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Effect of several nucleotides on the phosphorylating activities of the Rous-sarcoma-virus transforming protein
Bioscience Reports
|February 1, 1983
Abstract:
In the presence of ADP and GDP the tyrosine-phosphorylating activities of the viral as well as the cellular pp60src show a similar concentration-dependent inhibition in vitro. Addition of diadenosine 5',5"'-p1p4 tetraphosphate (Ap4A) to the kinase assay leads to an inhibition of the viral kinase activity, whereas the cellular kinase is not influenced.
Insights
Viral and cellular pp60src tyrosine phosphorylation are similarly inhibited by ADP and GDP in vitro. However, diadenosine tetraphosphate (Ap4A) selectively inhibits viral pp60src kinase activity, leaving the cellular form unaffected.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- pp60src is a tyrosine kinase involved in cellular signaling.
- Viral and cellular forms of pp60src play distinct roles.
- Understanding kinase regulation is crucial for deciphering cellular processes and viral pathogenesis.
Purpose of the Study:
- To investigate the differential regulation of viral and cellular pp60src tyrosine kinase activity.
- To explore the effects of specific nucleotides, ADP, GDP, and Ap4A, on pp60src activity.
Main Methods:
- In vitro kinase assays were performed.
- Tyrosine-phosphorylating activity of both viral and cellular pp60src was measured.
- Concentration-dependent inhibition studies were conducted using ADP and GDP.
- The effect of diadenosine tetraphosphate (Ap4A) was assessed.
Main Results:
- Both viral and cellular pp60src exhibited similar concentration-dependent inhibition by ADP and GDP in vitro.
- Diadenosine tetraphosphate (Ap4A) specifically inhibited the tyrosine kinase activity of viral pp60src.
- Cellular pp60src kinase activity remained unaffected by the addition of Ap4A.
Conclusions:
- ADP and GDP act as general inhibitors for both viral and cellular pp60src kinase activities.
- Ap4A demonstrates selective inhibition of viral pp60src, suggesting a potential mechanism for differential regulation.
- These findings highlight distinct regulatory mechanisms for viral and cellular pp60src, with implications for understanding oncogenesis.