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Inhibition of pp60c-src protein kinase by herbimycin A in polyomavirus middle tumor antigen-transformed cells

Y W Yang1, Y H Chang

  • 1School of Pharmacy, College of Medicine, National Taiwan University, Taipei, Taiwan.

Anticancer Research
|December 31, 1997
PubMed

Insights

Herbimycin A inhibits pp60c-src kinase activity in polyomavirus-transformed cells. This inhibition is more effective in cell lysates than in immunoprecipitates, suggesting differential sensitivity.

Area of Science:

  • Oncology
  • Virology
  • Biochemistry

Background:

  • Middle T antigen (MTAg) from polyomavirus is crucial for tumorigenesis.
  • MTAg-associated pp60c-src kinase activity drives polyomavirus-mediated cell transformation.

Purpose of the Study:

  • To investigate the impact of herbimycin A on pp60c-src kinase activity.
  • To compare herbimycin A's inhibitory effects on pp60c-src in polyomavirus-transformed cells.

Main Methods:

  • Studied herbimycin A effects on pp60c-src kinase activity in polyomavirus and MTAg-transformed cells.
  • Assessed phosphorylation of src and MTAg.
  • Evaluated drug concentration and incubation time dependency.
  • Compared inhibition in cell lysates versus immunoprecipitates.

Main Results:

  • Herbimycin A reduced src and MTAg phosphorylation in treated cells.
  • Inhibition was dependent on drug concentration and incubation time.
  • pp60c-src activity in immunoprecipitates was more resistant to herbimycin A than in cell lysates.
  • Herbimycin A did not affect MTAg or pp60c-src synthesis.

Conclusions:

  • pp60c-src kinase activity in cell lysates is more sensitive to herbimycin A inhibition than in immunoprecipitates.
  • Herbimycin A offers a potential therapeutic avenue for targeting polyomavirus-induced cancers.

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