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ATP-dependent degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in permeabilized cells

Leonard, D A ; Chen, H W

The Journal of biological chemistry, 1987-06, Vol.262 (16), p.7914-7919 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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Título:
ATP-dependent degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in permeabilized cells
Autor: Leonard, D A ; Chen, H W
Assuntos: Adenosine Triphosphate - pharmacology ; Alkaline Phosphatase - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; ATP ; Biological and medical sciences ; Cell Line ; Cell Membrane Permeability ; CHO cells ; endoplasmic reticulum ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydroxymethylglutaryl CoA Reductases - metabolism ; hydroxymethylglutaryl-CoA reductase (NADPH) ; Kinetics ; Oxidoreductases
É parte de: The Journal of biological chemistry, 1987-06, Vol.262 (16), p.7914-7919
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
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Descrição: A system for the assay of 3-hydroxy-3-methyglutaryl (HMG) coenzyme A (CoA) reductase in digitonin-permeabilized Chinese hamster ovary cells is described. Under these conditions, HMG-CoA reductase remained intact and associated with the endoplasmic reticulum, and values for Km (HMG-CoA), Ki (mevinolin), and active/total activity were similar to those seen in sonicated cell preparations. However, the mechanism by which this rapidly turned over (half-life approximately 2 h) enzyme is degraded was disrupted. Addition of ATP at physiological concentrations to digitonin-permeabilized cells resulted in the rapid, irreversible loss of enzyme activity. Immunoblot analysis showed that this loss of activity was followed by cleavage of the intact 97-kilodalton enzyme to a 68-kilodalton fragment which was distinct from the catalytically active fragments generated by nonspecific proteolysis in sonicated cell homogenates. Assay of a lysosomal marker enzyme confirmed that ATP-mediated inactivation and cleavage of reductase was not due to release of lysosomal proteases. The possible role of ATP in phosphorylation, inactivation, and degradation of reductase is discussed.
Editor: Bethesda, MD: Elsevier Inc
Idioma: Inglês

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ATP-dependent degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in permeabilized cells

Leonard, D A ; Chen, H W

Bethesda, MD: Elsevier Inc

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