messengers in the Gut

Dimaline

1988

Exp Physiol

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“…Extrarenal gastrin extraction amounted to 12.5±5.l%, indicating that some gastrin is ca tabolized outside the kidneys. Some more re cent experimental studies [8] also suggest such a conclusion, showing that enzymes which catabolize gastrin are found not only in kidneys but in other organs (liver, grain), and in plas ma as well [24], A newly discovered enzyme, endopeptidase 24.11 (encephalinase) is widely distributed in different human tissues (partic ularly in the gastrointestinal system) and de grades G-17 in the peripheral circulation.…”

Section: Discussionmentioning

confidence: 99%

Influence of Renal Functional Mass on the Catabolism of Endogenous Gastrin in Humans

Reiner²,

Filjak³

1993

Kidney Blood Press Res

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The influences of renal function and mass on the catabolism of serum gastrin were studied in 27 patients with hypertension caused by unilateral parenchymal renal disease (77.8%), renal artery stenosis (11.1%) and essential hypertension (11.1%). Blood for gastrin analysis was taken by catheterization from the aorta, inferior vena cava, renal veins and cubital vein. Separate renal functions were measured using radioisotope methods and the renal mass was also calculated. Significant differences (p < 0.001) in serum gastrin concentration between the aorta (29.5 ± 6.7pmol/l), inferior vena cava (23.4 ± 5.8 pmol/l) and cubital vein (19.4 ± 4.5 pmol/l) were found. Extrarenal gastrin extraction amounted to 12.5% and was considerably lower than renal gastrin extraction (20.5%). There was a significant positive correlation between renal gastrin extraction and renal blood flow or renal functional mass. Kidneys have an important, but not exclusive, role in the catabolism of endogenous gastrin in humans. In the catabolism of some, or at least some molecular forms of, gastrin, the capillary systems of extrarenal tissues have an important role.

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“…In brief, Suc-Ala-Ala-Phe-AMC, a fluorogenic substrate, is cleaved by endopeptidase 24.11 to produce Phe-AMC which, after incubation with aminopeptidase M, gen erates AMC [7]. By the use of a standard curve estab lished with purified human renal endopeptidase 24.11 [8], it was possible to convert the rate of AMC production into enzyme amounts.…”

Section: Determination Of Endopeptidase 14 11 Urinary Levelsmentioning

confidence: 99%

Pathological Release of Urinary Endopeptidase 24.11 Early after Renal Transplantation

Nortier¹,

Abramowicz²,

Kinnaert³

et al. 1992

Enzyme

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Endopeptidase 24.11 (EC 3.4.24.11) enzymatic activity was spectrofluorimetrically measured in human urine, using a synthetic peptidic substrate. Urinary endopeptidase 24.11 output (Uendo) was determined in 24-hour urine samples of 10 kidney transplant recipients during the first 2 weeks after surgery. In 9 patients, a large increase in Uendo levels was noted during the 1st and/or the 2nd postoperative days (mean ± SEM of peak Uendo 624 ± 122 pg/24 h, p = 0.0003 as compared to 239 ± 20 μg/24 h in a healthy control population). This occurred whether patients received OKT3 (n = 6) or cyclosporine A (n = 3) as primary immunosuppression. Uendo returned to normal between the 3rd and the 5th postoperative day. We conclude that renal transplantation is associated with an early and marked release of endopeptidase 24.11 in urine. This could be due to the potentially toxic effects of ischemia and/or immunosuppressive drugs on the proximal tubular epithelium. The clinical usefulness of urinary endopeptidase 24.11 as a marker of tubular injury remains to be assessed.

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In vitro and in vivo degradation of human gastrin by endopeptidase 24.11

Cited by 41 publications

References 27 publications

Post‐translational Modification of Peptide Messengers in the Gut

Post‐translational Modification of Peptide Messengers in the Gut

Influence of Renal Functional Mass on the Catabolism of Endogenous Gastrin in Humans

Pathological Release of Urinary Endopeptidase 24.11 Early after Renal Transplantation

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