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Article

Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli

by
Lara Console
1,
Maria Tolomeo
2,
Matilde Colella
2,
Maria Barile
2,* and
Cesare Indiveri
1,*
1
Department DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via P. Bucci 4C, 87036 Arcavacata di Rende, Italy
2
Department of Biosciences, Biotechnology and Biopharmaceutics, University of Bari, via Orabona 4, 70126 Bari, Italy
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(18), 4416; https://doi.org/10.3390/ijms20184416
Submission received: 1 August 2019 / Revised: 3 September 2019 / Accepted: 6 September 2019 / Published: 8 September 2019
(This article belongs to the Special Issue Flavin Adenine Dinucleotide (FAD): Biosynthesis and Function)
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Abstract

Background: the SLC52A2 gene encodes for the riboflavin transporter 2 (RFVT2). This transporter is ubiquitously expressed. It mediates the transport of Riboflavin across cell membranes. Riboflavin plays a crucial role in cells since its biologically active forms, FMN and FAD, are essential for the metabolism of carbohydrates, amino acids, and lipids. Mutation of the Riboflavin transporters is a risk factor for anemia, cancer, cardiovascular disease, neurodegeneration. Inborn mutations of SLC52A2 are associated with Brown-Vialetto-van Laere syndrome, a rare neurological disorder characterized by infancy onset. In spite of the important metabolic and physio/pathological role of this transporter few data are available on its function and regulation. Methods: the human recombinant RFVT2 has been overexpressed in E. coli, purified and reconstituted into proteoliposomes in order to characterize its activity following the [3H]Riboflavin transport. Results: the recombinant hRFVT2 showed a Km of 0.26 ± 0.07 µM and was inhibited by lumiflavin, FMN and Mg2+. The Riboflavin uptake was also regulated by Ca2+. The native protein extracted from fibroblast and reconstituted in proteoliposomes also showed inhibition by FMN and lumiflavin. Conclusions: proteoliposomes represent a suitable model to assay the RFVT2 function. It will be useful for screening the mutation of RFVT2.
Keywords: riboflavin; transport; proteoliposomes; SLC; FMN riboflavin; transport; proteoliposomes; SLC; FMN

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MDPI and ACS Style

Console, L.; Tolomeo, M.; Colella, M.; Barile, M.; Indiveri, C. Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli. Int. J. Mol. Sci. 2019, 20, 4416. https://doi.org/10.3390/ijms20184416

AMA Style

Console L, Tolomeo M, Colella M, Barile M, Indiveri C. Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli. International Journal of Molecular Sciences. 2019; 20(18):4416. https://doi.org/10.3390/ijms20184416

Chicago/Turabian Style

Console, Lara, Maria Tolomeo, Matilde Colella, Maria Barile, and Cesare Indiveri. 2019. "Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli" International Journal of Molecular Sciences 20, no. 18: 4416. https://doi.org/10.3390/ijms20184416

APA Style

Console, L., Tolomeo, M., Colella, M., Barile, M., & Indiveri, C. (2019). Reconstitution in Proteoliposomes of the Recombinant Human Riboflavin Transporter 2 (SLC52A2) Overexpressed in E. coli. International Journal of Molecular Sciences, 20(18), 4416. https://doi.org/10.3390/ijms20184416

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