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Int. J. Mol. Sci. 2017, 18(8), 1820; doi:10.3390/ijms18081820

GLUT10—Lacking in Arterial Tortuosity Syndrome—Is Localized to the Endoplasmic Reticulum of Human Fibroblasts

1
Department of Molecular and Developmental Medicine, University of Siena, 53100 Siena, Italy
2
Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1094 Budapest, Hungary
3
Division of Biology and Genetics, Department of Molecular and Translational Medicine, University of Brescia, 25123 Brescia, Italy
4
Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, 1111 Budapest, Hungary
5
Department of Biophysics and Radiation Biology, Semmelweis University, 1094 Budapest, Hungary
6
Center for Medical Genetics, Ghent University, B-9000 Ghent, Belgium
7
Institute of Clinical Experimental Research, Semmelweis University, 1094 Budapest, Hungary
The authors contributed equally to the work.
*
Authors to whom correspondence should be addressed.
Received: 28 July 2017 / Revised: 13 August 2017 / Accepted: 13 August 2017 / Published: 22 August 2017
(This article belongs to the Section Molecular Pathology, Diagnostics, and Therapeutics)
View Full-Text   |   Download PDF [3959 KB, uploaded 22 August 2017]   |  

Abstract

GLUT10 belongs to a family of transporters that catalyze the uptake of sugars/polyols by facilitated diffusion. Loss-of-function mutations in the SLC2A10 gene encoding GLUT10 are responsible for arterial tortuosity syndrome (ATS). Since subcellular distribution of the transporter is dubious, we aimed to clarify the localization of GLUT10. In silico GLUT10 localization prediction suggested its presence in the endoplasmic reticulum (ER). Immunoblotting showed the presence of GLUT10 protein in the microsomal, but not in mitochondrial fractions of human fibroblasts and liver tissue. An even cytosolic distribution with an intense perinuclear decoration of GLUT10 was demonstrated by immunofluorescence in human fibroblasts, whilst mitochondrial markers revealed a fully different decoration pattern. GLUT10 decoration was fully absent in fibroblasts from three ATS patients. Expression of exogenous, tagged GLUT10 in fibroblasts from an ATS patient revealed a strict co-localization with the ER marker protein disulfide isomerase (PDI). The results demonstrate that GLUT10 is present in the ER. View Full-Text
Keywords: GLUT10; arterial tortuosity syndrome; dehydroascorbic acid; endoplasmic reticulum; nuclear envelope; Fe2+/2-oxoglutarate dependent dehydrogenases GLUT10; arterial tortuosity syndrome; dehydroascorbic acid; endoplasmic reticulum; nuclear envelope; Fe2+/2-oxoglutarate dependent dehydrogenases
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Gamberucci, A.; Marcolongo, P.; Németh, C.E.; Zoppi, N.; Szarka, A.; Chiarelli, N.; Hegedűs, T.; Ritelli, M.; Carini, G.; Willaert, A.; Callewaert, B.L.; Coucke, P.J.; Benedetti, A.; Margittai, É.; Fulceri, R.; Bánhegyi, G.; Colombi, M. GLUT10—Lacking in Arterial Tortuosity Syndrome—Is Localized to the Endoplasmic Reticulum of Human Fibroblasts. Int. J. Mol. Sci. 2017, 18, 1820.

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