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Biological activity of progastrin posttranslational processing intermediates.

M Matsumoto, J Park, K Sugano

    The American Journal of Physiology
    |March 1, 1987
    PubMed
    Summary

    Carboxyl-terminally extended progastrin intermediates show minimal biological activity. Gastrin

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    Area of Science:

    • Gastroenterology and Molecular Biology
    • Peptide Hormone Research
    • Cellular Physiology

    Background:

    • Progastrin undergoes posttranslational processing into various intermediates.
    • Carboxyl-terminally extended progastrin intermediates are identified in G cells and cosecreted with gastrin.
    • The physiological significance of these intermediates remains unclear.

    Purpose of the Study:

    • To investigate the biological activity of synthetic gastrin precursor analogues (GL-7 and GL-9) with carboxyl-terminal extensions.
    • To compare the efficacy and potency of these analogues with gastrin heptadecapeptide on canine gastric cells.
    • To determine the role of carboxyl-terminal amidation in gastrin's biological activity.

    Main Methods:

    • Isolation of canine gastric parietal and D cells.
    • Synthesis of GL-7 and GL-9 analogues mimicking progastrin intermediates.
    • Assessment of receptor binding affinity using 125I-[Leu15]gastrin.
    • Measurement of [14C]aminopyrine uptake in parietal cells.
    • Quantification of somatostatin release from D cells.

    Main Results:

    • Both GL-7 and GL-9 analogues exhibited efficacy comparable to gastrin heptadecapeptide in displacing radiolabeled gastrin.
    • These analogues stimulated [14C]aminopyrine uptake and somatostatin release, similar to gastrin.
    • However, GL-7 and GL-9 were significantly less potent (10^4 to 10^5-fold) than gastrin heptadecapeptide.
    • The carboxyl-terminal amidation appears crucial for gastrin's high biological potency.

    Conclusions:

    • Progastrin processing intermediates, like GL-7 and GL-9, lack significant physiological relevance under normal conditions.
    • Carboxyl-terminal amidation of gastrin is essential for its potent biological activity.
    • These findings support the hypothesis that the amidated moiety is critical for the function of carboxyl-terminally amidated peptides.

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