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Regulation of apoptosis of interleukin 2‐dependent mouse T‐cell line protein tyrosine phosphorylation and polyamines
Author(s) -
Min An,
Hasuma Tadayoshi,
Yano Yoshihisa,
MatsuiYuasa Isao,
Otani Shuzo
Publication year - 1995
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041650320
Subject(s) - protein tyrosine phosphatase , tyrosine phosphorylation , microbiology and biotechnology , biology , tyrosine , dna fragmentation , putrescine , spermine , tyrosine kinase , phosphorylation , vanadate , ornithine decarboxylase , tyrosine kinase inhibitor , adenosylmethionine decarboxylase , biochemistry , apoptosis , programmed cell death , signal transduction , enzyme , genetics , cancer
We examined the effect of inhibitors of tyrosine kinase and tyrosine phosphatase on DNA fragmentation, protein tyrosine phosphorylation, and polyamine metabolism in the murine T‐cell line CTLL‐2. When cells were exposed to herbimycin A, a specific inhibitor of tyrosine kinase (Uehara et al., 1989, Biochem. Biophs. Res. Commun., 163 :803–809), in the presence of interleukin 2 (IL‐2), DNA was degraded into oligonucleosomal fragments in a dose‐dependent fashion. Genistein, another inhibitor of tyrosine kinase (Akiyama et al., 1987, J. Biol. Chem., 262 :5592–5596), had similar effects. Exposure of CTLL‐2 cells to vanadate, a tyrosine phosphatase inhibitor, blocked with the DNA fragmentation induced by herbimycin A. Tyrosine phosphorylation of 55 Kd protein was inhibited by herbimycin A, and the inhibition was reduced by vanadate. Ornithine decarboxylase (ODC) activity decreased rapidly after herbimycin A was added to CTLL‐2 cell cultures, while vanadate increased ODC activity. The exogenous addition of putrescine or spermine, but not that of spermidine, attenuated herbimycin A‐induced DNA fragmentation. These findings suggest that phosphorylation of tyrosine residues of 55 Kd protein prevents DNA fragmentation and that polyamines are involved in regulation of apoptosis. © 1995 Wiley‐Liss Inc.