Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and with protein fractions of rat liver cytosol

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Abstract

3-Hydroxy-3-methylglutaryl coenzyme A reductase activity is diminished in several in vitro liver systems preincubated in the presence of cAMP. Reductase activity in isolated, washed liver microsomes is inactivated by ATP, Mg++, and a protein fraction separated from the liver cytosol. This effect is augmented by 3′–5′ cyclic AMP. Reductase activity in previously inactivated microsomes can be partially restored by incubation with a second protein fraction of the cytosol.

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  • Regulation of podocytes function by AMP-activated protein kinase

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    Citation Excerpt :

    Extensive research has been conducted on the role and function of AMP-activated protein kinase (AMPK) since its discovery in 1973. In parallel studies, Carlson & Kim and Beg et al. described AMPK as different soluble protein factors that, on one hand, inactivated acetyl-CoA carboxylase, which was proposed to be due to a direct phosphorylation [1], and on the other hand, inhibited 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase [2]. Finally, in 1987, it was shown that the activities of these two enzymes were regulated by the same protein, which was called AMPK [3].

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Research supported by grants from the N.H.L.I. (HL-0419-15); the American Heart Association (70-680); and the Indiana Heart Association.

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