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Critical Reviews in Oral Biology & Medicine
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4(3):393-398 (1993)     Crit Rev Oral Biol Med
© 1993 SAGE Publications

Sorting and Secretion of Salivary Proteins

J. David Castle

Department of Anatomy and Cell Biology and the Molecular Biology Institute, University of Virginia, Charlottesville, VA 22908

Anna M. Castle

Department of Anatomy and Cell Biology and the Molecular Biology Institute, University of Virginia, Charlottesville, VA 22908

Most salivary proteins are stored in secretion granules prior to export from acinar cells in response to neural stimuli. A small subset of these proteins undergo unstimulated secretion without apparent storage. This pathway probably comprises vesicles that bud from maturing storage granules and carries proteins that do not aggregate efficiently at the storage site. Expression of a parotid proline-rich protein (and deletion mutants) in pituitary AtT-20 cells has shown that an N-terminal domain is necessary for storage in secretion granules. Evidence suggests that self-aggregation of proline-rich protein mediated by this domain may function in both efficient intracellular transport and storage. Thus selective aggregation may be an important secretory sorting mechanism.

Key Words: salivary proteins • protein sorting • intracellular transport • secretory granules • parotid gland.

Critical Reviews in Oral Biology & Medicine, Vol. 4, No. 3, 393-398 (1993)
DOI: 10.1177/10454411930040031901
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