K252a: a New Blocker of the Cell-cycle at G1 Phase in a Human Hepatoma Cell Line
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Abstract
The administration of 200 nM K252a to HuH7 suppressed the proliferation of the cells almost completely. The uptake of [3H]thymidine was inhibited, and flow cytometry revealed only one peak at 2C on day 3 after treatment with 100 nM K252a. The expression of proto-oncogene c-myc was not reduced. Despite the blockage at G1, both the size of the cells and the amount of cell protein had increased by 4 times by day 3 after treatment with K252a, while the cells secreted albumin and alpha-fetoprotein into the medium as usual. These results show that K252a can increase the cell size of HuH7 without losing its function by blocking the cell cycle at G1 phase.
References
1.
Gotoh Y, Nishida E, Matsuda S, Shiina N, Kosako H, Shiokawa K
. In vitro effects on microtubule dynamics of purified Xenopus M phase-activated MAP kinase. Nature. 1991; 349(6306):251-4.
DOI: 10.1038/349251a0.
View
2.
Kaneko Y, Shibuya M, Nakayama T, Hayashida N, Toda G, Endo Y
. Hypomethylation of c-myc and epidermal growth factor receptor genes in human hepatocellular carcinoma and fetal liver. Jpn J Cancer Res. 1985; 76(12):1136-40.
View
3.
Marcu K, Bossone S, Patel A
. myc function and regulation. Annu Rev Biochem. 1992; 61:809-60.
DOI: 10.1146/annurev.bi.61.070192.004113.
View
4.
Ohmi K, Yamashita S, Nonomura Y
. Effect of K252a, a protein kinase inhibitor, on the proliferation of vascular smooth muscle cells. Biochem Biophys Res Commun. 1990; 173(3):976-81.
DOI: 10.1016/s0006-291x(05)80881-2.
View
5.
Hashimoto Y, Nakayama T, Teramoto T, Kato H, Watanabe T, Kinoshita M
. Potent and preferential inhibition of Ca2+/calmodulin-dependent protein kinase II by K252a and its derivative, KT5926. Biochem Biophys Res Commun. 1991; 181(1):423-9.
DOI: 10.1016/s0006-291x(05)81436-6.
View