Inhibition of protein A24 lyase by nitrosoureas

FEBS Letters

Dornish, John M.¹  Smith-Kielland, Ingrid²  Markussen, Gunnar² 

[1] Department of Tissue Culture, Norsk Hydro's Institute for Cancer Research, The Norwegian Radium Hospital, Montebello, Oslo 3, Norway;Department of Biochemistry, University of Oslo, Blindern, Oslo 3 Norway

关键词: A24 (uH2A);    Alkylating agent;    Histone H2A;    Nitrosoureas;    Carbamoylation;    A24 lyase (Ehrlich ascites tumor cell);   

DOI  :  10.1016/0014-5793(84)81211-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein A24 content of Ehrlich ascites tumor cells increased several-fold following treatment of cell cultures with nitrosoureas, but did not increase when other alkylating agents not containing carbamoyl moieties were tested. The same nitrosoureas and, in addition, 2-chloroethyl isocyanate inhibited an A24 lyase-containing cytoplasmic extract in cleaving protein A24 into histone H2A and ubiquitin. It appears that carbamoylation of A24 lyase by nitrosoureas inhibits the enzyme and is responsible for the measured increases in cellular protein A24 content due to reduced turnover of this protein.

【 授权许可】

Unknown