| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| 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.
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