Stimulation of a histone H4 protein kinase in Triton X-100 lysates of rabbit peritoneal neutrophils pretreated with chemotactic factors: Lack of requirements of calcium mobilization and protein kinase C activation
✍ Scribed by Chi-Kuang Huang; Gary R. Laramee; Munehiro Yamazaki; Ramadan I. Sha'afi
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 506 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
The characteristics of the activation of a histone H4 kinase activity in Triton X-100 lysates of rabbit peritoneal neutrophils pretreated with met-Leu-Phe were studied: The activation of the kinase was a) inhibited by the antagonist of formylpeptide, t-Boc-(Phe-Leu),_-Phe, b) completely inhibited by pertussis toxin pretreatment, c) not affected by the pretreatment of neutrophils with an activator of protein kinase C, phorbol-12-myristate-13-acetate, or an inhibitor of protein kinase C, l-(5-isoquinoline-sulfonyl)-2-methyl-piperazine, and d) not inhibited in the cells preloaded with the intracellular calcium chelators, bis-(o-aminophenoxy)ethane-N,N,N,N-tetra acetic acid acetoxymethyl-ester (BAITA/AM). These results suggest that the stimulus-induced activation of H4 kinase requires functional receptor and GTP-binding protein but neither calcium mobilization nor protein kinase C activation.