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Article ; Online: Clinical and biochemical footprints of congenital disorders of glycosylation: Proposed nosology.

Ng, Bobby G / Freeze, Hudson H / Himmelreich, Nastassja / Blau, Nenad / Ferreira, Carlos R

2024 Volume 142, Issue 1, Page(s) 108476

Abstract: We have identified 200 congenital disorders of glycosylation (CDG) caused by 189 different gene defects and have proposed a classification system for CDG based on the mode of action. This classification includes 8 categories: 1. Disorders of ... ...

Abstract	We have identified 200 congenital disorders of glycosylation (CDG) caused by 189 different gene defects and have proposed a classification system for CDG based on the mode of action. This classification includes 8 categories: 1. Disorders of monosaccharide synthesis and interconversion, 2. Disorders of nucleotide sugar synthesis and transport, 3. Disorders of N-linked protein glycosylation, 4. Disorders of O-linked protein glycosylation, 5. Disorders of lipid glycosylation, 6. Disorders of vesicular trafficking, 7. Disorders of multiple glycosylation pathways and 8. Disorders of glycoprotein/glycan degradation. Additionally, using information from IEMbase, we have described the clinical involvement of 19 organs and systems, as well as essential laboratory investigations for each type of CDG. Neurological, dysmorphic, skeletal, and ocular manifestations were the most prevalent, occurring in 81%, 56%, 53%, and 46% of CDG, respectively. This was followed by digestive, cardiovascular, dermatological, endocrine, and hematological symptoms (17-34%). Immunological, genitourinary, respiratory, psychiatric, and renal symptoms were less frequently reported (8-12%), with hair and dental abnormalities present in only 4-7% of CDG. The information provided in this study, including our proposed classification system for CDG, may be beneficial for healthcare providers caring for individuals with metabolic conditions associated with CDG.
Language	English
Publishing date	2024-04-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	1418518-0
ISSN	1096-7206 ; 1096-7192
ISSN (online)	1096-7206
ISSN	1096-7192
DOI	10.1016/j.ymgme.2024.108476
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Article: COVID-19-Practicing Prevention in the Workplace.

Joseph, Bobby / Angeline, Nancy G / Arasu, Sakthi

Indian journal of occupational and environmental medicine

2020 Volume 24, Issue 3, Page(s) 133–136

Language	English
Publishing date	2020-12-14
Publishing country	India
Document type	Editorial
ZDB-ID	1456082-3
ISSN	1998-3670 ; 0973-2284 ; 0019-5278
ISSN (online)	1998-3670
ISSN	0973-2284 ; 0019-5278
DOI	10.4103/ijoem.ijoem_460_20
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Zs.A 4967: Show issues

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Article ; Online: Chemical Therapies for Congenital Disorders of Glycosylation.

Sosicka, Paulina / Ng, Bobby G / Freeze, Hudson H

ACS chemical biology

2021 Volume 17, Issue 11, Page(s) 2962–2971

Abstract: Congenital disorders of glycosylation (CDG) are ultrarare, genetically and clinically heterogeneous metabolic disorders. Although the number of identified CDG is growing rapidly, there are few therapeutic options. Most treatments involve dietary ... ...

Abstract	Congenital disorders of glycosylation (CDG) are ultrarare, genetically and clinically heterogeneous metabolic disorders. Although the number of identified CDG is growing rapidly, there are few therapeutic options. Most treatments involve dietary supplementation with monosaccharides or other precursors. These approaches are relatively safe, but in many cases, the molecular and biochemical underpinnings are incomplete. Recent studies demonstrate that yeast, worm, fly, and zebrafish models of CDG are powerful tools in screening repurposed drugs, ushering a new avenue to search for novel therapeutic options. Here we present a perspective on compounds that are currently in use for CDG treatment or have a potential to be applied as therapeutics in the near future.
MeSH term(s)	Animals ; Congenital Disorders of Glycosylation/drug therapy ; Congenital Disorders of Glycosylation/diagnosis ; Congenital Disorders of Glycosylation/metabolism ; Zebrafish ; Glycosylation
Language	English
Publishing date	2021-11-17
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.1c00601
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Article ; Online: GLUT1 is a highly efficient L-fucose transporter.

Ng, Bobby G / Sosicka, Paulina / Xia, Zhijie / Freeze, Hudson H

The Journal of biological chemistry

2022 Volume 299, Issue 1, Page(s) 102738

Abstract: Understanding L-fucose metabolism is important because it is used as a therapy for several congenital disorders of glycosylation. Exogenous L-fucose can be activated and incorporated directly into multiple N- and O-glycans via the fucose salvage/ ... ...

Abstract	Understanding L-fucose metabolism is important because it is used as a therapy for several congenital disorders of glycosylation. Exogenous L-fucose can be activated and incorporated directly into multiple N- and O-glycans via the fucose salvage/recycling pathway. However, unlike for other monosaccharides, no mammalian L-fucose transporter has been identified. Here, we functionally screened nearly 140 annotated transporters and identified GLUT1 (SLC2A1) as an L-fucose transporter. We confirmed this assignment using multiple approaches to alter GLUT1 function, including chemical inhibition, siRNA knockdown, and gene KO. Collectively, all methods demonstrate that GLUT1 contributes significantly to L-fucose uptake and its utilization at low micromolar levels. Surprisingly, millimolar levels of D-glucose do not compete with L-fucose uptake. We also show macropinocytosis, but not other endocytic pathways, can contribute to L-fucose uptake and utilization. In conclusion, we determined that GLUT1 functions as the previously missing transporter component in mammalian L-fucose metabolism.
MeSH term(s)	Biological Transport ; Fucose/metabolism ; Glucose ; Glucose Transporter Type 1/genetics ; Glucose Transporter Type 1/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism
Chemical Substances	Fucose (28RYY2IV3F) ; Glucose (IY9XDZ35W2) ; Glucose Transporter Type 1 ; Membrane Transport Proteins
Language	English
Publishing date	2022-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102738
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Article: Perspectives on Glycosylation and Its Congenital Disorders.

Ng, Bobby G / Freeze, Hudson H

Trends in genetics : TIG

2018 Volume 34, Issue 6, Page(s) 466–476

Abstract: Congenital disorders of glycosylation (CDG) are a rapidly expanding group of metabolic disorders that result from abnormal protein or lipid glycosylation. They are often difficult to clinically diagnose because they broadly affect many organs and ... ...

Abstract	Congenital disorders of glycosylation (CDG) are a rapidly expanding group of metabolic disorders that result from abnormal protein or lipid glycosylation. They are often difficult to clinically diagnose because they broadly affect many organs and functions and lack clinical uniformity. However, recent technological advances in next-generation sequencing have revealed a treasure trove of new genetic disorders, expanded the knowledge of known disorders, and showed a critical role in infectious diseases. More comprehensive genetic tools specifically tailored for mammalian cell-based models have revealed a critical role for glycosylation in pathogen-host interactions, while also identifying new CDG susceptibility genes. We highlight recent advancements that have resulted in a better understanding of human glycosylation disorders, perspectives for potential future therapies, and mysteries for which we continue to seek new insights and solutions.
MeSH term(s)	Congenital Disorders of Glycosylation/complications ; Congenital Disorders of Glycosylation/genetics ; Congenital Disorders of Glycosylation/metabolism ; Congenital Disorders of Glycosylation/pathology ; Glycosylation ; High-Throughput Nucleotide Sequencing ; Host-Pathogen Interactions/genetics ; Humans ; Infection/complications ; Infection/genetics ; Infection/metabolism ; Infection/pathology ; Lipid Metabolism
Language	English
Publishing date	2018-03-29
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	619240-3
ISSN	1362-4555 ; 0168-9525 ; 0168-9479
ISSN (online)	1362-4555
ISSN	0168-9525 ; 0168-9479
DOI	10.1016/j.tig.2018.03.002
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Zs.A 2272: Show issues

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Article ; Online: Therapeutic Monosaccharides: Looking Back, Moving Forward.

Sosicka, Paulina / Ng, Bobby G / Freeze, Hudson H

Biochemistry

2019 Volume 59, Issue 34, Page(s) 3064–3077

Abstract: In this review, we focus on the metabolism of mammalian glycan-associated monosaccharides, where the vast majority of our current knowledge comes from research done during the 1960s and 1970s. Most monosaccharides enter the cell using distinct, often ... ...

Abstract	In this review, we focus on the metabolism of mammalian glycan-associated monosaccharides, where the vast majority of our current knowledge comes from research done during the 1960s and 1970s. Most monosaccharides enter the cell using distinct, often tissue specific transporters from the SLC2A family. If not catabolized, these monosaccharides can be activated to donor nucleotide sugars and used for glycan synthesis. Apart from exogenous and dietary sources, all monosaccharides and their associated nucleotide sugars can be synthesized
MeSH term(s)	Dietary Carbohydrates/pharmacology ; Glycosylation/drug effects ; Humans ; Monosaccharides/chemistry ; Monosaccharides/pharmacology ; Monosaccharides/therapeutic use
Chemical Substances	Dietary Carbohydrates ; Monosaccharides
Language	English
Publishing date	2019-08-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.9b00565
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Article ; Online: N-Glycanase 1 Transcriptionally Regulates Aquaporins Independent of Its Enzymatic Activity.

Tambe, Mitali A / Ng, Bobby G / Freeze, Hudson H

Cell reports

2019 Volume 29, Issue 13, Page(s) 4620–4631.e4

Abstract: Patients with pathogenic mutations in NGLY1 cannot make tears and have global developmental delay and liver dysfunction. Traditionally, NGLY1 cleaves intact N-glycans from misfolded, retrotranslocated glycoproteins before proteasomal degradation. We ... ...

Abstract	Patients with pathogenic mutations in NGLY1 cannot make tears and have global developmental delay and liver dysfunction. Traditionally, NGLY1 cleaves intact N-glycans from misfolded, retrotranslocated glycoproteins before proteasomal degradation. We demonstrate that Ngly1-null mouse embryonic fibroblasts, NGLY1 knockout human cells, and patient fibroblasts are resistant to hypotonic lysis. Ngly1-deficient mouse embryonic fibroblasts swell slower and have reduced aquaporin1 mRNA and protein expression. Ngly1 knockdown and overexpression confirms that Ngly1 regulates aquaporin1 and hypotonic cell lysis. Patient fibroblasts and NGLY1 knockout cells show reduced aquaporin11 mRNA, supporting NGLY1 as regulating expression of multiple aquaporins across species. Complementing Ngly1-deficient cells with catalytically inactive NGLY1 (p.Cys309Ala) restores normal hypotonic lysis and aquaporin1 protein. We show that transcription factors Atf1/Creb1 regulate aquaporin1 and that the Atf1/Creb1 signaling pathway is disrupted in Ngly1-deficient mouse embryonic fibroblasts. These results identify a non-enzymatic, regulatory function of NGLY1 in aquaporin transcription, possibly related to alacrima and neurological symptoms.
MeSH term(s)	Activating Transcription Factor 1/genetics ; Activating Transcription Factor 1/metabolism ; Animals ; Aquaporin 1/genetics ; Aquaporin 1/metabolism ; Aquaporins/genetics ; Aquaporins/metabolism ; Cell Line ; Congenital Disorders of Glycosylation/genetics ; Congenital Disorders of Glycosylation/metabolism ; Congenital Disorders of Glycosylation/pathology ; Eye Diseases, Hereditary/genetics ; Eye Diseases, Hereditary/metabolism ; Eye Diseases, Hereditary/pathology ; Fibroblasts/metabolism ; Fibroblasts/pathology ; Gene Expression Regulation ; Genetic Complementation Test ; Humans ; Isoenzymes/antagonists & inhibitors ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Lacrimal Apparatus Diseases/genetics ; Lacrimal Apparatus Diseases/metabolism ; Lacrimal Apparatus Diseases/pathology ; Mice ; Mice, Knockout ; Osmosis ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/antagonists & inhibitors ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/deficiency ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/genetics ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism ; Polysaccharides/metabolism ; Primary Cell Culture ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Signal Transduction ; Transcription, Genetic
Chemical Substances	AQP1 protein, human ; AQP11 protein, human ; ATF1 protein, human ; Activating Transcription Factor 1 ; Aquaporins ; Isoenzymes ; Polysaccharides ; RNA, Messenger ; RNA, Small Interfering ; Aquaporin 1 (146410-94-8) ; NGLY1 protein, human (EC 3.5.1.52) ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (EC 3.5.1.52)
Language	English
Publishing date	2019-12-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2019.11.097
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Article ; Online: Uridine monophosphate (UMP)-responsive developmental and epileptic encephalopathy

Ali Al-Otaibi / Alaa AlAyed / Asma Al Madhi / Leena Saeed / Bobby G. Ng / Hudson H. Freeze / Mohammed Almannai

Molecular Genetics and Metabolism Reports, Vol 30, Iss , Pp 100835- (2022)

A case report of two siblings and a review of literature

2022

Abstract: Developmental and epileptic encephalopathy type 50 is an autosomal recessive disorder caused by pathogenic variants in CAD. This gene encodes a multifunctional enzyme involved in the initial steps of de novo pyrimidine synthesis. Uridine treatment has ... ...

Abstract	Developmental and epileptic encephalopathy type 50 is an autosomal recessive disorder caused by pathogenic variants in CAD. This gene encodes a multifunctional enzyme involved in the initial steps of de novo pyrimidine synthesis. Uridine treatment has been shown to be effective in this disease. Here, we report two siblings with CAD pathogenic variants who presented with developmental regression and intractable epilepsy. Treatment with oral uridine monophosphate (UMP) resulted in remarkable and rapid clinical improvement in terms of developmental progress and seizure control. We also reviewed previous literature and summarized all reported patients to date.
Keywords	Uridine ; CAD ; Seizure ; Developmental delay ; Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Uridine monophosphate (UMP)-responsive developmental and epileptic encephalopathy: A case report of two siblings and a review of literature.

Al-Otaibi, Ali / AlAyed, Alaa / Al Madhi, Asma / Saeed, Leena / Ng, Bobby G / Freeze, Hudson H / Almannai, Mohammed

Molecular genetics and metabolism reports

2021 Volume 30, Page(s) 100835

Abstract: Developmental and epileptic encephalopathy type 50 is an autosomal recessive disorder caused by pathogenic variants ... ...

Abstract	Developmental and epileptic encephalopathy type 50 is an autosomal recessive disorder caused by pathogenic variants in
Language	English
Publishing date	2021-12-16
Publishing country	United States
Document type	Case Reports
ZDB-ID	2821908-9
ISSN	2214-4269
ISSN	2214-4269
DOI	10.1016/j.ymgmr.2021.100835
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Article: Therapeutic Monosaccharides: Looking Back, Moving Forward

Sosicka, Paulina / Ng, Bobby G / Freeze, Hudson H

Biochemistry. 2019 Aug. 09, v. 59, no. 34

2019

Abstract	In this review, we focus on the metabolism of mammalian glycan-associated monosaccharides, where the vast majority of our current knowledge comes from research done during the 1960s and 1970s. Most monosaccharides enter the cell using distinct, often tissue specific transporters from the SLC2A family. If not catabolized, these monosaccharides can be activated to donor nucleotide sugars and used for glycan synthesis. Apart from exogenous and dietary sources, all monosaccharides and their associated nucleotide sugars can be synthesized de novo, using mostly glucose to produce all nine nucleotide sugars present in human cells. Today, monosaccharides are used as treatment options for a small number of rare genetic disorders and even some common conditions. Here, we cover therapeutic applications of these sugars and highlight biochemical gaps that must be revisited as we go forward.
Keywords	cells ; dietary nutrient sources ; genetic disorders ; glucose ; humans ; knowledge ; metabolism ; research ; synthesis ; therapeutics ; transporters
Language	English
Dates of publication	2019-0809
Size	p. 3064-3077.
Publishing place	American Chemical Society
Document type	Article
Note	NAL-light
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.9b00565
Database	NAL-Catalogue (AGRICOLA)

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