Co-localization of receptor and transducer proteins in glycolipid-enriched membrane domain.
| Project/Area Number |
13680686
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Structural biochemistry
|
|---|
| Research Institution | Nagoya University |
|---|
Principal Investigator |
KITAJIMA Ken Nagoya University, Bioscience Center, Associate Professor, 生物分子応答研究センター, 助教授 (80192558)
|
|---|
| Project Period (FY) |
2001 – 2002
|
| Project Status |
Completed (Fiscal Year 2002)
|
| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2002: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 2001: ¥2,100,000 (Direct Cost: ¥2,100,000)
|
|---|
| Keywords | LIPID RAFT / MEMBRANE DOMAIN / SEA URCHIN / PIG / EGG / SPERM / FERTILIZATION / GLYCOLIPID |
|---|
| Research Abstract |
The objective of this research project was to demonstrate molecular mechanism for co-localization and recruitment of functionally cognate proteins into glycolipid-enriched microdomain. The results are following :
1. Chemical and functional analyses of components of the glycolipid-enriched microdomain :
(1) At least two distinct membrane microdomains, each of which contains functionally cognate molecules, are present in sea urchin sperm, based on analysis of immunoprecipitation experiments.
(2) Comparison of components of sperm membrane microdomain from sea urchin with those from pig sperm shows that both commonly contain arylsulfatase, indicating the universal importance of sulfatide in fertilization.
(3) Liposomes containing phospholipid, cholesterol and glycolipids that are reconstituted based on composition of the sperm membrane microdomain inhibit sea urchin fertilization.
2. Elucidation of mechanism for recruitment of cognate components into glycolipid-enriched membrane microdomain :
(1) The sea urchin sperm membrane microdomain has a high melting point and shows more rigid nature than whole membrane.
(2) Recruitment of certain transducer proteins into the membrane microdomain dramatically changes during acrosome reaction after treatment of sperm with egg jelly components.
(3) Much more membrane microdomain samples that are homogenous in components are required to elucidate molecular mechanism for the recruitment of components into the membrane microdomains physicochemically.
|
Report
(3 results)
Research Products
(15 results)
