期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 18, 期 21, 页码 7607-7610出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2010.08.043
关键词
Okadaic acid; Okadaic acid binding protein; Binding; Cytotoxicity
资金
- MEXT, Japan [21603003]
- Naito Science and Engineering Foundation
- Novartis Foundation
- Grants-in-Aid for Scientific Research [21603003] Funding Source: KAKEN
Okadaic acid (OA) and dinophysistoxin-1 (DTX1) cause diarrheic shellfish poisoning. This article examines the biochemical interactions of the two toxins with novel okadaic acid binding proteins (OABPs) 2.1 and 2.3, originally isolated from the marine sponge Halichondria okadai. First, recombinant OABPs 2.1 and 2.3 were expressed in Escherichia coli BL21 (DE3) cells. Binding assays using [24-(3)H] OA and the recombinant OABP 2.1 or 2.3 demonstrated the dissociation constant K(d) of 1.30 +/- 0.56 nM and 1.54 +/- 0.35 nM, respectively. Binding of [24-(3)H] okadaic acid to recombinant OABP2.1 was almost equally replaced with OA and DTX1. OA-induced cytotoxicity in mouse leukemia P388 cells was inhibited in the presence of the recombinant OABPs 2.1 and 2.3 with an EC(50) of 92 +/- 8.4 nM and 87 +/- 13 nM, respectively. These results suggest that the blockage of OA-induced cytotoxicity by OABPs 2.1 and 2.3 may be involved in regulating symbiotic relationships present in the sponge H. okadai. (C) 2010 Elsevier Ltd. All rights reserved.
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