Exocyst subunits are involved in isoproterenol-induced amylase release from rat parotid acinar cells

Imai, A; Yoshie, S; Haga-Tsujimura, Maiko; Nashida, T; Shimomura, H (2012). Exocyst subunits are involved in isoproterenol-induced amylase release from rat parotid acinar cells. European journal of oral sciences, 120(2), pp. 123-131. Chichester: Wiley-Blackwell 10.1111/j.1600-0722.2012.00952.x

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Exocytosis of secretory granules in parotid acinar cells requires multiple events: tethering, docking, priming, and fusion with a luminal plasma membrane. The exocyst complex, which is composed of eight subunits (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70, and Exo84) that are conserved in yeast and mammalian cells, is thought to participate in the exocytotic pathway. However, to date, no exocyst subunit has been identified in salivary glands. In the present study, we investigated the expression and function of exocyst subunits in rat parotid acinar cells. The expression of mRNA for all eight exocyst subunits was detected in parotid acinar cells by RT-PCR, and Sec6 and Sec8 proteins were localized on the luminal plasma membrane. Sec6 interacted with Sec8 after 5 min of stimulation with isoproterenol. In addition, antibodies to-Sec6 and Sec8 inhibited isoproterenol-induced amylase release from streptolysin O-permeabilized parotid acinar cells. These results suggest that an exocyst complex of eight subunits is required for amylase release from parotid acinar cells.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Head Organs and Neurology (DKNS) > Clinic of Craniomaxillofacial Surgery

UniBE Contributor:

Haga-Tsujimura, Maiko

Subjects:

600 Technology > 610 Medicine & health

ISSN:

0909-8836

Publisher:

Wiley-Blackwell

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:37

Last Modified:

17 Dec 2014 07:46

Publisher DOI:

10.1111/j.1600-0722.2012.00952.x

PubMed ID:

22409218

Web of Science ID:

000301350500004

URI:

https://boris.unibe.ch/id/eprint/15152 (FactScience: 222392)

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