1999 Fiscal Year Final Research Report Summary
Studies on regulatory mechanisms of phospholipid-metabolizing enzymes
| Project/Area Number |
10470035
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Sapporo Medical University |
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Principal Investigator |
KANOH Hideo Sapporo Medical University, School of Medicine, Department of Biochemistry, Prof., 医学部, 教授 (70045475)
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| Co-Investigator(Kenkyū-buntansha) |
IMAI Shinichi Sapporo Medical University, School of Medicine, Department of Biochemistry, Research Associate., 医学部, 助手 (20213209)
KAI Masahiro Sapporo Medical University, School of Medicine, Department of Biochemistry, Research Associated., 医学部, 助手 (80260777)
WADA Ikuo Sapporo Medical University, School of Medicine, Department of Biochemistry, Associated Prof., 医学部, 助教授 (40182969)
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| Project Period (FY) |
1998 – 1999
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| Keywords | diacylglycerol kinase / phosphatidic acid phosphatase / phospholipid / signal transduction / raft |
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| Research Abstract |
We transfected into cultured cells cDNAs coding for diacylglycerol kinase(KGK) and phosphatidic acid phosphatase(PAP9, and investigated their intracellular localization and catalytic activities. We found that DGK-delta binds to the endoplasmic reticulum through its C-terminal SAM domain serving as an anchoring signal. We also noted that the commercially available DGK inhibitors such as R59022 are selective to calcium-dependent DGK isozymes classified by us as type I isozymes.
In the case of PAP, we showed that PAP-2b expressed in HEK293 cells acts as an ectoenzyme hydrolyzing extracellular lyso-phosphatidic acid. We are currently studying the physiological implication of the localization of PAP-2s in non-caveolar raft microdomains.
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