Identification of Alkylbenzene Sulfonate Surfactants Leaching from an Acrylonitrile Butadiene Rubber as Novel Inhibitors of Calcineurin Activity

Calcineurin (CN) is a Ca(2+)/calmodulin (CaM) dependent serine/threonine protein phosphatase and plays important role in several cellular functions in both higher and lower eukaryotes. Here we report inhibition of CN by linear alkylbenzene sulfonate. The clue to the finding was obtained while identi...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2013, Vol.77 (5), p.954-960
Main Authors: ITO, Noboru, SHIBUGUCHI, Nao, ISHIKAWA, Ryoki, TANAKA, Susumu, TOKITA, Yoshiharu, NAKAJIMA-SHIMADA, Junko, HOSAKA, Kohei
Format: Article
Language:English
Subjects:
Acrylonitrile - chemistry
acrylonitrile butadiene rubber
alkylbenzene sulfonates
Animals
Benzene - analysis
Benzene - chemistry
Benzene - isolation & purification
Benzene - pharmacology
Butadienes - chemistry
calcineurin
Calcineurin Inhibitors
Cattle
Drug Evaluation, Preclinical
Enzyme Inhibitors - analysis
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - isolation & purification
Enzyme Inhibitors - pharmacology
Ethanol - chemistry
inhibitors
Rubber - chemistry
Surface-Active Agents - analysis
Surface-Active Agents - chemistry
Surface-Active Agents - isolation & purification
Surface-Active Agents - pharmacology
surfactants
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Summary:Calcineurin (CN) is a Ca(2+)/calmodulin (CaM) dependent serine/threonine protein phosphatase and plays important role in several cellular functions in both higher and lower eukaryotes. Here we report inhibition of CN by linear alkylbenzene sulfonate. The clue to the finding was obtained while identifying the inhibitory material leaching from acrylonitrile butadiene rubber used for packing. Using standard dodecylbenzene sulfonate (C12-LAS), we obtained strong inhibition of CN with a half maximal inhibitory concentration of 9.3 µM, whereas analogs such as p-octylbenzene sulfonate and SDS hardly or only slightly affected CN activity. Three alkaline phosphatases, derived from shrimp, bacteria, and calf-intestine, which exhibit similar enzymatic activities to CN, were not inhibited by C12-LAS at concentrations of up to 100 µM. Furthermore, C12-LAS did not inhibit Ca(2+)/CaM-dependent myosin light chain kinase activity when tested at concentrations of up to 36 µM. The results indicate that C12-LAS is a potent selective inhibitor of CN activity.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.120902