Cloning, Purification, and Characterization of the Catalytic C-Terminal Domain of the Human 3-Hydroxy-3-methyl glutaryl-CoA Reductase: An Effective, Fast, and Easy Method for Testing Hypocholesterolemic Compounds.


Journal

Molecular biotechnology
ISSN: 1559-0305
Titre abrégé: Mol Biotechnol
Pays: Switzerland
ID NLM: 9423533

Informations de publication

Date de publication:
Feb 2020
Historique:
pubmed: 24 11 2019
medline: 10 6 2020
entrez: 24 11 2019
Statut: ppublish

Résumé

3-hydroxy-3-methyl glutaryl-CoA reductase, also known as HMGR, plays a crucial role in regulating cholesterol biosynthesis and represents the main pharmacological target of statins. In mammals, this enzyme localizes to the endoplasmic reticulum membrane. HMGR includes different regions, an integral N-terminal domain connected by a linker-region to a cytosolic C-terminal domain, the latter being responsible for enzymatic activity. The aim of this work was to design a simple strategy for cloning, expression, and purification of the catalytic C-terminal domain of the human HMGR (cf-HMGR), in order to spectrophotometrically test its enzymatic activity. The recombinant cf-HMGR protein was heterologously expressed in Escherichia coli, purified by Ni

Identifiants

pubmed: 31758489
doi: 10.1007/s12033-019-00230-1
pii: 10.1007/s12033-019-00230-1
doi:

Substances chimiques

Hydroxymethylglutaryl-CoA Reductase Inhibitors 0
Recombinant Proteins 0
Hydroxymethylglutaryl CoA Reductases EC 1.1.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

119-131

Subventions

Organisme : Associazione Italiana per la Ricerca sul Cancro
ID : 15404/2014

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Auteurs

Rosita Curcio (R)

Department of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.

Donatella Aiello (D)

Department of Chemistry and Chemical Technologies, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.

Angelo Vozza (A)

Laboratory of Biochemistry and Molecular Biology, Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70125, Bari, Italy.

Luigina Muto (L)

Department of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.

Emanuela Martello (E)

Department of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.

Anna Rita Cappello (AR)

Department of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.

Loredana Capobianco (L)

Department of Biological and Environmental Sciences and Technologies, University of Salento, 73100, Lecce, Italy.

Giuseppe Fiermonte (G)

Laboratory of Biochemistry and Molecular Biology, Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, 70125, Bari, Italy.

Carlo Siciliano (C)

Department of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy.

Anna Napoli (A)

Department of Chemistry and Chemical Technologies, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy. amc.napoli@unical.it.

Vincenza Dolce (V)

Department of Pharmacy, Health, and Nutritional Sciences, University of Calabria, 87036, Arcavacata di Rende, Cosenza, Italy. vincenza.dolce@unical.it.

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Classifications MeSH