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Am J Physiol Cell Physiol (October 22, 2003). doi:10.1152/ajpcell.00338.2003
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Submitted on August 5, 2003
Accepted on October 12, 2003

Differential aggregation properties of secretory proteins that are stored in exocrine secretory granules of the pancreas and parotid glands

S. G Venkatesh1, Darrin J Cowley1, and Sven-Ulrik Gorr2*

1 Department of Periodontics, Endodontics & Dental Hygiene, University of Louisville, Louisville, KY, USA
2 Department of Periodontics, Endodontics & Dental Hygiene, University of Louisville, Louisville, KY, USA; Department of Biochemistry and Molecular Biology, University of Louisville, Louisville, KY, USA

* To whom correspondence should be addressed. E-mail: sven.gorr{at}louisville.edu.

Low-pH- and calcium-induced aggregation of regulated secretory proteins has been proposed to play a role in their retention and storage in secretory granules. However, this has not been tested for secretory proteins that are stored in the exocrine parotid secretory granules. Parotid granule matrix proteins were analyzed for aggregation in the presence or absence of calcium and the pH range from 5.5 - 7.5. Amylase did not aggregate under these conditions, while less than 10% of parotid secretory protein (PSP) aggregated below pH 6.0. To test aggregation directly in isolated granules, rat parotid secretory granules were permeabilized with 0.1% Saponin in the presence or absence of calcium and in the pH range 5.0 - 8.4. In contrast to the low-pH dependent retention of amylase in exocrine pancreatic granules, amylase was quantitatively released and most PSP was released from parotid granules under all conditions. Both proteins were completely released upon granule membrane solubilization. Thus, neither amylase nor PSP show low-pH or calcium-induced aggregation under physiological conditions in the exocrine parotid secretory granules.




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