To clarify the unelucidated parts in the control mechanism and cancer onset mechanisms of DHPS and provide novel anticancer agents.
ERK and DHPS have been newly found to react with each other, while the phosphorylation of ERK has been newly found to suppress the mutual reaction. Thus, (1) ERK and DHPS act with each other to retain the interaction between the enzyme activation site in the three-dimensional structure of the DHPS and the spherical structure, thereby the enzymatic activity of DHPS (hypsination of IF5A) is suppressed. (2) When ERK is phosphorylated, the interaction between ERK and DHPS is suppressed and the interaction state between the enzyme activation site of DHPS and the spherical structure is not retained thereby it is strongly suggested the presence of the hypsination of IF5A. The substances holding or retaining the interaction state between the enzymatically activated site of DHPS and the spherical structure have a possibility to be useful as anticancer agent.
HATTA TOMOHISA
SASAKI YASUNORI
JPN6010062097, "Biochemical and Biophysical Research Communications", 1992, Vol.182, No.3, pp.1416−1422
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