2015 Fiscal Year Final Research Report
Signals for selective transport of secretory proteins in salivary glands
| Project/Area Number |
25462901
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Functional basic dentistry
|
|---|
| Research Institution | Nihon University |
|---|
Principal Investigator |
|
|---|
| Project Period (FY) |
2013-04-01 – 2016-03-31
|
| Keywords | 唾液腺 / 分泌顆粒 / 選別輸送 / 調節性分泌 / 構成性分泌 / 細胞極性 |
|---|
| Outline of Final Research Achievements |
Secretory proteins are exocytosed via two pathways: regularoty and constitutive secretory pathways. Secretory proteins may be separated into two pathways in the Golgi apparatus and the mechanism is unknown. To study the sorting mechanism in salivary glands, we have been using HaloTag, a reporter protein that was constructed to bind fluorescent ligands. We constructed HaloTag proteins fused with various proteins and examined their transport in primary culture of parotid acinar cells. As a result, cystatin, one of saliva proteins, fused with HaloTag was localized in the secretory granules and was released upon secretory stimulation. By fluorescent microscopy analysis, the signal intensity of HaloTag-fused cystatin is correlated with amylase. These results suggest that cystatin may interact with amylase in the Golgi apparatus which can promote sorting into regulated secretory pathway in parotid acinar cells.
|
| Free Research Field |
口腔生理学
|
