1991 Fiscal Year Final Research Report Summary
Physiological role of endogenous mono (ADP-ribosyl) ation of GTP binding proteins
| Project/Area Number |
02807205
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biological pharmacy
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
TANUMA Sei-ichi Tokyo Institute of Technology, Life Science, Associate Professor, 生命理工学部, 助教授 (10142449)
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| Project Period (FY) |
1990 – 1991
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| Keywords | mono (ADP-ribosyl) ation / mono (ADP-ribosyl) transferase / G protein / adenylate cyclase / platelet / signal transduction |
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| Research Abstract |
Three types of arginine-specific ADP-ribosyltransferase, named ADP-ribosyltransferase A, were purified from human platelets using polyarginine as an ADP-ribose acceptor. When human platelet membranes were incubated with the transferase A in the presence of [32P]-NAD, a 45 K Membrane protein was specifically labeled. On the analysis of labeled product with phosphodiesterase by strong-anion exchange HPLC, more than 90% of the radioactivity was deleted as 5'-AMP. The linkage between mono (ADP-ribose) and 45K protein was sensitive to neutral hydroxylamine treatment. ADP-ribose transfer to 45K protein by this enzyme was suppressed when membranes were pre-ADP-ribosylated by chlera toxin. These results suggest that the ADP-ribosyltransferase AI catalyzes mono (ADP-ribosyl) ation of the specific membrane G protein, Gs.
Incubation of platelet membranes with the transferase AI resulted in activation of the adenylate cyclase system. This stimulatory effects of the transferase AI on the adenylate cyclase system was further enhanced by prostagrandin (PG) El treatment.
These results indicate a role of ADP-ribosyltransferase AI in regulation of the adentlate cyclase system via endogenous mono (ADP-ribosyl) ation og Gs.
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Research Products
(15 results)
