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Related Experiment Videos

Exocrine secretion granules contain peptide amidation activity.

M von Zastrow, T R Tritton, J D Castle

    Proceedings of the National Academy of Sciences of the United States of America
    |May 1, 1986
    PubMed
    Summary

    Rat parotid glands contain a novel enzyme, peptidyl-glycine alpha-amidating monooxygenase, in secretion granules. This enzyme, similar to pituitary forms, suggests exocrine glands may also perform peptide post-translational processing.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Endocrinology

    Background:

    • Alpha-amidation is a critical post-translational modification for many biologically active peptides.
    • Peptidyl-glycine alpha-amidating monooxygenase (PAM) is known to process secretory polypeptides in neural and endocrine granules.
    • The presence and function of PAM in exocrine secretion have not been previously established.

    Purpose of the Study:

    • To investigate the presence and characteristics of alpha-amidation enzyme activity in exocrine secretion granules.
    • To determine if exocrine secretion granules function as sites for post-translational processing of polypeptides.
    • To explore the potential role of L-ascorbic acid in exocrine secretion granules.

    Main Methods:

    • Enzyme assays were performed on purified secretion granule fractions from rat parotid glands.

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  • Biochemical properties such as ascorbate and copper requirements, pH dependence, and kinetics were analyzed.
  • Amidation activity was also assessed in granule fractions from other exocrine glands.
  • Carboxypeptidase activity was examined in parotid granule fractions.

    • Main Results:

    • Exocrine secretion granules from rat parotid glands contain an alpha-amidation enzyme closely resembling pituitary PAM.
    • The parotid enzyme exhibits similar cofactor requirements, pH dependence, and kinetic properties to the pituitary enzyme.
    • This activity is primarily localized within secretion granules and released via exocytosis.
    • Similar amidation activity was detected in other exocrine glands, and a B-type carboxypeptidase activity was found in parotid granules.

    Conclusions:

    • Exocrine secretion granules possess a novel alpha-amidation enzyme activity.
    • These findings suggest that exocrine secretion granules may serve as sites for post-translational processing, analogous to neural and endocrine granules.
    • The study highlights a potential role for L-ascorbic acid within parotid granules and opens avenues for future research into the identity and function of modified exocrine peptides.