Planta Med 2015; 81(01): 26-31
DOI: 10.1055/s-0034-1383311
Biological and Pharmacological Activity
Original Papers
Georg Thieme Verlag KG Stuttgart · New York

Comparison of the Inhibitory Effects of Delphinidin and Its Glycosides on Cell Transformation

Takayuki Sogo
1   The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan
,
Takuma Kumamoto
1   The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan
,
Hisako Ishida
2   Faculty of Agriculture, Kagoshima University, Kagoshima, Japan
,
Ayami Hisanaga
1   The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan
,
Kozue Sakao
1   The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan
2   Faculty of Agriculture, Kagoshima University, Kagoshima, Japan
,
Norihiko Terahara
3   Faculty of Health and Nutrition, Minami-Kyushu University, Miyazaki, Japan
,
Koji Wada
1   The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan
4   Faculty of Agriculture, University of the Ryukyus, Okinawa, Japan
,
De-Xing Hou
1   The United Graduate School of Agricultural Science, Kagoshima University, Kagoshima, Japan
2   Faculty of Agriculture, Kagoshima University, Kagoshima, Japan
› Author Affiliations
Further Information

Publication History

received 25 June 2014
revised 18 October 2014

accepted 26 October 2014

Publication Date:
03 December 2014 (online)

Abstract

Although anthocyanins are major forms distributed in many plant foods and promising as chemopreventive source, many molecular data are obtained from anthocyanidins, showing their low bioavailability. This study aims to clarify the inhibitory effects of delphinidin glycosides on cell transformation comparing them to those of delphinidin. Screening data revealed that delphinidin 3-sambubioside could directly bind to MAPK/ERK kinase 1. Affinity assay data confirmed that delphinidin 3-sambubioside had higher binding affinity to MAPK/ERK kinase 1 than ERK1/2 and B-Raf. Colony assay data further demonstrated that delphinidin 3-sambubioside inhibited 12-O- tetradecanoylphorbol-13-acetate-induced phosphorylation of MAPK/ERK kinase 1 and sequentially suppressed cell transformation. All of these effects caused by delphinidin 3-sambubioside were weaker than those by its aglycon, delphinidin. Our data suggested that the weaker anti- transformation activity of delphinidin glycosides compared to that of their aglycon is due to lower binding affinity to the target molecule MAPK/ERK kinase 1.

Supporting Information

 
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