Development of biotin-avidin technology to investigate okadaic acid-promoted cell signaling pathway

Keiichi Konoki; Naoyuki Sugiyama; Michio Murata; Kazuo Tachibana; Yasumaru Hatanaka

doi:10.1016/S0040-4020(00)00752-3

Development of biotin-avidin technology to investigate okadaic acid-promoted cell signaling pathway

Keiichi Konoki, Naoyuki Sugiyama, Michio Murata, Kazuo Tachibana, Yasumaru Hatanaka

AGR - Agricultural Chemistry

Research output: Contribution to journal › Article › peer-review

24 Citations (Scopus)

Abstract

Four biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A (PP2A) by surface plasmon resonance (SPR). C7-biotinylated okadaic acid exhibited the strongest binding affinity to the enzyme, while Cl-biotinylated derivative was devoid of affinity. C24- or C27-biotinylated okadaic acid showed moderate affinity to the enzyme. In the wake of this finding, a biotinyl photoaffinity probe was introduced into 7-OH of okadaic acid. Photoaffinity labeling followed by SDS-PAGE analysis indicated that the okadaic acid derivative clearly labeled PP2A. Furthermore, three proteins were also labeled in crude extracts of a marine sponge Halichondria okadai. All these results imply that the C7-biotin conjugate is a versatile reagent for biochemical studies of okadaic acid-binding proteins including PP2A. (C) 2000 Elsevier Science Ltd.

Original language	English
Pages (from-to)	9003-9014
Number of pages	12
Journal	Tetrahedron
Volume	56
Issue number	46
DOIs	https://doi.org/10.1016/S0040-4020(00)00752-3
Publication status	Published - 2000 Nov 10

Keywords

Okadaic acid
Photoaffinity labeling
Protein phosphatase
Surface plasmon resonance

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0040-4020(00)00752-3

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title = "Development of biotin-avidin technology to investigate okadaic acid-promoted cell signaling pathway",

abstract = "Four biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A (PP2A) by surface plasmon resonance (SPR). C7-biotinylated okadaic acid exhibited the strongest binding affinity to the enzyme, while Cl-biotinylated derivative was devoid of affinity. C24- or C27-biotinylated okadaic acid showed moderate affinity to the enzyme. In the wake of this finding, a biotinyl photoaffinity probe was introduced into 7-OH of okadaic acid. Photoaffinity labeling followed by SDS-PAGE analysis indicated that the okadaic acid derivative clearly labeled PP2A. Furthermore, three proteins were also labeled in crude extracts of a marine sponge Halichondria okadai. All these results imply that the C7-biotin conjugate is a versatile reagent for biochemical studies of okadaic acid-binding proteins including PP2A. (C) 2000 Elsevier Science Ltd.",

keywords = "Okadaic acid, Photoaffinity labeling, Protein phosphatase, Surface plasmon resonance",

author = "Keiichi Konoki and Naoyuki Sugiyama and Michio Murata and Kazuo Tachibana and Yasumaru Hatanaka",

note = "Funding Information: This work is supported in part by Grant-In-Aids from the Ministry of Education, Science, Sports and Culture of Japan (EYS10780349 to K. K.; SRPA08281105 and SR12470504 to Y. H.). The authors are grateful to Dr M. Ojika of Nagoya University and Dr M. Sasaki in our laboratory of The University of Tokyo for discussion on the derivatization of okadaic acid, to Dr J. Inagawa of Biacore (K. K.) for valuable discussions and suggestions on SPR analysis, Ms M. Izumikawa in our laboratory of The University of Tokyo for mass spectrometry, and to Messrs H. Kusuoku, S. Matsuoka, H. Hori, and K. Otsuki in our laboratory of The University of Tokyo for their help in collecting H. okadai.",

year = "2000",

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doi = "10.1016/S0040-4020(00)00752-3",

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journal = "Tetrahedron",

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T1 - Development of biotin-avidin technology to investigate okadaic acid-promoted cell signaling pathway

AU - Konoki, Keiichi

AU - Sugiyama, Naoyuki

AU - Murata, Michio

AU - Tachibana, Kazuo

AU - Hatanaka, Yasumaru

N1 - Funding Information: This work is supported in part by Grant-In-Aids from the Ministry of Education, Science, Sports and Culture of Japan (EYS10780349 to K. K.; SRPA08281105 and SR12470504 to Y. H.). The authors are grateful to Dr M. Ojika of Nagoya University and Dr M. Sasaki in our laboratory of The University of Tokyo for discussion on the derivatization of okadaic acid, to Dr J. Inagawa of Biacore (K. K.) for valuable discussions and suggestions on SPR analysis, Ms M. Izumikawa in our laboratory of The University of Tokyo for mass spectrometry, and to Messrs H. Kusuoku, S. Matsuoka, H. Hori, and K. Otsuki in our laboratory of The University of Tokyo for their help in collecting H. okadai.

PY - 2000/11/10

Y1 - 2000/11/10

N2 - Four biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A (PP2A) by surface plasmon resonance (SPR). C7-biotinylated okadaic acid exhibited the strongest binding affinity to the enzyme, while Cl-biotinylated derivative was devoid of affinity. C24- or C27-biotinylated okadaic acid showed moderate affinity to the enzyme. In the wake of this finding, a biotinyl photoaffinity probe was introduced into 7-OH of okadaic acid. Photoaffinity labeling followed by SDS-PAGE analysis indicated that the okadaic acid derivative clearly labeled PP2A. Furthermore, three proteins were also labeled in crude extracts of a marine sponge Halichondria okadai. All these results imply that the C7-biotin conjugate is a versatile reagent for biochemical studies of okadaic acid-binding proteins including PP2A. (C) 2000 Elsevier Science Ltd.

AB - Four biotin conjugates of okadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A (PP2A) by surface plasmon resonance (SPR). C7-biotinylated okadaic acid exhibited the strongest binding affinity to the enzyme, while Cl-biotinylated derivative was devoid of affinity. C24- or C27-biotinylated okadaic acid showed moderate affinity to the enzyme. In the wake of this finding, a biotinyl photoaffinity probe was introduced into 7-OH of okadaic acid. Photoaffinity labeling followed by SDS-PAGE analysis indicated that the okadaic acid derivative clearly labeled PP2A. Furthermore, three proteins were also labeled in crude extracts of a marine sponge Halichondria okadai. All these results imply that the C7-biotin conjugate is a versatile reagent for biochemical studies of okadaic acid-binding proteins including PP2A. (C) 2000 Elsevier Science Ltd.

KW - Okadaic acid

KW - Photoaffinity labeling

KW - Protein phosphatase

KW - Surface plasmon resonance

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JF - Tetrahedron

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ER -

Development of biotin-avidin technology to investigate okadaic acid-promoted cell signaling pathway

Abstract

Keywords

UN SDGs

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