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KMID : 0624620090420120817
BMB Reports
2009 Volume.42 No. 12 p.817 ~ p.822
Regulation of type-1 protein phosphatase in a model of metabolic arrest
Christopher J. Ramnanan

Kenneth B. Storey
Abstract
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.
KEYWORD
Enzyme, Estivation, Metabolic rate depression, Protein phosphatase type-1, Purification
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