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Articles in PresS, published online ahead of print April 18, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00552.2001
Submitted on November 18, 2001
Accepted on April 10, 2002
1 Department of Periodontics, Endodontics and Dental Hygiene, University of Louisville, Louisville, Kentucky, USA
2 Department of Periodontics, Endodontics and Dental Hygiene, University of Louisville, Louisville, Kentucky, USA; Department of Biochemistry and Molecular Biology, University of Louisville, Louisville, Kentucky, USA
* To whom correspondence should be addressed. E-mail: sven.gorr{at}louisville.edu.
Sulfated proteoglycans have been proposed to play a role in the sorting and storage of secretory proteins in exocrine secretory granules. Rat parotid acinar cells expressed a 40-60 kDa proteoglycan that was stored in secretory granules. Treatment of the tissue with the proteoglycan synthesis inhibitor, p-nitrophenyl xyloside, resulted in the complete abrogation of the sulfated proteoglycan. Pulse-chase experiments in the presence of the xyloside analog showed a significant reduction in the stimulated secretion and granule storage of the newly synthesized regulated secretory proteins amylase and parotid secretory protein (PSP). Inhibition of proteoglycan sulfation by chlorate did not affect the sorting of these proteins. The effect of proteoglycan synthesis inhibition on protein sorting was completely reversed upon treatment with a weak acid. These results suggest that the sulfated proteoglycan is necessary for sorting and storage of regulated secretory proteins in the exocrine parotid gland. Preliminary evidence suggests that the mechanism involves the modulation of granule pH by the proteoglycan, rather than a direct interaction with other granule components.
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