Purification and characterization of fermodulin, an Fe2+-dependent inhibitor protein of 3-hydroxy-3-methylglutaryl-CoA reductase

Menon, A.Satish; Devi, Susheela; Ramasarma, T.

doi:10.1016/0003-9861(85)90697-6

Cited by 6 publications

(2 citation statements)

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“…We described another type of inhibition which required hemin and oxygen (but not its radicals) [36] in which inactivation is obtained by oxidation of protein-thiols to an internal disulfide. Rapid inactivation was also achieved in the presence of ferrous ions and a cytosolic 58 kDa-protein, fermodulfi~ [37]. All these examples refer to modification of the protein in the active site domain by phosphorylation, oxidation of cysteine-sulfhydryl groups or by protein-protein interaction.…”

Section: Many Hypocholesterolemic Agents Which Inhibitmentioning

confidence: 96%

Preparation of a soluble 58kDa-3-hydroxy-3-methylglutaryl CoA reductase from liver microsomes and its inhibition by ethoxysilatrane, a hypocholesterolemic compound

et al. 1992

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On repeated thawing at room temperature of frozen preparations of heavy microsomes from rat livers, HMGCoA reductase activity was solubilized due to limited proteolysis. This soluble enzyme was partially purified by fractionation with ammonium sulfate and filtration on Sephacryl S-200 column. The active enzyme was coeluted with a major 92 kDa-protein and was identified as a 58 kDa-protein after separation by SDS-PAGE and immunoblotting. Ethoxysilatrane, a hypocholesterolemic compound, which decreased the liver-microsomal activity of HMGCoA reductase on intra-peritonial treatment of animals, showed little effect on the enzyme activity with isolated microsomes or the 50 kDa-soluble enzyme when added in the assay. But it was able to inhibit the activity of the soluble 58 kDa-enzyme in a concentration-dependent, reversible manner. Cholesterol and an oxycholesterol were without effect whereas chlorophenoxyisobutyrate and ubiquinone showed small inhibition under these conditions. The extra region that links the active site domain (50 kDa protein) to the membrane, present in the 58 kDa-protein appears to be involved in mediating the inhibition by silatrane.

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Section: Many Hypocholesterolemic Agents Which Inhibitmentioning

confidence: 96%

Preparation of a soluble 58kDa-3-hydroxy-3-methylglutaryl CoA reductase from liver microsomes and its inhibition by ethoxysilatrane, a hypocholesterolemic compound

et al. 1992

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“…Hepcidin (encoded by HAMP) is the Fe-dependent inhibitor protein of rat liver microsomal 3-hydroxy-3-methylglutaryl-CoA (HMGCoA) reductase, which interacts with Fe ( 21 ). HMGCoA reductase activity was inhibited by the addition of FeSO 4 and the cytosolic protein hepcidin ( 22 ). Occasionally, hepcidin is the key factor that regulates iron balance, and the JAK/STAT3 signal pathway regulates its expression.…”

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confidence: 99%

The Effect of STAT3 Signal Pathway Activation on Retinopathy of Prematurity

Ren

Jiang

et al. 2021

Front. Pediatr.

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Objective: To investigate the mechanism of activation of the signal transducer and activator of transcription 3 (STAT3) signal pathway in the process of retinopathy of prematurity (ROP).Methods: Sixty newborn Sprague-Dawley (SD) rats were randomly separated into the hyperoxia and air control groups (n = 30/in each group). The serum hepcidin level on 21 d was measured using the enzyme-linked immunosorbent assay (ELISA). The expression of HAMP and STAT3 protein in the liver was determined using reverse transcription-polymerase chain reaction (RT-PCR) and western blotting. Retinal neovasculature was evaluated by hematoxylin and eosin (HE) stain and fluorescein lectin. The retinal endothelial cells were treated with 250 μmol/L cobalt chloride for 72 h and added S3I-201. The STAT3 level was determined by western blotting.Results: The expression of STAT3 protein increased significantly after hyperoxia stimulation. The expression of HAMP mRNA in the hyperoxia group was significantly higher than that of the control group. The proliferation of retinal cells was inhibited, and the expression of STAT3 was increased. No significant difference was noted in vascular endothelial growth factor (VEGF) mRNA. The expression of STAT3 and VEGF mRNA was significantly reduced.Conclusion: The activation of the STAT3 signal pathway increased hepcidin expression, contributing to the pathogenesis of ROP. S3I-201 inhibited the expression of STAT3 and VEGF mRNA levels. This information provides potential novel therapeutic approach to the prevention and treatment of ROP.

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Mevalonate-metabolizing enzymes in Arachis hypogaea

1989

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The activities of the mevalonate metabolizing enzymes-HMG-CoA reductase, mevalonate kinase, mevalonate phosphokinase and mevalonate pyrophosphate decarboxylase -were assayed with the respective substrates in green seedlings of Arachis hypogaea. MVAPP decarboxylase is the rate-limiting step among these enzymes and is inhibited by phenolic acids. Its activity in the seedlings was found to decrease in the absence of light and on treatment with abscisic acid. These results suggest that regulation of isoprene pathway in groundnut seedlings may occur at the level of mevalonate decarboxylation.

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Purification and characterization of fermodulin, an Fe2+-dependent inhibitor protein of 3-hydroxy-3-methylglutaryl-CoA reductase

Cited by 6 publications

References 25 publications

Preparation of a soluble 58kDa-3-hydroxy-3-methylglutaryl CoA reductase from liver microsomes and its inhibition by ethoxysilatrane, a hypocholesterolemic compound

Preparation of a soluble 58kDa-3-hydroxy-3-methylglutaryl CoA reductase from liver microsomes and its inhibition by ethoxysilatrane, a hypocholesterolemic compound

The Effect of STAT3 Signal Pathway Activation on Retinopathy of Prematurity

Mevalonate-metabolizing enzymes in Arachis hypogaea

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