Stress-induced non-vesicular extracellular release of complex of Ca^<2+>-binding proteins
| Project/Area Number |
20770105
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | Sojo University |
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Principal Investigator |
MATSUNAGA Hayato Sojo University, 生物生命学部, 助教 (20437833)
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| Co-Investigator(Renkei-kenkyūsha) |
UEDA Hiroshi 長崎大学, 医歯(薬)学総合研究科, 教授 (00145674)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 膜輸送と輸送タンパク質 / 神経科学 / ストレス / 蛋白質 / 脳・神経 / プロテオーム / 繊維芽細胞増殖因子 / S100A13 / カルシウム |
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| Research Abstract |
The nuclear protein prothymosin-α (ProT_α), which lacks a signal peptide sequence, is release from neurons and astrocytes on ischemic stress and exerts a unique form of neuroprotection through an anti-necrotic mechanism. Ischemic stress-induced ProT_α release is initiated by a nuclear release due to ATP loss, followed by extracellular release in a non-vesicular manner. S100A13, a Ca^<2+>-biniding protein, was identified to be a major protein co-released with ProT_α. The Ca^<2+>-dependent inteaction between ProT_α and S100A13 was found to require the C-terminal peptide sequences of both proteins. Under apoptotic condition, ProT_α was cleaved by casase-3 to generate a C-terminal peptide-deficient fragment, which lacks the nuclear localization signal. However, there was no extracellular release of ProT_α. These results suggest that necrosis-inducing stress induces an extracellula release of ProT_α in a non-vesicular maner, whereas apoptosis-inducing stress does not, owing to the loss of its interaction with S100A13, a cargo molecule for extracellular release.
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Report
(3 results)
Research Products
(11 results)
