Involvement of histone phosphorylation in thymocyte apoptosis by protein phosphatase inhibitors.
IUBMB Life
; 48(1): 79-83, 1999 Jul.
Article
en En
| MEDLINE
| ID: mdl-10791919
ABSTRACT
Incubation of rat thymocytes with the inhibitors of protein phosphatase such as calyculin A and okadaic acid resulted in an increase in DNA fragmentation. These effects were dependent on the concentration of the inhibitors and the incubation time. Analyses of the fragmented DNA revealed the production of approximately 50 kbp of DNA and a 180 bp DNA ladder. In addition, a laser scanning-microscopic analysis showed that these compounds caused nuclear condensation. Thus, these results demonstrated that protein phosphatase inhibitors induced thymocyte apoptosis. The inhibitors of protein phosphatase increased the phosphorylation of proteins of approximately 15 kDa. The phosphorylation of proteins preceded the DNA fragmentation induced by these inhibitors. Judging from acetic acid-urea-Triton X-100 gel electrophoresis, the phosphorylated proteins were histone H1 and H2A/H3. Therefore, these results suggest that phosphorylation of histones triggers the DNA fragmentation of thymocytes undergoing apoptosis.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oxazoles
/
Timo
/
Histonas
/
Linfocitos T
/
Proteínas Tirosina Fosfatasas
/
Apoptosis
/
Ácido Ocadaico
/
Inhibidores Enzimáticos
Límite:
Animals
Idioma:
En
Revista:
IUBMB Life
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
1999
Tipo del documento:
Article
País de afiliación:
Japón