| Project/Area Number |
02660108
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
応用微生物学・発酵学
|
|---|
| Research Institution | Institute of Physical and Chemical Research (1991)
The University of Tokyo (1990) |
|---|
Principal Investigator |
TAKATSUKI Akira Institute of Physical and Chemical Research, Animal and Cellular Systems Laboratory, Head, 動物・細胞システム研究室, 主任研究員 (80011972)
|
|---|
| Project Period (FY) |
1990 – 1991
|
| Project Status |
Completed (Fiscal Year 1991)
|
| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1991: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1990: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
|---|
| Keywords | Glycoprotein / Translocation / Secretion / Inhibitor / ATPase / Virus / Brefeldin A / Golgi / ATP分解酵素 / フォリマイシン |
|---|
| Research Abstract |
Specific inhibitors are expected to be useful probes in analysis of the mechanism of intracellular translocation of glycoproteins. Very restricted are such inhibitors at present. Novel inhibitors have been searched for by a newly established screening method.
Many of the compounds isolated in this study were found to inhibit specifically the V-type ATPase among H^+-translocating ATPases. In the presence of such a compounds, cell surface expression of virus glycoprotein was greatly suppressed and accumulated intracellularly. The site(s) of blockade was indicated to be before or at the Golgi by analysing the structure of the N-glycosidically bound oligosaccharide moiety. On the contrary, invertase secretion to the periplasm and targetting of carboxypeptidase Y to the vacuole in Saccharomyces cerevisiae were not affected in spite of the fact the saccharide moiety of these glycoproteins was immaturely processed in the presence of inhibitor of V-type ATPase.
The already reported novel blockade by brefeldin was partly reversed by nocadazole, suggesting that induction of the retrograde trafficking from the Golgi to endoplasmic reticulum is the cause of the blockade of cell surface expression of virus glycoprotein.
|
