KMID : 0624620090420120817
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BMB Reports 2009 Volume.42 No. 12 p.817 ~ p.822
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Regulation of type-1 protein phosphatase in a model of metabolic arrest
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Christopher J. Ramnanan
Kenneth B. Storey
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Abstract
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Type-1 phosphatase (PP-1) was assessed in foot muscle (FM) and hepatopancreas (HP) of estivating (EST) Otala lactea. Snail PP-1 displayed several conserved traits, including sensitivity to inhibitors, substrate affinity, and reduction in size to a 39 kDa catalytic subunit (PP-1c). During EST, PP-1 activity in FM and HP crude extracts was reduced, though kinetics and protein levels of purified PP-1c isoforms were not altered. PP-1c protein levels increased and decreased in nuclear and glycogen-associated fractions, respectively, during EST. Gel filtration determined that a 257 kDa low Km PP-1¥á complex decreased during estivation whereas a 76 kDa high Km complex increased in EST. Western blotting confirmed that the 76 kDa protein consisted of PP-1¥á and nuclear inhibitor of PP-1 (NIPP-1). A suppression of PP-1 activity factors in the overall metabolic rate depression in estivating snails and the mechanism is mediated through altered cellular localization and interaction with binding partners.
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KEYWORD
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Enzyme, Estivation, Metabolic rate depression, Protein phosphatase type-1, Purification
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