PMID: 2125695Aug 10, 1990Paper

Antiproliferative activity of L-asparaginase of Tetrahymena pyriformis on human breast cancer cell lines

Molecular and Cellular Biochemistry
D A KyriakidisA H Kortsaris

Abstract

Purified L-asparaginase of Tetrahymena pyriformis is a multi-subunit enzyme exhibiting protein kinase activity as well. The enzyme's L-asparaginase activity is affected by its phosphorylation state. Both native and dephosphorylated L-asparaginase show antiproliferative activity on three breast cancer cell lines (T47D, BT20 and MCF-7) and on Walker 256 cells. These cells do not possess measurable L-asparaginase or L-asparagine synthetase activity. When T47D cells are treated for different times with L-asparaginase and then placed in fresh medium, the growth of cells treated for 1, 3, or 6 hours is initiated and parallels control curve, while the growth of cells treated for 24 or 48 hours with L-asparaginase stays at the same inhibitory level (24 h treatment) or continues to drop (48 h treatment). Addition of D-asparagine, a competitive inhibitor of T. pyriformis L-asparaginase, counteracts the antiproliferative activity of L-asparaginase, indicating that L-asparaginase and not the kinase activity is responsible for that effect.

References

Dec 1, 1975·FEBS Letters·Y Fishman, N Citri
Jun 1, 1990·Molecular and Cellular Biochemistry·S A Tsirka, D A Kyriakidis
May 1, 1988·Molecular and Cellular Biochemistry·D J TriantafillouD A Kyriakidis
Oct 1, 1988·Molecular and Cellular Biochemistry·S A Tsirka, D A Kyriakidis
Jan 1, 1985·Methods in Enzymology·J C Wriston
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Sep 15, 1982·International Journal of Cancer. Journal International Du Cancer·J A DistasioD L Durden
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