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Related Experiment Videos

Gastrin biosynthesis in canine G cells.

Vinzenz Stepan1, Kentaro Sugano, Tadataka Yamada

  • 1Department of Pediatrics, University of Michigan, Ann Arbor, Michigan 48109-0656, USA.

American Journal of Physiology. Gastrointestinal and Liver Physiology
|April 19, 2002
PubMed
Summary

This study reveals that progastrin is cleaved by prohormone convertase 2 (PC2) into a glycine-extended intermediate (G-Gly). This intermediate is then amidated by peptidyl-glycine alpha-amidating monooxygenase (PAM) to form active gastrin.

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Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cell Biology

Background:

  • Gastrin, a key hormone, requires complex posttranslational modifications for its biological activity.
  • Progastrin processing involves cleavage at basic amino acid sites and C-terminal amidation.
  • The specific enzymes involved in progastrin processing in primary cells remained to be fully elucidated.

Purpose of the Study:

  • To investigate the precise biochemical pathway of progastrin processing in canine antral G cells.
  • To identify the prohormone convertase responsible for the initial cleavage of progastrin.
  • To confirm the role of peptidyl-glycine alpha-amidating monooxygenase (PAM) in the final amidation step.

Main Methods:

  • Utilized [(35)S]methionine-labeled pulse-chase biosynthetic experiments in primary canine antral G cells.

Related Experiment Videos

  • Employed PC2 antisense oligonucleotide probes to assess the role of prohormone convertase 2 (PC2).
  • Measured the accumulation and conversion of radiolabeled progastrin and its intermediates.

    • Main Results:

    • Progastrin processing intermediates, including glycine-extended gastrin (G-Gly), were identified and their temporal appearance characterized.
    • The conversion of G-Gly to amidated gastrin was significantly enhanced by ascorbic acid, a cofactor for PAM.
    • Inhibition of PC2 expression using antisense probes led to progastrin accumulation and delayed amidated gastrin formation.

    Conclusions:

    • Progastrin is cleaved by prohormone convertase 2 (PC2) in antral G cells to generate a glycine-extended intermediate (G-Gly).
    • This G-Gly intermediate is subsequently converted to COOH-terminally amidated gastrin through the enzymatic action of peptidyl-glycine alpha-amidating monooxygenase (PAM).
    • This study confirms the sequential enzymatic steps in gastrin biosynthesis within a relevant cellular context.