1996 Fiscal Year Final Research Report Summary
Cellular dynamics of functional molecules and second messengers during synaptic transmission
| Project/Area Number |
07508004
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (A)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 試験 |
|---|
| Research Field |
Neurochemistry/Neuropharmacology
|
|---|
| Research Institution | The University of Tokyo |
|---|
Principal Investigator |
MIKOSHIBA Katsuhiko Inst.Medical Science, Professor, 医科学研究所, 教授 (30051840)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
MICHIKAWA Takayuki Inst.Medical Science, Research Associate, 医科学研究所, 助手 (90282516)
FURYICHI Teiichi Inst.Medical Science, Associate professor, 医科学研究所, 助教授 (50219094)
|
|---|
| Project Period (FY) |
1995 – 1996
|
| Keywords | neurotransmitter / neurotransmission / synaptotagmin / inositol polyphosphate / synapse / sinaptic vesicle |
|---|
| Research Abstract |
The inositol high-polyphodphate series (IP4, IP5 and IP6 ; IHPS) inhibit the neurotransmission through binding to the 2nd C2 domain of synaptotagmin (Syt), synaptic vesicle membrane proteins using superior cervical ganglion and squid giant synapse. Now we have revealed several proteins, including alpha adaptins which are specific subunits of clathrin AP2, from mouse brain were eluted by affinity elution chromatography from the C2 domain of Syt II-immobilized Sepharose using 50muM of inositol hexakisphosphate (IP6). The interaction between Syt II and AP2 was inhibited more strongly by IHPS than by the same concentration of IP3. Limited digestion of mouse crude synaptosomal fractions with trypsin revealed different cleavage pattern between in the presenc and the absence of 50muM IP6. These results suggests that IHPS-binding to C2B domain of synaptotagmin alter the state of protein-protein interaction such as synaptotagmin-AP2 interaction, which may induce the inhibition of some events involved in the neurotransmission, e.g. endocytosis.
|
