TY - JOUR
T1 - The small GTPase Rab33A participates in regulation of amylase release from parotid acinar cells
AU - Imai, Akane
AU - Tsujimura, Maiko
AU - Yoshie, Sumio
AU - Fukuda, Mitsunori
N1 - Funding Information:
We would like to thank Dr. Hiromi Shimomura (The Nippon Dental University) and Dr. Miwa Sohda (Division of Oral Biochemistry, Niigata University) for helpful suggestions, and Dr. Ritsuko Sato (Department of Dental Hygiene, College at Niigata, The Nippon Dental University) for technical assistance. This work was supported by Grants-in-Aid for Scientific Research (C) ( 24592827 , 15K11063 ) (to A.I.) and ( 15H04367 ) (to M.F.) from the Japan Society for the Promotion of Science (JSPS).
Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.
PY - 2015/6/5
Y1 - 2015/6/5
N2 - Amylase is released from exocrine parotid acinar cells via typical exocytosis. Exocytosis of amylase-containing granules occurs through several steps, including formation, maturation, and transport of granules. These steps are thought to be regulated by members of the small GTPase Rab family. We previously demonstrated that Rab27 and its effectors mediate amylase release from parotid acinar cells, but the functional involvement of other Rab proteins in exocrine granule exocytosis remains largely unknown. Here, we studied isoproterenol (IPR)-induced amylase release from parotid acinar cells to investigate the possible involvement of Rab33A, which was recently suggested to regulate exocytosis in hippocampal neurons and PC12 cells. Rab33A was endogenously expressed in parotid acinar cells and present in secretory granules and the Golgi body. Functional ablation of Rab33A with anti-Rab33A antibody or a dominant-negative Rab33A-T50N mutant significantly reduced IPR-induced amylase release. Our results indicated that Rab33A is a novel component of IPR-stimulated amylase secretion from parotid acinar cells.
AB - Amylase is released from exocrine parotid acinar cells via typical exocytosis. Exocytosis of amylase-containing granules occurs through several steps, including formation, maturation, and transport of granules. These steps are thought to be regulated by members of the small GTPase Rab family. We previously demonstrated that Rab27 and its effectors mediate amylase release from parotid acinar cells, but the functional involvement of other Rab proteins in exocrine granule exocytosis remains largely unknown. Here, we studied isoproterenol (IPR)-induced amylase release from parotid acinar cells to investigate the possible involvement of Rab33A, which was recently suggested to regulate exocytosis in hippocampal neurons and PC12 cells. Rab33A was endogenously expressed in parotid acinar cells and present in secretory granules and the Golgi body. Functional ablation of Rab33A with anti-Rab33A antibody or a dominant-negative Rab33A-T50N mutant significantly reduced IPR-induced amylase release. Our results indicated that Rab33A is a novel component of IPR-stimulated amylase secretion from parotid acinar cells.
KW - Amylase release
KW - Intracellular distribution
KW - Parotid
KW - Rab33A
KW - β-stimulation
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U2 - 10.1016/j.bbrc.2015.04.022
DO - 10.1016/j.bbrc.2015.04.022
M3 - Article
C2 - 25871792
AN - SCOPUS:84937762999
SN - 0006-291X
VL - 461
SP - 469
EP - 474
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -