TY - JOUR
T1 - Functional involvement of Noc2, a Rab27 effector, in rat parotid acinar cells
AU - Imai, Akane
AU - Yoshie, Sumio
AU - Nashida, Tomoko
AU - Shimomura, Hiromi
AU - Fukuda, Mitsunori
N1 - Funding Information:
We thank Eiko Kanno for technical assistance. This work was supported in part by Ministry of Education, Culture, Sports, and Technology of Japan Grants 17657067, 18022048, 18050038, 18057026, 18207015 (to M.F.), by the Kato Memorial Bioscience Foundation (to M.F.), by The Sumitomo Foundation (to M.F.), by the Brain Science Foundation (to M.F.), by The Naito Foundation (to MF), and by a Research promotion Grant (NDUF-05-10, NDUF-06-01 and NDUF-06-15) from The Nippon Dental University.
PY - 2006/11/15
Y1 - 2006/11/15
N2 - Noc2 has recently been proposed to regulate exocytosis in both endocrine and exocrine cells; however, protein expression, subcellular localization and function of Noc2 in exocrine cells have never been elucidated. In this study, we investigated whether Noc2, a Rab27 effector, is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Rab27 was detected in the apical plasma membrane (APM) and secretory granule membrane (SGM) fractions, and was translocated to the APM after IPR stimulation for 5 min, but was detected at lower levels in the APM after 30 min. In contrast, although Noc2 was expressed in SGM bound to Rab27, Noc2 was not translocated to APM and the Noc2/Rab27 complex was disrupted after stimulation with IPR for short time. In addition, the anti-Noc2-Rab-binding-domain antibody inhibited IPR-stimulated amylase release from streptolysin O-permeabilized parotid acinar cells. Our results suggest that the Noc2/Rab27 complex is an important constituent of the early stages of IPR-stimulated amylase release.
AB - Noc2 has recently been proposed to regulate exocytosis in both endocrine and exocrine cells; however, protein expression, subcellular localization and function of Noc2 in exocrine cells have never been elucidated. In this study, we investigated whether Noc2, a Rab27 effector, is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Rab27 was detected in the apical plasma membrane (APM) and secretory granule membrane (SGM) fractions, and was translocated to the APM after IPR stimulation for 5 min, but was detected at lower levels in the APM after 30 min. In contrast, although Noc2 was expressed in SGM bound to Rab27, Noc2 was not translocated to APM and the Noc2/Rab27 complex was disrupted after stimulation with IPR for short time. In addition, the anti-Noc2-Rab-binding-domain antibody inhibited IPR-stimulated amylase release from streptolysin O-permeabilized parotid acinar cells. Our results suggest that the Noc2/Rab27 complex is an important constituent of the early stages of IPR-stimulated amylase release.
KW - Interaction
KW - Noc2
KW - Parotid acinar cell
KW - Rab27
KW - Rab27 effector
KW - Secretory granule exocytosis
KW - Subcellular localization
KW - Translocation
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U2 - 10.1016/j.abb.2006.09.021
DO - 10.1016/j.abb.2006.09.021
M3 - Article
C2 - 17067543
AN - SCOPUS:33750701171
SN - 0003-9861
VL - 455
SP - 127
EP - 135
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -