INHIBITION OF HUMAN TELOMERASE BY L-ENANTIOMERS OF NATURAL 2′-DEOXYRIBONUCLEOSIDE 5′-TRIPHOSPHATES

Toyofumi Yamaguchi Department of Biological Sciences, Teikyo University of Science and Technology, Uenohara, Yamanashi, 409-0193, Japan

Rieko Yamada Department of Biological Sciences, Teikyo University of Science and Technology, Uenohara, Yamanashi, 409-0193, Japan

Aki Tomikawa Department of Biological Sciences, Teikyo University of Science and Technology, Uenohara, Yamanashi, 409-0193, Japan

Koichi Shudo National Institute of Health Sciences, Kamiyoga 1-18-1, Setagaya-ku, Tokyo, 158-8501, Japan

Motoki Saito Department of Life Science, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan

Fuyuki Ishikawa Department of Life Science, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan

Mineo Saneyoshi Department of Biological Sciences, Teikyo University of Science and Technology, Uenohara, Yamanashi, 409-0193, Japan

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Abstract

In order to clarify whether L-enantiomers of natural 2′-deoxyribonucleoside 5′-triphosphates (dNTPs) are recognized by human telomerase, a quantitative telomerase assay based on the ‘stretch PCR’ method was developed and used for kinetic analysis. Among the four L-dNTPs, L-dTTP and L-dGTP inhibited telomerase activity and the others showed slight or no inhibitory effect. Lineweaver-Burk plot analysis showed that the inhibition mode L-dGTP was competitive with dGTP.

ACKNOWLEDGMENTS

This study was supported in part by Grants-in-Aid for Scientific Research (Category C, 10672097) and Scientific Research on Bioscience/Biotechnology Areas from the Ministry of Education, Science, Sports and Culture of Japan, and Grants from The Promotion and Mutual Corporation for Private Schools of Japan, and The TV Yamanashi Science Development Fund.

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INHIBITION OF HUMAN TELOMERASE BY L-ENANTIOMERS OF NATURAL 2′-DEOXYRIBONUCLEOSIDE 5′-TRIPHOSPHATES

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INHIBITION OF HUMAN TELOMERASE BY L-ENANTIOMERS OF NATURAL 2′-DEOXYRIBONUCLEOSIDE 5′-TRIPHOSPHATES

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