Novel insight into FCSK‐congenital disorder of glycosylation through a CRISPR‐generated cell model
Background FCSK‐congenital disorder of glycosylation (FCSK‐CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe mul...
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| Vydané v: | Molecular genetics & genomic medicine Ročník 12; číslo 5; s. e2445 - n/a |
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| Hlavní autori: | , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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United States
John Wiley & Sons, Inc
01.05.2024
John Wiley and Sons Inc Wiley |
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| Abstract | Background
FCSK‐congenital disorder of glycosylation (FCSK‐CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK‐CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency.
Methods
In this study, CRISPR/Cas9 was employed to construct an FCSK‐CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real‐time PCR analyses.
Results
Comparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O‐fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF‐like repeats O‐fucosylation.
Conclusion
This study expands insight into the FCSK‐CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease.
The current study exploring FCSK‐CDG through a CRISPR‐generated cell model demonstrated the effect of this disease on EGF‐like repeats O‐fucosylation by revealing NOTCH3 as the first identified gene whose expression level alters due to FCSK‐CDG. In addition, it suggested a probable effect of this disease on secretory glycoproteins. |
|---|---|
| AbstractList | The current study exploring FCSK‐CDG through a CRISPR‐generated cell model demonstrated the effect of this disease on EGF‐like repeats O‐fucosylation by revealing NOTCH3 as the first identified gene whose expression level alters due to FCSK‐CDG. In addition, it suggested a probable effect of this disease on secretory glycoproteins. BackgroundFCSK-congenital disorder of glycosylation (FCSK-CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK-CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency.MethodsIn this study, CRISPR/Cas9 was employed to construct an FCSK-CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real-time PCR analyses.ResultsComparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O-fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF-like repeats O-fucosylation.ConclusionThis study expands insight into the FCSK-CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease. FCSK-congenital disorder of glycosylation (FCSK-CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK-CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency.BACKGROUNDFCSK-congenital disorder of glycosylation (FCSK-CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK-CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency.In this study, CRISPR/Cas9 was employed to construct an FCSK-CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real-time PCR analyses.METHODSIn this study, CRISPR/Cas9 was employed to construct an FCSK-CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real-time PCR analyses.Comparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O-fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF-like repeats O-fucosylation.RESULTSComparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O-fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF-like repeats O-fucosylation.This study expands insight into the FCSK-CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease.CONCLUSIONThis study expands insight into the FCSK-CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease. Background FCSK‐congenital disorder of glycosylation (FCSK‐CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK‐CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency. Methods In this study, CRISPR/Cas9 was employed to construct an FCSK‐CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real‐time PCR analyses. Results Comparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O‐fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF‐like repeats O‐fucosylation. Conclusion This study expands insight into the FCSK‐CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease. The current study exploring FCSK‐CDG through a CRISPR‐generated cell model demonstrated the effect of this disease on EGF‐like repeats O‐fucosylation by revealing NOTCH3 as the first identified gene whose expression level alters due to FCSK‐CDG. In addition, it suggested a probable effect of this disease on secretory glycoproteins. Abstract Background FCSK‐congenital disorder of glycosylation (FCSK‐CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK‐CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency. Methods In this study, CRISPR/Cas9 was employed to construct an FCSK‐CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real‐time PCR analyses. Results Comparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O‐fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF‐like repeats O‐fucosylation. Conclusion This study expands insight into the FCSK‐CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease. FCSK-congenital disorder of glycosylation (FCSK-CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to mutations in the fucokinase encoding gene, FCSK. Despite the essential role of fucokinase in the fucose salvage pathway and severe multisystem manifestations of FCSK-CDG patients, it is not elucidated which cells or which types of fucosylation are affected by its deficiency. In this study, CRISPR/Cas9 was employed to construct an FCSK-CDG cell model and explore the molecular mechanisms of the disease by lectin flow cytometry and real-time PCR analyses. Comparison of cellular fucosylation by lectin flow cytometry in the created CRISPR/Cas9 FCSK knockout and the same unedited cell lines showed no significant change in the amount of cell surface fucosylated glycans, which is consistent with the only documented previous study on different cell types. It suggests a probable effect of this disease on secretory glycoproteins. Investigating O-fucosylation by analysis of the NOTCH3 gene expression as a potential target revealed a significant decrease in the FCSK knockout cells compared with the same unedited ones, proving the effect of fucokinase deficiency on EGF-like repeats O-fucosylation. This study expands insight into the FCSK-CDG molecular mechanism; to the best of our knowledge, it is the first research conducted to reveal a gene whose expression level alters due to this disease. |
| Author | Tabei, Seyed Mohammad Bagher Fallahi, Jafar Fazelzadeh Haghighi, Maryam Jafari Khamirani, Hossein Ashrafi Dehkordi, Korosh Monfared, Ali Arabi |
| AuthorAffiliation | 1 Department of Molecular Medicine, School of Advanced Technologies Shahrekord University of Medical Sciences Shahrekord Iran 5 Maternal‐Fetal Medicine Research Center Shiraz University of Medical Sciences Shiraz Iran 2 Department of Medical Genetics Shiraz University of Medical Sciences Shiraz Iran 3 Molecular Medicine Department, School of Advanced Medical Sciences and Technologies Shiraz University of Medical Sciences Shiraz Iran 4 Central Research Laboratory Shiraz University of Medical Sciences Shiraz Iran |
| AuthorAffiliation_xml | – name: 2 Department of Medical Genetics Shiraz University of Medical Sciences Shiraz Iran – name: 5 Maternal‐Fetal Medicine Research Center Shiraz University of Medical Sciences Shiraz Iran – name: 3 Molecular Medicine Department, School of Advanced Medical Sciences and Technologies Shiraz University of Medical Sciences Shiraz Iran – name: 4 Central Research Laboratory Shiraz University of Medical Sciences Shiraz Iran – name: 1 Department of Molecular Medicine, School of Advanced Technologies Shahrekord University of Medical Sciences Shahrekord Iran |
| Author_xml | – sequence: 1 givenname: Maryam orcidid: 0009-0009-7410-1254 surname: Fazelzadeh Haghighi fullname: Fazelzadeh Haghighi, Maryam organization: Shahrekord University of Medical Sciences – sequence: 2 givenname: Hossein orcidid: 0000-0001-7703-7387 surname: Jafari Khamirani fullname: Jafari Khamirani, Hossein organization: Shiraz University of Medical Sciences – sequence: 3 givenname: Jafar orcidid: 0000-0002-8485-9247 surname: Fallahi fullname: Fallahi, Jafar organization: Shiraz University of Medical Sciences – sequence: 4 givenname: Ali Arabi orcidid: 0000-0002-1446-5015 surname: Monfared fullname: Monfared, Ali Arabi organization: Shiraz University of Medical Sciences – sequence: 5 givenname: Korosh orcidid: 0000-0001-7105-731X surname: Ashrafi Dehkordi fullname: Ashrafi Dehkordi, Korosh email: ashrafi.k@skums.ac.ir organization: Shahrekord University of Medical Sciences – sequence: 6 givenname: Seyed Mohammad Bagher orcidid: 0000-0001-9923-6969 surname: Tabei fullname: Tabei, Seyed Mohammad Bagher email: tabeismb@sums.ac.ir organization: Shiraz University of Medical Sciences |
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| Cites_doi | 10.1016/j.tig.2018.03.002 10.1002/nbm.3239 10.1182/blood‐2008‐04‐149641 10.1074/jbc.M802027200 10.1126/science.1207438 10.1016/j.addr.2003.10.017 10.1016/j.ajhg.2017.12.009 10.1038/ng0501‐73 10.1093/glycob/cwg054 10.1002/jimd.12426 10.1016/j.chembiol.2017.08.023 10.1038/nri2417 10.1016/j.ajhg.2018.10.021 10.1083/jcb.200203125 10.1074/jbc.RA117.000775 10.1371/journal.pone.0070298 10.1083/jcb.202205038 10.1021/bi00685a011 10.1126/scisignal.aac6479 10.1371/journal.pone.0199128 10.1016/j.ajhg.2013.04.022 10.1016/0009‐8981(89)90058‐2 10.1002/mgg3.2117 10.1002/cpbi.5 10.1016/j.sbi.2011.08.008 10.1038/nrm.2016.94 10.1007/s44162‐022‐00003‐6 10.1016/j.braindev.2021.11.001 10.1093/glycob/cwx034 10.3389/fphys.2020.00929 10.1002/art.38711 10.1038/ng0501‐69 10.18502/ajmb.v13i2.5517 10.1021/acs.biochem.9b00565 10.1007/s10545‐011‐9370‐0 10.1016/j.mimet.2021.106267 10.3389/fonc.2018.00039 10.3390/cancers11091241 10.1038/s41598‐019‐54933‐1 10.15252/emmm.202114332 10.1186/s12885‐018‐4524‐1 10.1111/febs.16815 10.1021/ja044631v 10.1016/j.ejmg.2022.104535 10.1021/bi00624a021 10.1038/jid.2014.406 10.1002/bies.950120406 10.1242/dev.033290 10.1038/s41581‐019‐0129‐4 10.1016/j.bjhh.2016.07.005 10.1016/S0021‐9258(19)56958‐7 10.1203/00006450‐198002000‐00117 |
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| Keywords | congenital disorder of glycosylation CRISPR/Cas9 FCSK fucokinase |
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| References | 1990; 12 1968; 243 2019; 11 2002; 158 2019; 15 2003; 13 2020; 59 2008; 8 1975; 14 2020; 11 2022; 65 2013; 8 2016; 38 2014; 66 2018; 8 2018; 293 2015; 135 2011; 21 2018; 34 2008; 112 2011; 333 2019; 9 2023; 11 2021; 44 2017; 27 2018; 102 2017; 24 2018; 103 2016; 54 2013; 92 1989; 184 2011; 34 2001; 28 2022; 44 2021; 187 2016; 17 2015; 8 2009; 136 2008; 283 2022; 221 2021; 13 2018; 18 1980; 14 2015; 28 2023 2022 1977; 16 2005; 127 2004; 56 2022; 1 2018; 13 e_1_2_12_4_1 e_1_2_12_6_1 e_1_2_12_19_1 e_1_2_12_2_1 e_1_2_12_17_1 e_1_2_12_38_1 Varki A. (e_1_2_12_51_1) 2022 e_1_2_12_20_1 e_1_2_12_41_1 e_1_2_12_22_1 e_1_2_12_43_1 e_1_2_12_24_1 e_1_2_12_45_1 e_1_2_12_26_1 e_1_2_12_47_1 e_1_2_12_28_1 e_1_2_12_49_1 e_1_2_12_31_1 e_1_2_12_52_1 e_1_2_12_33_1 e_1_2_12_54_1 e_1_2_12_35_1 e_1_2_12_37_1 e_1_2_12_14_1 e_1_2_12_12_1 e_1_2_12_8_1 e_1_2_12_10_1 e_1_2_12_50_1 e_1_2_12_3_1 e_1_2_12_5_1 e_1_2_12_18_1 e_1_2_12_16_1 e_1_2_12_39_1 e_1_2_12_42_1 e_1_2_12_21_1 e_1_2_12_44_1 e_1_2_12_23_1 e_1_2_12_46_1 e_1_2_12_25_1 e_1_2_12_48_1 e_1_2_12_40_1 e_1_2_12_27_1 e_1_2_12_29_1 e_1_2_12_30_1 e_1_2_12_53_1 e_1_2_12_32_1 e_1_2_12_34_1 e_1_2_12_36_1 e_1_2_12_15_1 e_1_2_12_13_1 e_1_2_12_11_1 e_1_2_12_7_1 e_1_2_12_9_1 |
| References_xml | – volume: 54 start-page: 1.30‐1 issue: 1 year: 2016 end-page: 1.30‐33 article-title: The GeneCards suite: From gene data mining to disease genome sequence analyses publication-title: Current Protocols in Bioinformatics – volume: 28 start-page: 73 issue: 1 year: 2001 end-page: 76 article-title: Complementation cloning identifies CDG‐IIc, a new type of congenital disorders of glycosylation, as a GDP‐fucose transporter deficiency publication-title: Nature Genetics – volume: 34 start-page: 849 issue: 4 year: 2011 end-page: 852 article-title: How to find and diagnose a CDG due to defective N‐glycosylation publication-title: Journal of Inherited Metabolic Disease – volume: 13 issue: 9 year: 2021 article-title: A spoonful of L‐fucose‐an efficient therapy for GFUS‐CDG, a new glycosylation disorder publication-title: EMBO Molecular Medicine – volume: 15 start-page: 346 issue: 6 year: 2019 end-page: 366 article-title: Glycosylation in health and disease publication-title: Nature Reviews. Nephrology – volume: 24 start-page: 1467 issue: 12 year: 2017 end-page: 1478.e5 article-title: An alkynyl‐fucose halts hepatoma cell migration and invasion by inhibiting GDP‐Fucose‐synthesizing enzyme FX, TSTA3 publication-title: Cell Chemistry & Biology – volume: 27 start-page: 601 issue: 7 year: 2017 end-page: 618 article-title: Biological functions of fucose in mammals publication-title: Glycobiology – volume: 11 year: 2020 article-title: Understanding the principles of pattern formation driven by Notch signaling by integrating experiments and theoretical models publication-title: Frontiers in Physiology – volume: 28 start-page: 69 issue: 1 year: 2001 end-page: 72 article-title: The gene defective in leukocyte adhesion deficiency II encodes a putative GDP‐fucose transporter publication-title: Nature Genetics – volume: 293 start-page: 7300 issue: 19 year: 2018 end-page: 7314 article-title: Distinct human alpha(1,3)‐fucosyltransferases drive Lewis‐X/sialyl Lewis‐X assembly in human cells publication-title: The Journal of Biological Chemistry – volume: 184 start-page: 251 issue: 3 year: 1989 end-page: 258 article-title: Abnormally‐fucosylated serum haptoglobins in patients with inflammatory joint disease publication-title: Clinica Chimica Acta – volume: 9 issue: 1 year: 2019 article-title: Two new fucose‐alpha (1‐2)‐glycans assigned in the healthy human brain taking the number to seven publication-title: Scientific Reports – volume: 16 start-page: 944 issue: 5 year: 1977 end-page: 953 article-title: Equilibration of fucosyl glycoprotein pools in HeLa cells publication-title: Biochemistry – volume: 158 start-page: 801 issue: 4 year: 2002 end-page: 815 article-title: Conditional control of selectin ligand expression and global fucosylation events in mice with a targeted mutation at the FX locus publication-title: The Journal of Cell Biology – volume: 44 start-page: 239 issue: 3 year: 2022 end-page: 243 article-title: A case with congenital disorder of glycosylation with defective fucosylation 2 and new mutation in FUK gene publication-title: Brain & Development – volume: 65 issue: 8 year: 2022 article-title: A combination of two novels homozygous FCSK variants cause disorder of glycosylation with defective fucosylation: New patient and literature review publication-title: European Journal of Medical Genetics – year: 2023 article-title: Notch signalling: Multifaceted role in development and disease publication-title: The FEBS Journal – volume: 18 start-page: 600 issue: 1 year: 2018 article-title: GMDS knockdown impairs cell proliferation and survival in human lung adenocarcinoma publication-title: BMC Cancer – volume: 8 issue: 7 year: 2013 article-title: Mutation of GDP‐mannose‐4,6‐dehydratase in colorectal cancer metastasis publication-title: PLoS One – volume: 221 issue: 10 year: 2022 article-title: Origin of cytoplasmic GDP‐fucose determines its contribution to glycosylation reactions publication-title: The Journal of Cell Biology – year: 2022 – volume: 44 start-page: 1441 issue: 6 year: 2021 end-page: 1452 article-title: Congenital disorders of glycosylation with defective fucosylation publication-title: Journal of Inherited Metabolic Disease – volume: 283 start-page: 13638 issue: 20 year: 2008 end-page: 13651 article-title: Roles of Pofut1 and O‐fucose in mammalian Notch signaling publication-title: The Journal of Biological Chemistry – volume: 38 start-page: 331 issue: 4 year: 2016 end-page: 340 article-title: Structural diversity and biological importance of ABO, H, Lewis and secretor histo‐blood group carbohydrates publication-title: Revista Brasileira de Hematologia e Hemoterapia – volume: 28 start-page: 291 issue: 3 year: 2015 end-page: 296 article-title: Six fucose‐alpha(1‐2) sugars and alpha‐fucose assigned in the human brain using in vivo two‐dimensional MRS publication-title: NMR in Biomedicine – volume: 136 start-page: 1653 issue: 10 year: 2009 end-page: 1663 article-title: Neuroepithelial cells require fucosylated glycans to guide the migration of vagus motor neuron progenitors in the developing zebrafish hindbrain publication-title: Development – volume: 21 start-page: 583 issue: 5 year: 2011 end-page: 589 article-title: Fringe benefits: Functional and structural impacts of O‐glycosylation on the extracellular domain of Notch receptors publication-title: Current Opinion in Structural Biology – volume: 333 start-page: 1761 issue: 6050 year: 2011 end-page: 1764 article-title: Human sperm binding is mediated by the sialyl‐Lewisx oligosaccharide on the zona pellucida publication-title: Science – volume: 1 start-page: 3 issue: 1 year: 2022 article-title: Epidemiology of congenital disorders of glycosylation (CDG)—Overview and perspectives publication-title: Journal of Rare Diseases – volume: 8 issue: 406 year: 2015 article-title: The transcription factor ATF2 promotes melanoma metastasis by suppressing protein fucosylation publication-title: Science Signaling – volume: 135 start-page: 615 issue: 2 year: 2015 end-page: 618 article-title: Pathogenicity of POFUT1 in Dowling‐Degos disease: Additional mutations and clinical overlap with reticulate acropigmentation of kitamura publication-title: The Journal of Investigative Dermatology – volume: 34 start-page: 466 issue: 6 year: 2018 end-page: 476 article-title: Perspectives on glycosylation and its congenital disorders publication-title: Trends in Genetics – volume: 102 start-page: 188 issue: 1 year: 2018 end-page: 195 article-title: Biallelic mutations in FUT8 cause a congenital disorder of glycosylation with defective fucosylation publication-title: American Journal of Human Genetics – volume: 12 start-page: 173 issue: 4 year: 1990 end-page: 179 article-title: Glycoconjugate expression during embryogenesis and its biological significance publication-title: BioEssays – volume: 13 issue: 6 year: 2018 article-title: The fucose salvage pathway inhibits invadopodia formation and extracellular matrix degradation in melanoma cells publication-title: PLoS One – volume: 14 start-page: 179 issue: 2 year: 1980 article-title: Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG‐deficiency, increased serum arylsulphatase A and increased CSF protein: A new syndrome?: 90 publication-title: Pediatric Research – volume: 127 start-page: 1340 issue: 5 year: 2005 end-page: 1341 article-title: A role for fucose alpha(1‐2) galactose carbohydrates in neuronal growth publication-title: Journal of the American Chemical Society – volume: 8 start-page: 874 issue: 11 year: 2008 end-page: 887 article-title: Mammalian glycosylation in immunity publication-title: Nature Reviews. Immunology – volume: 56 start-page: 491 issue: 4 year: 2004 end-page: 509 article-title: Drug targeting to the colon with lectins and neoglycoconjugates publication-title: Advanced Drug Delivery Reviews – volume: 17 start-page: 722 issue: 11 year: 2016 end-page: 735 article-title: Notch signalling in context publication-title: Nature Reviews. Molecular Cell Biology – volume: 13 start-page: 54 issue: 2 year: 2021 end-page: 57 article-title: Using CRISPR/Cas9 system to knock out exon 48 in DMD gene publication-title: Avicenna Journal Of Medical Biotechnology – volume: 11 issue: 9 year: 2019 article-title: The diverse contributions of fucose linkages in cancer publication-title: Cancers (Basel) – volume: 59 start-page: 3064 issue: 34 year: 2020 end-page: 3077 article-title: Therapeutic monosaccharides: Looking back, moving forward publication-title: Biochemistry – volume: 14 start-page: 3107 issue: 14 year: 1975 end-page: 3114 article-title: Fucosyl‐glycoprotein and precursor pools in HeLa cells publication-title: Biochemistry – volume: 112 start-page: 3744 issue: 9 year: 2008 end-page: 3752 article-title: E‐selectin receptors on human leukocytes publication-title: Blood – volume: 13 start-page: 41R issue: 7 year: 2003 end-page: 53R article-title: Fucose: Biosynthesis and biological function in mammals publication-title: Glycobiology – volume: 8 year: 2018 article-title: Fucosylated antigens in cancer: An alliance toward tumor progression, metastasis, and resistance to chemotherapy publication-title: Frontiers in Oncology – volume: 243 start-page: 1103 issue: 6 year: 1968 end-page: 1109 article-title: The metabolism of l‐fucose: III. The enzymatic synthesis of β‐l‐fucose 1‐phosphate publication-title: The Journal of Biological Chemistry – volume: 187 year: 2021 article-title: CtNorm: Real time PCR cycle of threshold (Ct) normalization algorithm publication-title: Journal of Microbiological Methods – volume: 92 start-page: 895 issue: 6 year: 2013 end-page: 903 article-title: Mutations in POFUT1, encoding protein O‐fucosyltransferase 1, cause generalized Dowling‐Degos disease publication-title: American Journal of Human Genetics – volume: 103 start-page: 1030 issue: 6 year: 2018 end-page: 1037 article-title: Pathogenic variants in fucokinase cause a congenital disorder of glycosylation publication-title: American Journal of Human Genetics – volume: 11 issue: 4 year: 2023 article-title: Congenital disorder of glycosylation with defective fucosylation 2 (FCSK gene defect): The third report in the literature with a mild phenotype publication-title: Molecular Genetics & Genomic Medicine – volume: 66 start-page: 2368 issue: 9 year: 2014 end-page: 2379 article-title: Inhibition of fucosylation reshapes inflammatory macrophages and suppresses type II collagen‐induced arthritis publication-title: Arthritis & Rhematology – ident: e_1_2_12_31_1 doi: 10.1016/j.tig.2018.03.002 – ident: e_1_2_12_29_1 doi: 10.1002/nbm.3239 – ident: e_1_2_12_34_1 doi: 10.1182/blood‐2008‐04‐149641 – ident: e_1_2_12_47_1 doi: 10.1074/jbc.M802027200 – ident: e_1_2_12_37_1 doi: 10.1126/science.1207438 – volume-title: Essentials of Glycobiology year: 2022 ident: e_1_2_12_51_1 – ident: e_1_2_12_27_1 doi: 10.1016/j.addr.2003.10.017 – ident: e_1_2_12_33_1 doi: 10.1016/j.ajhg.2017.12.009 – ident: e_1_2_12_23_1 doi: 10.1038/ng0501‐73 – ident: e_1_2_12_4_1 doi: 10.1093/glycob/cwg054 – ident: e_1_2_12_12_1 doi: 10.1002/jimd.12426 – ident: e_1_2_12_18_1 doi: 10.1016/j.chembiol.2017.08.023 – ident: e_1_2_12_26_1 doi: 10.1038/nri2417 – ident: e_1_2_12_32_1 doi: 10.1016/j.ajhg.2018.10.021 – ident: e_1_2_12_44_1 doi: 10.1083/jcb.200203125 – ident: e_1_2_12_28_1 doi: 10.1074/jbc.RA117.000775 – ident: e_1_2_12_30_1 doi: 10.1371/journal.pone.0070298 – ident: e_1_2_12_46_1 doi: 10.1083/jcb.202205038 – ident: e_1_2_12_53_1 doi: 10.1021/bi00685a011 – ident: e_1_2_12_19_1 doi: 10.1126/scisignal.aac6479 – ident: e_1_2_12_16_1 doi: 10.1371/journal.pone.0199128 – ident: e_1_2_12_22_1 doi: 10.1016/j.ajhg.2013.04.022 – ident: e_1_2_12_49_1 doi: 10.1016/0009‐8981(89)90058‐2 – ident: e_1_2_12_2_1 doi: 10.1002/mgg3.2117 – ident: e_1_2_12_48_1 doi: 10.1002/cpbi.5 – ident: e_1_2_12_40_1 doi: 10.1016/j.sbi.2011.08.008 – ident: e_1_2_12_7_1 doi: 10.1038/nrm.2016.94 – ident: e_1_2_12_38_1 doi: 10.1007/s44162‐022‐00003‐6 – ident: e_1_2_12_36_1 doi: 10.1016/j.braindev.2021.11.001 – ident: e_1_2_12_43_1 doi: 10.1093/glycob/cwx034 – ident: e_1_2_12_6_1 doi: 10.3389/fphys.2020.00929 – ident: e_1_2_12_21_1 doi: 10.1002/art.38711 – ident: e_1_2_12_24_1 doi: 10.1038/ng0501‐69 – ident: e_1_2_12_8_1 doi: 10.18502/ajmb.v13i2.5517 – ident: e_1_2_12_45_1 doi: 10.1021/acs.biochem.9b00565 – ident: e_1_2_12_20_1 doi: 10.1007/s10545‐011‐9370‐0 – ident: e_1_2_12_39_1 doi: 10.1016/j.mimet.2021.106267 – ident: e_1_2_12_5_1 doi: 10.3389/fonc.2018.00039 – ident: e_1_2_12_17_1 doi: 10.3390/cancers11091241 – ident: e_1_2_12_50_1 doi: 10.1038/s41598‐019‐54933‐1 – ident: e_1_2_12_10_1 doi: 10.15252/emmm.202114332 – ident: e_1_2_12_52_1 doi: 10.1186/s12885‐018‐4524‐1 – ident: e_1_2_12_42_1 doi: 10.1111/febs.16815 – ident: e_1_2_12_15_1 doi: 10.1021/ja044631v – ident: e_1_2_12_25_1 doi: 10.1016/j.ejmg.2022.104535 – ident: e_1_2_12_54_1 doi: 10.1021/bi00624a021 – ident: e_1_2_12_3_1 doi: 10.1038/jid.2014.406 – ident: e_1_2_12_11_1 doi: 10.1002/bies.950120406 – ident: e_1_2_12_35_1 doi: 10.1242/dev.033290 – ident: e_1_2_12_41_1 doi: 10.1038/s41581‐019‐0129‐4 – ident: e_1_2_12_9_1 doi: 10.1016/j.bjhh.2016.07.005 – ident: e_1_2_12_13_1 doi: 10.1016/S0021‐9258(19)56958‐7 – ident: e_1_2_12_14_1 doi: 10.1203/00006450‐198002000‐00117 |
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| Snippet | Background
FCSK‐congenital disorder of glycosylation (FCSK‐CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation... FCSK-congenital disorder of glycosylation (FCSK-CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation due to... BackgroundFCSK-congenital disorder of glycosylation (FCSK-CDG) is a recently discovered rare autosomal recessive genetic disorder with defective fucosylation... The current study exploring FCSK‐CDG through a CRISPR‐generated cell model demonstrated the effect of this disease on EGF‐like repeats O‐fucosylation by... Abstract Background FCSK‐congenital disorder of glycosylation (FCSK‐CDG) is a recently discovered rare autosomal recessive genetic disorder with defective... |
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| SubjectTerms | Age Cell culture Cell lines Cell surface Congenital anomalies Congenital diseases congenital disorder of glycosylation Congenital Disorders of Glycosylation - genetics Congenital Disorders of Glycosylation - metabolism Congenital Disorders of Glycosylation - pathology Convulsions & seizures CRISPR CRISPR-Cas Systems CRISPR/Cas9 Design Disease Enzymes Epilepsy FCSK Flow cytometry Fucokinase Fucose - metabolism Gene expression Genetic disorders Glycoproteins Glycosylation Hereditary diseases Humans Intellectual disabilities Molecular modelling Notch3 protein Original Patients Phosphotransferases (Alcohol Group Acceptor) Polysaccharides Receptors, Notch - genetics Receptors, Notch - metabolism |
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| Title | Novel insight into FCSK‐congenital disorder of glycosylation through a CRISPR‐generated cell model |
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