GLUT10 deficiency leads to oxidative stress and non-canonical αvβ3 integrin-mediated TGFβ signalling associated with extracellular matrix disarray in arterial tortuosity syndrome skin fibroblasts
Open accessAbstract
Arterial tortuosity syndrome (ATS) is an autosomal recessive connective tissue disorder caused by loss-of-function mutations in SLC2A10, which encodes facilitative glucose transporter 10 (GLUT10). The role of GLUT10 in ATS pathogenesis remains an enigma, and the transported metabolite(s), i.e. glucose and/or dehydroascorbic acid, have not been clearly elucidated. To discern the molecular mechanisms underlying the ATS aetiology, we performed gene expression profiling and biochemical studies on skin fibroblasts. Transcriptome analyses revealed the dysregulation of several genes involved in TGFβ signalling and extracellular matrix (ECM) homeostasis as well as the perturbation of specific pathways that control both the cell energy balance and the oxidative stress response. Biochemical and functional studies showed a marked increase in ROS-induced lipid peroxidation sustained by altered PPARγ function, which contributes to the redox imbalance and the compensatory antioxidant activity of ALDH1A1. ATS fibroblasts also showed activation of a non-canonical TGFβ signalling due to TGFBRI disorganization, the upregulation of TGFBRII and connective tissue growth factor, and the activation of the αvβ3 integrin transduction pathway, which involves p125FAK, p60Src and p38 MAPK. Stable GLUT10 expression in patients' fibroblasts normalized redox homeostasis and PPARγ activity, rescued canonical TGFβ signalling and induced partial ECM re-organization. These data add new insights into the ATS dysregulated biological pathways and definition of the pathomechanisms involved in this disorder.
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More than 90% of cEDS patients harbor a heterozygous mutation in one of the genes encoding type V collagen (COL5A1 and COL5A2).
“Morethan 90% of cEDS patients harbor a heterozygous mutation in one of the genes encoding type V collagen ( COL5A1 and COL5A2 ) [Symoens et al., 2012; Ritelli et al., 2013; Zoppi et al., 2015]”
From The 2017 international classification of the Ehlers–Danlos syndromes (2017) · cites this paper as Zoppi et al., 2015
The Materials and Methods section describes patients with arterial tortuosity syndrome and SLC2A10 mutations, while the Results discuss type V collagen organization in their fibroblasts. Searches for cEDS, COL5A1/COL5A2, and the >90% figure found no passage addressing the claimed mutation frequency in cEDS patients. Page numbers were not available in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredOur protein data indicated the disorganization of the core proteins of PGs perlecan, versican, and DCN, and their abnormal organization could contribute to the defective COLLIII fibril assembly in vEDS cells, as well as to the defective fibrillogenesis of other COLLs.
“Our protein data indicated the disorganization of the core proteins of PGs perlecan, versican, and DCN, which enhance COLL fibril formation [26], and their abnormal organization could contribute to the defective COLLIII fibril assembly in vEDS cells, as well as to the defective fibrillogenesis of other COLLs previously described in skin fibroblasts of different EDS types and in other connective”
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“Twenty-three SLC2A10 genemutations have been reported (8).”
Self-citationTwo novel SLC2A10/GLUT10 mutations in a patient with arterial tortuosity syndrome
Drera, B. A., Guala, A., Zoppi, N., Gardella, R., Franceschini, P., Barlati, S., & Colombi, M. (2006) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.31514 · Cited by 34 · cited 1× · see citing works
“All of the three ATS patients were previously characterized for three different mutations in the SLC2A10 gene (3,4,7).”
Self-citationAbsence of arterial phenotype in mice with homozygous slc2A10 missense substitutions
Callewaert, B. L., Loeys, B., Casteleyn, C. R., Willaert, A., Dewint, P., Backer, J. F. A. D., Sedlmeier, R., Simoens, P., Paepe, A. M. D., & Coucke, P. J. (2008) · genesis · doi:10.1002/dvg.20409 · Cited by 32 · see citing works
FAK-independent αvβ3 integrin-EGFR complexes rescue from anoikis matrix-defective fibroblasts
Zoppi, N., Barlati, S., & Colombi, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.03.003 · Cited by 31 · cited 3× · see citing works
“A cell survival role for αvβ3 integrin was reported in Ehlers-Danlos syndrome skin fibroblasts, wherein this receptor rescues the cells from apoptosis induced by ECM disassembly due to COL5A1 and COL3A1 mutations (58,59).”
Self-citationCastori, M., Ritelli, M., Zoppi, N., Molisso, L., Chiarelli, N., Zaccagna, F., Grammatico, P., & Colombi, M. (2012) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.35266 · Cited by 30 · cited 2× · see citing works
“Val430_Ile470del) (7); patient 3 (P3) was compound heterozygous for the c.”
Self-citationTall, E. G., Bernstein, A. M., Oliver, N., Gray, J., & Masur, S. K. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-5110 · Cited by 28 · cited 2× · see citing works
“in 1% BSA and immunoreacted for 1 h at room temperature (RT) with 1:50 anti-CTGFAb (34).”
Larroque-Cardoso, P., Mucher, E., Grazide, M.-H., Josse, G., Schmitt, A.-M., Nadal-Wollbold, F., Žarković, K., Salvayre, R., & Nègre‐Salvayre, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.015 · Cited by 28 · cited 1× · see citing works
“Recently, impairment of the TGFβ pathway by oxidative exposure of human skin fibroblasts has been reported (70), and inhibition of TGFβ signalling by 4-HNE, which triggers ELN assembly in the ECM, was reported in oxidative stress-associated aging using human skin fibroblasts (71).”
Arterial tortuosity syndrome in two Italian paediatric patients
Ritelli, M., Drera, B. A., Vicchio, M., Puppini, G., Biban, P., Pilati, M., Prioli, M. A., Barlati, S., & Colombi, M. (2009) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-4-20 · Cited by 25 · see citing works
Self-citationA sweet link between TGFβ and vascular disease?
Akhurst, R. J. (2006) · Nature Genetics · doi:10.1038/ng0406-400 · Cited by 22 · see citing works
Peroxisome proliferator-activated receptors and the vascular system: beyond their metabolic effects
Marchesi, C., & Schiffrin, E. L. (2008) · Journal of the American Society of Hypertension · doi:10.1016/j.jash.2007.12.007 · Cited by 15 · cited 3× · see citing works
“PPARγ also regulates lipid and glucidic metabolism (27); therefore, in ATS cells, the increased PPARγ may be involved in upregulating genes related to peroxisomal β-oxidation and PUFA metabolism, as shown in the array.”
InfluentialIn silico aided thoughts on mitochondrial vitamin C transport
Szarka, A., & Balogh, T. (2014) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2014.10.015 · Cited by 15 · cited 1× · see citing works
“Despite these findings, a recent study suggested that GLUT10 is not likely to be present in mitochondria because this transporter got far the lowest mitochondrial localization scores using in silico prediction tools (20).”
Ahn, H.-H., Oh, Y., Lee, H., Lee, W., Chang, J.-W., Pyo, H.-K., Nah, D. H., & Jung, Y. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.018 · Cited by 13 · see citing works
[MicroRNAs expression in normal and dissected aortic tissue].
Hu, Z.-Y., Luo, J., Zhong, S., Xue, L., Chen, Y., & Fan, R. (2012) · PubMed · Cited by 11 · see citing works
Chiarelli, N., Ritelli, M., Zoppi, N., Benini, A., Borsani, G., Barlati, S., & Colombi, M. (2011) · The International Journal of Developmental Biology · doi:10.1387/ijdb.103179nc · Cited by 11 · cited 1× · see citing works
“The zebrafish model better highlighted the essential role of GLUT10 in cardiovascular development because knockdown of the slc2a10 orthologue, which is broadly expressed during embryogenesis (13), was associated with several cardiovascular defects (14).”
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
The 2017 international classification of the Ehlers–Danlos syndromes
Malfait, F., Francomano, C., Byers, P., Belmont, J., Berglund, B., Black, J., Bloom, L., Bowen, J. M., Brady, A. F., Burrows, N. P., et al. (2017) · American Journal of Medical Genetics Part C: Seminars in Medical Genetics · doi:10.1002/ajmg.c.31552 · Cited by 1,936 · see citing works
“• Molecular basis More than 90% of cEDS patients harbor a heterozygous mutation in one of the genes encoding type V collagen (COL5A1 and COL5A2) [Symoens et al., 2012; Ritelli et al., 2013; Zoppi et al., 2015] (see also “Ehlers–Danlos Syndrome, Classical Type,” by Bowen et al., this issue).”
BackgroundSelf-citationGenes Associated with Thoracic Aortic Aneurysm and Dissection: 2018 Update and Clinical Implications
Brownstein, A. J., Kostiuk, V., Ziganshin, B. A., Zafar, M. A., Kuivaniemi, H., Body, S. C., Bale, A. E., & Elefteriades, J. A. (2018) · Aorta · doi:10.1055/s-0038-1639612 · Cited by 179 · see citing works
Liu, Y., Wang, F., Peng, D., Zhang, D., Liu, L., Wei, J., Yuan, J., Zhao, L., Jiang, H., Zhang, T., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adk7399 · Cited by 115 · see citing works
“Previous studies have shown that GLUT10 facilitated the transport of dehydro-ascorbic acid into mitochondria to maintain cellular redox homeostasis ( 28 , 29 ).”
BackgroundGenes Associated with Thoracic Aortic Aneurysm and Dissection
Brownstein, A. J., Ziganshin, B. A., Kuivaniemi, H., Body, S. C., Bale, A. E., & Elefteriades, J. A. (2017) · Aorta · doi:10.12945/j.aorta.2017.17.003 · Cited by 112 · see citing works
Genes Associated with Thoracic Aortic Aneurysm and Dissection: 2019 Update and Clinical Implications
Vinholo, T. F., Brownstein, A. J., Ziganshin, B. A., Zafar, M. A., Kuivaniemi, H., Body, S. C., Bale, A. E., & Elefteriades, J. A. (2019) · Aorta · doi:10.1055/s-0039-3400233 · Cited by 86 · see citing works
Glucose Transport and Transporters in the Endomembranes
Lizák, B., Szarka, A., Kim, Y., Choi, K.-S., Németh, C. E., Marcolongo, P., Benedetti, A., Bánhegyi, G., & Margittai, É. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235898 · Cited by 84 · see citing works
The pathobiology of vascular malformations: insights from human and model organism genetics
Wetzel‐Strong, S. E., Detter, M. R., & Marchuk, D. A. (2016) · The Journal of Pathology · doi:10.1002/path.4844 · Cited by 83 · see citing works
“As described below, inactivation of SLC2A10 appears to increase cellular oxidative stress, ultimately resulting in TGF-β signalling via αvβ3-dependent mechanisms [126].”
BackgroundInfluentialChiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82 · see citing works
Self-citationChiarelli, N., Carini, G., Zoppi, N., Dordoni, C., Ritelli, M., Venturini, M., Castori, M., & Colombi, M. (2016) · PLOS ONE · doi:10.1371/journal.pone.0161347 · Cited by 78 · see citing works
“To analyze FBNs and ELN organization into ECM, cells were fixed immunoreacted as described previously [15].”
MethodSelf-citationArterial dissections: Common features and new perspectives
Bax, M., Romanov, V., Junday, K., Giannoulatou, E., Martinac, B., Kovacic, J. C., Liu, R., Iismaa, S. E., & Graham, R. M. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1055862 · Cited by 48 · see citing works
“Variants in SLC2A10 lead to a decreased density of Glut10 transporters, which causes ECM disarray and subsequent inappropriate TGF-β signaling, as well as oxidative stress (154).”
BackgroundChiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2018) · PLOS ONE · doi:10.1371/journal.pone.0191220 · Cited by 45 · see citing works
Self-citationEgea, G., Jiménez-Altayó, F., & Campuzano, V. (2020) · Antioxidants · doi:10.3390/antiox9101013 · Cited by 36 · see citing works
“The rescue of normal GLUT10 expression normalized redox homeostasis, PPARγ activity, and TGF-β signaling, accompanied by partial ECM reorganization [273].”
BackgroundMarfan Syndrome: Enhanced Diagnostic Tools and Follow-up Management Strategies
Marelli, S., Micaglio, E., Taurino, J., Salvi, P., Rurali, E., Perrucci, G. L., Dolci, C., Udugampolage, N. S., Caruso, R., Gentilini, D., et al. (2023) · Diagnostics · doi:10.3390/diagnostics13132284 · Cited by 46 · see citing works
“Arterial tortuosity syndrome also shows additional signs shared with other connectivopathies, including soft/velvety/hyper extensible skin, mild dysmorphic facial features (hypertelorism, high palate, bifid uvula, micrognathia), hernias and joint hypermobility and instability [92].”
BackgroundZoppi, N., Chiarelli, N., Ritelli, M., & Colombi, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040982 · Cited by 37 · see citing works
“The exact pathomechanisms by which GLUT10 deficiency leads to the generalized ECM disarray, which reflects not only the typical ATS vascular anomalies but also the multisystem involvement overlapping with EDSs [171], were debated for long time and remain incompletely explored [98,99,105,115,116,172].”
BackgroundInfluentialSelf-citationChiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2019) · PLOS ONE · doi:10.1371/journal.pone.0211647 · Cited by 35 · see citing works
Self-citationLi, Y., Zhou, H., Bi, R., Li, X., Zha, M., Yang, Y., Ni, J., Liew, W. H., Olivo, M., Yao, K., et al. (2021) · Journal of Materials Chemistry B · doi:10.1039/d1tb02282b · Cited by 31 · see citing works
Németh, C. E., Marcolongo, P., Gamberucci, A., Fulceri, R., Benedetti, A., Zoppi, N., Ritelli, M., Chiarelli, N., Colombi, M., Willaert, A., et al. (2016) · FEBS Letters · doi:10.1002/1873-3468.12204 · Cited by 30 · see citing works
Self-citationConte, F., Sam, J.-E. S. J. B. , Lefeber, D. J., & Passier, R. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108632 · Cited by 29 · see citing works
Syu, Y.-W., Lai, H.-W., Jiang, C., Tsai, H., Lin, C., & Lee, Y. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx401 · Cited by 25 · see citing works
“Recent studies showed DHA transport is defective in the endomembranes of fibroblasts from ATS patients (22).”
Analysis on the desert adaptability of indigenous sheep in the southern edge of Taklimakan Desert
Zhang, C.-L., Liu, C., Zhang, J., Zheng, L., Chang, Q., Cui, Z., & Liu, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-15986-x · Cited by 21 · see citing works
Arterial Tortuosity Syndrome: An Ascorbate Compartmentalization Disorder?
Boel, A., Veszelyi, K., Németh, C. E., Beyens, A., Willaert, A., Coucke, P. J., Callewaert, B. L., & Margittai, É. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7843 · Cited by 20 · see citing works
Jiang, C., Jen, W., Tsao, C.-Y., Chang, L.-C., Chen, C.-H., & Lee, Y. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008823 · Cited by 18 · see citing works
Gamberucci, A., Marcolongo, P., Németh, C. E., Zoppi, N., Szarka, A., Chiarelli, N., Hegedűs, T., Ritelli, M., Carini, G., Willaert, A., et al. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081820 · Cited by 17 · see citing works
“Ten nanograms of the pG10 expression vector [5,18] were used as PCR template to amplify the full-length coding sequence of SLC2A10, from the Kozak consensus sequence to the last amino acid codon.”
BackgroundMethodResultInfluentialSelf-citationGestational exposure to air pollutants perturbs metabolic and placenta-fetal phenotype
Ganguly, A., Ghosh, S., Shin, B., Touma, M., Wadehra, M., & Devaskar, S. U. (2024) · Reproductive Toxicology · doi:10.1016/j.reprotox.2024.108657 · Cited by 15 · see citing works
Boel, A., Burger, J. E., Vanhomwegen, M., Beyens, A., Renard, M., Barnhoorn, S., Casteleyn, C. R., Reinhardt, D. P., Descamps, B., Vanhove, C., et al. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa071 · Cited by 12 · see citing works
Jian, L., Wu, Q., Min, X., Li, B., Zhang, M., Wu, Z., Hu, X., Ren, Z., Wang, Z., & Hu, Z. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e13836 · Cited by 11 · see citing works
“Previous studies have confirmed that GLUT10 is involved in oxidative stress, vitamin C transportation, extracellular matrix degradation and TNF-β signal transduction [24,25].”
BackgroundThoracic aortic aneurysm gene dictionary
Rohde, S. C., Zafar, M. A., Ziganshin, B. A., & Elefteriades, J. A. (2020) · Asian Cardiovascular and Thoracic Annals · doi:10.1177/0218492320943800 · Cited by 11 · see citing works
Jacinto, J. G. P., Häfliger, I. M., Veiga, I. B., Letko, A., Benazzi, C., Bolcato, M., & Drögemüller, C. (2020) · Animals · doi:10.3390/ani10112002 · Cited by 11 · see citing works
“COLLV is thought to regulate the diameter of these fibrils by retention of its large N-propeptide domain, which projects above the surface of the collagen fibril [35].”
BackgroundInfluentialAragoneses-Cazorla, G., Vallet‐Regí, M., Gómez-Gómez, M. M., González, B., & Luque-Garcia, J. L. (2023) · Microchimica Acta · doi:10.1007/s00604-023-05712-3 · Cited by 10 · see citing works
Giatti, S., Cioffi, L., Diviccaro, S., Chrostek, G., Piazza, R., & Melcangi, R. C. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04592-9 · Cited by 10 · see citing works
Clinical variability in two Macedonian families with Arterial tortuosity syndrome
Kočova, M., Kacarska, R., Kuzevska-Maneva, K., Prijić, S., Lazareska, M., Dordoni, C., Ritelli, M., & Colombi, M. (2018) · Balkan Journal of Medical Genetics · doi:10.2478/bjmg-2018-0009 · Cited by 9 · see citing works
“extracellular matrix proteins both at epigenetic and posttranslational levels [4,5].”
BackgroundSelf-citationDong, J., Wang, F., Gao, X., Zhao, H., Zhang, J., Wang, N., Liu, Z., Yan, X., Jin, J., Ba, Y., et al. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2022.977251 · Cited by 8 · see citing works
Wu, Q., Hu, Z., Wang, Z., Che, Y., Zhang, M., Zheng, S., Xing, K., Zhong, X., Chen, Y., Shi, F., et al. (2023) · Translational research · doi:10.1016/j.trsl.2023.05.001 · Cited by 7 · see citing works
Németh, C. E., Nemoda, Z., Lőw, P., Szabó, P. T., Horvath, E. Z., Willaert, A., Boel, A., Callewaert, B. L., Coucke, P. J., Colombi, M., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8156592 · Cited by 6 · see citing works
“Dysregulation of the PPAR-γ-TGF-β pathway has been reported in fibroblasts from ATS patients [41].”
Self-citationPiccinelli, S. C., Premi, E., Bonacina, S., Gilberti, N., Vergani, V., Gamba, M., Spezi, R., Delrio, I., Bernier, M., Costa, A., et al. (2021) · BMC Neurology · doi:10.1186/s12883-021-02458-4 · Cited by 5 · see citing works
“The reduction of hydroxylation of these residues appears to lead to impairment of vessel walls due to the perturbation of the transforming growth factor beta pathway caused by GLUT10 deficiency [3, 4].”
BackgroundSelf-citationHosen, M. J., Hasan, M., Chakraborty, S., Abir, R. A., Zubaer, A., & Coucke, P. J. (2020) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201020666190613152030 · Cited by 5 · see citing works
Arterial Tortuosity Syndrome: Keys to Early Diagnosis and Report of a New Mutation
Tunks, R. D., Miranda, K. W., Hackett, G. L., & Aliu, E. (2024) · CASE · doi:10.1016/j.case.2024.09.009 · Cited by 4 · see citing works
Chiarelli, N., Cinquina, V., Zoppi, N., Bertini, V., Maddaluno, M., Leonibus, C. D., Settembre, C., Venturini, M., Colombi, M., & Ritelli, M. (2024) · Biomedicines · doi:10.3390/biomedicines12122749 · Cited by 4 · see citing works
Self-citationFaiyaz‐Ul‐Haque, M., Mubarak, M., AbdulWahab, A., Al‐Rikabi, A. C., Alsaeed, A. H., Al‐Otaiby, M., Nawaz, Z., Zaidi, S. H. E., & Basit, S. (2022) · Journal of Cutaneous Pathology · doi:10.1111/cup.14228 · Cited by 4 · see citing works
“The GLUT10 deficiency was associated with the lack of assembly of fibronectins, collagens, elastin, and decorin in the extracellular matrix.(16) The transcriptome profiling also revealed differentially expressed genes that influence lipid metabolism, intracellular redox homeostasis, and extra-”
BackgroundOxidative Stress Mediates Vascular Tortuosity
Fumoto, T., Kinoshita, S., Sasaki, T., Shimamura, N., & Ohkuma, H. (2021) · Antioxidants · doi:10.3390/antiox10060926 · Cited by 3 · see citing works
“oxidative stress and elevated transforming growth factor β (TGF-β) signaling in fibroblasts from ATS patients [15].”
BackgroundA rare case of arterial tortuosity syndrome in an adult
Elnaggar, M. E., Aly, M. M., Abduljawad, H. O., Bubshait, M., & Ibrahim, W. H. (2022) · Radiology Case Reports · doi:10.1016/j.radcr.2022.05.005 · Cited by 2 · see citing works
Localization of Glucose Transporter 10 to Hair Cells’ Cuticular Plate in the Mouse Inner Ear
Chen, B., Wang, Y., Geng, M., Lin, X., & Tang, W. (2018) · BioMed Research International · doi:10.1155/2018/7817453 · Cited by 2 · see citing works
Intracranial Vascular Tortuosity in an Infant With Dysmorphic Facies
Tempchin, A. F., Nagesh, D., Paulsen, K. C., Ho, E., & Santoro, J. D. (2022) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2022.04.001 · Cited by 1 · see citing works
Kitt, D. Q. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.12.010 · Cited by 1 · see citing works
Mowafy, K. A., & Soliman, M. (2018) · Angiology Open Access · doi:10.4172/2329-9495.1000218
“Mutation(s) in SLC2A10 lead to low levels of that protein in the affected patients [1-4].”
BackgroundClinical Aspects of Heritable Connective Tissue Disorders
Verstraeten, A., & Loeys, B. (2019) · Springer eBooks · doi:10.1007/978-3-7091-4874-7_34
Transcriptomic Analysis of GLUT10 Deficiency in Arterial Tortuosity Syndrome
Yorgancıoğlu-Budak, G., Bingol, N. N., Türkgenç, B., Uysal, F., Bostan, Ö., Sağ, Ş. Ö., Çil, E., & Temel, Ş. G. (2026) · The EuroBiotech Journal · doi:10.2478/ebtj-2026-0008
“Therefore, GLUT10 acts as a cellular defense against oxidative stress by mitigating ROS-induced extracellular matrix (ECM) protein fragmentation [15,17].”
Николаевна, К. А., & Nazarenko, M. S. (2026) · Russian Journal of Genetics · doi:10.1134/s1022795426700183
“…with this pathology, 217 DEGs were identified in fibroblasts compared to controls (including 112 genes with increased and 105 with decreased expression), among which genes involved in lipid metabolism were overrepresented ( PLA2G4A , PPARG were upregulated, while IL1B was downregulated) [39].”
Arterial Tortuosity Syndrome (ATS)
Kalantari, A. (2025) · Springer eBooks · doi:10.1007/978-3-319-66816-1_1217-1
Arterial tortuosity syndrome with coronary artery involvement in a middle-aged female: A case report
Shrestha, P., Shah, A., Saroj, G. C., Sharma, N. K., Mahaseth, A., & Shrestha, S. K. (2026) · Radiology Case Reports · doi:10.1016/j.radcr.2026.09.029
- Authors
- Zoppi, N., Chiarelli, N., Cinquina, V., Ritelli, M., & Colombi, M.
- Affiliations
- University of Brescia (IT)
- Corresponding author
- Colombi, Marina
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2015-09-16
- Volume
- 24
- Issue
- 23
- Pages
- 6769-6787
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC4634379
- OpenAlex
- W2113237914
- Cited by
- 50
- References
- 78
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 5 · 2023: 6 · 2022: 5 · 2021: 3 · 2020: 6 · 2019: 7 · 2018: 6 · 2017: 4 · 2016: 3 · 2015: 1
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Human Molecular Genetics (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion, other-oa)
- Funders
- Telethon Foundation (GGP13167)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Dermatological and Skeletal Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- arterial tortuosity syndrome, GLUT10, SLC2A10, glucose transporters, oxidative stress, TGF-beta signaling, integrin αvβ3, extracellular matrix, dermal fibroblasts, connective tissue growth factor, PPARγ, ALDH1A1, lipid peroxidation, redox homeostasis, p38 MAPK, p125FAK, p60src, connective tissue diseases
- MeSH terms
- Arteries, Extracellular Matrix, Fibroblasts, Homeostasis, Humans, Joint Instability, Mutation, Skin, Skin Diseases, Genetic, Signal Transduction, Transforming Growth Factor beta, Oxidative Stress, Gene Expression Profiling, Integrin alphaVbeta3, Glucose Transport Proteins, Facilitative, Vascular Malformations
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