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GLUT10 - lacking in arterial tortuosity syndrome - is localized to the endoplasmic reticulum of human fibroblasts

Alessandra Gamberucci, Paola Marcolongo, Csilla E Németh, Nicoletta Zoppi, András Szarka, Nicola Chiarelli, Tamás Hegedűs, Marco Ritelli, Giulia Carini, Andy Willaert (UGent) , et al.
(2017) INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 18(8).
Author
Organization
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.
Keywords
GLUT10, arterial tortuosity syndrome, dehydroascorbic acid, endoplasmic reticulum, nuclear envelope, Fe2+, 2-oxoglutarate dependent dehydrogenases, PREDICTING SUBCELLULAR-LOCALIZATION, TERMINAL TARGETING SEQUENCES, LIVER MICROSOMAL VESICLES, GLUCOSE-TRANSPORTER, OXIDATIVE STRESS, ACID TRANSPORT, ASCORBIC-ACID, GLUT10, MITOCHONDRIA, MUTATIONS

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MLA
Gamberucci, Alessandra, et al. “GLUT10 - Lacking in Arterial Tortuosity Syndrome - Is Localized to the Endoplasmic Reticulum of Human Fibroblasts.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 18, no. 8, 2017, doi:10.3390/ijms18081820.
APA
Gamberucci, A., Marcolongo, P., Németh, C. E., Zoppi, N., Szarka, A., Chiarelli, N., … Colombi, M. (2017). GLUT10 - lacking in arterial tortuosity syndrome - is localized to the endoplasmic reticulum of human fibroblasts. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 18(8). https://doi.org/10.3390/ijms18081820
Chicago author-date
Gamberucci, Alessandra, Paola Marcolongo, Csilla E Németh, Nicoletta Zoppi, András Szarka, Nicola Chiarelli, Tamás Hegedűs, et al. 2017. “GLUT10 - Lacking in Arterial Tortuosity Syndrome - Is Localized to the Endoplasmic Reticulum of Human Fibroblasts.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 18 (8). https://doi.org/10.3390/ijms18081820.
Chicago author-date (all authors)
Gamberucci, Alessandra, Paola Marcolongo, Csilla E Németh, Nicoletta Zoppi, András Szarka, Nicola Chiarelli, Tamás Hegedűs, Marco Ritelli, Giulia Carini, Andy Willaert, Bert Callewaert, Paul Coucke, Angiolo Benedetti, Éva Margittai, Rosella Fulceri, Gábor Bánhegyi, and Marina Colombi. 2017. “GLUT10 - Lacking in Arterial Tortuosity Syndrome - Is Localized to the Endoplasmic Reticulum of Human Fibroblasts.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 18 (8). doi:10.3390/ijms18081820.
Vancouver
1.
Gamberucci A, Marcolongo P, Németh CE, Zoppi N, Szarka A, Chiarelli N, et al. GLUT10 - lacking in arterial tortuosity syndrome - is localized to the endoplasmic reticulum of human fibroblasts. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2017;18(8).
IEEE
[1]
A. Gamberucci et al., “GLUT10 - lacking in arterial tortuosity syndrome - is localized to the endoplasmic reticulum of human fibroblasts,” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 18, no. 8, 2017.
@article{8529519,
  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.}},
  articleno    = {{1820}},
  author       = {{Gamberucci, Alessandra and Marcolongo, Paola and Németh, Csilla E and Zoppi, Nicoletta and Szarka, András and Chiarelli, Nicola and Hegedűs, Tamás and Ritelli, Marco and Carini, Giulia and Willaert, Andy and Callewaert, Bert and Coucke, Paul and Benedetti, Angiolo and Margittai, Éva and Fulceri, Rosella and Bánhegyi, Gábor and Colombi, Marina}},
  issn         = {{1422-0067}},
  journal      = {{INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}},
  keywords     = {{GLUT10,arterial tortuosity syndrome,dehydroascorbic acid,endoplasmic reticulum,nuclear envelope,Fe2+,2-oxoglutarate dependent dehydrogenases,PREDICTING SUBCELLULAR-LOCALIZATION,TERMINAL TARGETING SEQUENCES,LIVER MICROSOMAL VESICLES,GLUCOSE-TRANSPORTER,OXIDATIVE STRESS,ACID TRANSPORT,ASCORBIC-ACID,GLUT10,MITOCHONDRIA,MUTATIONS}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{12}},
  title        = {{GLUT10 - lacking in arterial tortuosity syndrome - is localized to the endoplasmic reticulum of human fibroblasts}},
  url          = {{http://doi.org/10.3390/ijms18081820}},
  volume       = {{18}},
  year         = {{2017}},
}
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