Journal of Lipid Research, Vol 31, 919-926, Copyright © 1990 by Lipid Research, Inc.
Purification and characterization of a protein inhibitor from rat liver that inhibits type 1 protein phosphatase when 3-hydroxy-3- methylglutaryl CoA reductase is the substrate
D Serra, G Asins and FG Hegardt
Unit of Biochemistry, University of Barcelona School of Pharmacy, Spain.
A protein inhibitor of HMG-CoA reductase phosphatase activity from rat
liver was purified to homogeneity. The protein was purified 4,000-fold with
an overall yield of 4%. The purified protein had a molecular mass of 31
kDa. This spontaneously active protein is thermostable and acid- resistant.
The protein inhibitor is phosphorylated by glycogen synthase kinase-3 and
cAMP-dependent protein kinase without change in its inhibitory activity.
The inhibition caused by this inhibitor on phosphatases 1 and 2A is similar
to that of inhibitor-2 from rabbit skeletal muscle using
hydroxymethylglutaryl-CoA reductase as substrate. The regulation properties
of this inhibitor towards phosphatase 1 together with another protein
inhibitor of phosphatase 2A in cholesterol metabolism are discussed.
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