Data on SVCT2 transporter expression and localization in cancer cell lines and tissues

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Abstract

The data presented in this article are related to the research paper entitled “Increased expression of mitochondrial sodium-coupled ascorbic acid transporter-2 (mitSVCT2) as a central feature in breast cancer”, available in Free Radical Biology and Medicine Journal [1]. In this article, we examined the SVCT2 transporter expression in various breast cancer cell lines using RT-PCR and Western blot assays. In addition, we analyzed the subcellular localization of SVCT2 by immunofluorescence colocalization assays and cellular fractionation experiments. Finally, an analysis of different cancer tissue microarrays immunostained for SVCT2 and imaged by The Human Protein Atlas (https://www.proteinatlas.org) is presented.

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Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts.

Christian Frezza, Sara Cipolat, Luca Scorrano (2007)

Mitochondria participate in key metabolic reactions of the cell and regulate crucial signaling pathways including apoptosis. Although several approaches are available to study mitochondrial function in situ are available, investigating functional mitochondria that have been isolated from different tissues and from cultured cells offers still more unmatched advantages. This protocol illustrates a step-by-step procedure to obtain functional mitochondria with high yield from cells grown in culture, liver and muscle. The isolation procedures described here require 1-2 hours, depending on the source of the organelles. The polarographic analysis can be completed in 1 hour.

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Mitochondrial ascorbic acid transport is mediated by a low-affinity form of the sodium-coupled ascorbic acid transporter-2.

Carola Muñoz-Montesino, Francisco J Roa, Eduardo Peña … (2014)

Despite the fundamental importance of the redox metabolism of mitochondria under normal and pathological conditions, our knowledge regarding the transport of vitamin C across mitochondrial membranes remains far from complete. We report here that human HEK-293 cells express a mitochondrial low-affinity ascorbic acid transporter that molecularly corresponds to SVCT2, a member of the sodium-coupled ascorbic acid transporter family 2. The transporter SVCT1 is absent from HEK-293 cells. Confocal colocalization experiments with anti-SVCT2 and anti-organelle protein markers revealed that most of the SVCT2 immunoreactivity was associated with mitochondria, with minor colocalization at the endoplasmic reticulum and very low immunoreactivity at the plasma membrane. Immunoblotting of proteins extracted from highly purified mitochondrial fractions confirmed that SVCT2 protein was associated with mitochondria, and transport analysis revealed a sigmoidal ascorbic acid concentration curve with an apparent ascorbic acid transport Km of 0.6mM. Use of SVCT2 siRNA for silencing SVCT2 expression produced a major decrease in mitochondrial SVCT2 immunoreactivity, and immunoblotting revealed decreased SVCT2 protein expression by approximately 75%. Most importantly, the decreased protein expression was accompanied by a concomitant decrease in the mitochondrial ascorbic acid transport rate. Further studies using HEK-293 cells overexpressing SVCT2 at the plasma membrane revealed that the altered kinetic properties of mitochondrial SVCT2 are due to the ionic intracellular microenvironment (low in sodium and high in potassium), with potassium acting as a concentration-dependent inhibitor of SVCT2. We discarded the participation of two glucose transporters previously described as mitochondrial dehydroascorbic acid transporters; GLUT1 is absent from mitochondria and GLUT10 is not expressed in HEK-293 cells. Overall, our data indicate that intracellular SVCT2 is localized in mitochondria, is sensitive to an intracellular microenvironment low in sodium and high in potassium, and functions as a low-affinity ascorbic acid transporter. We propose that the mitochondrial localization of SVCT2 is a property shared across cells, tissues, and species.

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Increased expression of mitochondrial sodium-coupled ascorbic acid transporter-2 (mitSVCT2) as a central feature in breast cancer

Eduardo Peña, Francisco J Roa, Eveling Inostroza … (2019)

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Author and article information

Contributors

Carola Muñoz-Montesino

Coralia I. Rivas

Journal

Journal ID (nlm-ta): Data Brief

Journal ID (iso-abbrev): Data Brief

Title: Data in Brief

Publisher: Elsevier

ISSN (Electronic): 2352-3409

Publication date PMC-release: 06 May 2019

Publication date Collection: August 2019

Publication date (Electronic): 06 May 2019

Volume: 25

Electronic Location Identifier: 103972

Affiliations

[a ]Departamento de Fisiopatología, Facultad de Ciencias Biológicas, Universidad de Concepción, Barrio Universitario s/n, PO Box 160C, Concepción, Chile

[b ]Departamento de Especialidades Médicas, Facultad de Medicina, Universidad de Concepción, Barrio Universitario s/n, PO Box 160C, Concepción, Chile

[c ]Departamento de Fisiología, Facultad de Ciencias Biológicas, Universidad de Concepción, Barrio Universitario s/n, PO Box 160C, Concepción, Chile

[d ]Instituto de Bioquímica y Microbiología, Facultad de Ciencias, Universidad Austral de Chile, Campus Isla Teja, PO Box 567, Valdivia, Chile

Author notes

[∗ ]Corresponding author. corivas@ 123456udec.cl

[∗∗ ]Corresponding author. carmunozm@ 123456udec.cl

[1]

These authors contributed equally to this work.

Article

Publisher ID: S2352-3409(19)30325-7 Publisher ID: 103972

DOI: 10.1016/j.dib.2019.103972

PMC ID: 6586595

PubMed ID: 31249848

SO-VID: 1bff444e-9a68-443b-9af5-43a9127e8b26

License:

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

History

Date received : 16 March 2019

Date revision received : 12 April 2019

Date accepted : 26 April 2019

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Data on SVCT2 transporter expression and localization in cancer cell lines and tissues

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Cancer Immunotherapy

Most cited references 3

Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts.

Mitochondrial ascorbic acid transport is mediated by a low-affinity form of the sodium-coupled ascorbic acid transporter-2.

Increased expression of mitochondrial sodium-coupled ascorbic acid transporter-2 (mitSVCT2) as a central feature in breast cancer

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