Project/Area Number |
11671871
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
病態科学系歯学(含放射線系歯学)
|
Research Institution | Nagasaki University |
Principal Investigator |
TASHIRO Sigeki Nagasaki University, School of Dentistry, Instructor., 歯学部, 助手 (20300882)
|
Co-Investigator(Kenkyū-buntansha) |
SUMI Tadateru Nagasaki University, School of Dentistry, Instructor., 歯学部・附属病院, 助手 (80284701)
KATAYAMA Ikuo Nagasaki University, School of Dentistry, Instructor., 歯学部・附属病院, 助手 (80295089)
SHIBATA Yosiyuki Nagasaki University, School of Dentistry, Instructor., 歯学部, 助手 (20253685)
NAKAMURA Takashi Nagasaki University, School of Dentistry, Prof., 歯学部, 教授 (30172406)
|
Project Period (FY) |
1999 – 2000
|
Project Status |
Completed (Fiscal Year 2000)
|
Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2000: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1999: ¥2,000,000 (Direct Cost: ¥2,000,000)
|
Keywords | cPLA2 / CaLB domain / nuclear export signal / intramolecular interaction / localization / transcriptional factor |
Research Abstract |
Cytosolic phospholipase A2 (cPLA2) cleaves membrane phospholipids to release arachidonic acid, initiating lipoxygenase and cyclooxygenase pathways. Mice lacking a gene for cPLA2 exhibit impaired allergic responses and fertility, and may have defects in neuronal cell death1,2. cPLA2 is activated by cytokines, submicromolar concentrations of Ca2+ ions, and MAP kinase-mediated phosphorylation of serine residues in the protein3.4. Activated cPLA2 protein distributes preferentially to the perinuclear region of the cell4-7, where the enzyme is thought to participate in arachidonic acid release. Here we show that cPLA2 binds directly and specifically to the B-Myb transcription factor and that, as a result, cPLA2 translocates into the nucleus. Binding site analysis demonstrated that both the N-and C-termini of cPLA2 interact with the C-terminus of B-Myb. The results also demonstrate that formation of cPLA2-B-Myb complexes and translocation to the nucleus is associated with regulation of B-Myb-dependent gene expression. These findings provide new insights into the intranuclear regulation of B-Myb function by cPLA2.
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