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J. Biol. Chem., Vol. 276, Issue 9, 6797-6806, March 2, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/9/6797    most recent M009355200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Murai, T. Articles by Terada, K. Search for Related Content PubMed PubMed Citation Articles by Murai, T. Articles by Terada, K. Social Bookmarking                      What's this?

Altered Regulation of Cell Cycle Machinery Involved in Interleukin-1-induced G₁ and G₂ Phase Growth Arrest of A375S2 Human Melanoma Cells^*

Toshimi Murai, Yukari Nakagawa, Hideko Maeda, and Kinuko Terada

From the Department of Biological Evaluation, National Institute of Health Sciences, Osaka Branch, Hoenzaka 1-1-43, Chuo-ku, Osaka 540-0006, Japan

Interleukin-1 (IL-1) inhibits the growth of A375S2 human melanoma cells by arresting them at G₁ and G₂ phases of the cell cycle. The arrests are preceded by a rapid decrease in kinase activities of cyclin E-Cdk2 and cyclin B1-Cdc2, which are critical for G₁-S and G₂-M progression, respectively. IL-1 quickly enhances the protein expression of the CDK inhibitor p21^cip1. The induced p21 binds preferentially to cyclin E-Cdk2, and the increase in p21 binding parallels the decrease in cyclin E-Cdk2 activity. Thus, p21 is likely to be responsible for the inhibition of cyclin E-Cdk2 activity and G₁ arrest. Coinciding with the decrease in cyclin B1-Cdc2 activity, there is an increase in tyrosine phosphorylation of Cdc2, suggesting that an increase in the inactive Tyr-15-phosphorylated form of Cdc2 is involved in the decrease in cyclin B1-Cdc2 activity and G₂ arrest. Furthermore, we found that IL-1 causes rapid dephosphorylation of p107, but not of pRb or p130, while the total protein levels of p130 are increased. Thus, IL-1 may exert its growth-arresting effects via p107 and p130 pathways rather than through pRb.

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