Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease

Burt, Rajan A.; Alghusen, Ibtihal; Ephrame, Sophiya John; Villar, María T.; Artigues, Antonio; Slawson, Chad

doi:10.3389/fmolb.2022.920727

Cited by 8 publications

(10 citation statements)

References 147 publications

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“…(3) How is O-GlcNAcylation regulated in different tissues in physiological and pathophysiological contexts? These questions require advances in detection methods for O-GlcNAcylated sites and cell-specific knock-out models that are being currently developed by different groups [ 159 , 160 , 161 ]. Current detection limitations still delay the development of the protein O-GlcNAcylation field.…”

Section: Discussionmentioning

confidence: 99%

“…Compared to protein phosphorylation, the development of specific antibodies to detect single site O-GlcNAcylation have intrinsic biological limitations (detection of GlcNAc-modified sites by antibodies). Additionally, the detection tools currently being employed are complex and expensive, such as O-GlcNAc labelling followed by mass spectrometry analysis [ 159 ]. Recent advances such as chemical reporters and biorthogonal reactions, however, are promising strategies to foster future protein O-GlcNAcylation studies [ 162 ].…”

Section: Discussionmentioning

confidence: 99%

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O-GlcNAcylation in Renal (Patho)Physiology

Silva-Aguiar

Peruchetti

Pinheiro

et al. 2022

IJMS

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Kidneys maintain internal milieu homeostasis through a well-regulated manipulation of body fluid composition. This task is performed by the correlation between structure and function in the nephron. Kidney diseases are chronic conditions impacting healthcare programs globally, and despite efforts, therapeutic options for its treatment are limited. The development of chronic degenerative diseases is associated with changes in protein O-GlcNAcylation, a post-translation modification involved in the regulation of diverse cell function. O-GlcNAcylation is regulated by the enzymatic balance between O-GlcNAc transferase (OGT) and O-GlcNAcase( OGA) which add and remove GlcNAc residues on target proteins, respectively. Furthermore, the hexosamine biosynthetic pathway provides the substrate for protein O-GlcNAcylation. Beyond its physiological role, several reports indicate the participation of protein O-GlcNAcylation in cardiovascular, neurodegenerative, and metabolic diseases. In this review, we discuss the impact of protein O-GlcNAcylation on physiological renal function, disease conditions, and possible future directions in the field.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

O-GlcNAcylation in Renal (Patho)Physiology

Silva-Aguiar

Peruchetti

Pinheiro

et al. 2022

IJMS

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“…O-GlcNAc glycosylation modification is widely involved in many cells’ life processes, such as cell cycle, gene transcription, protein translation and processing, and signal transduction. Abnormal modification of O-GlcNAc glycosylation occurred in many diseases [ 42 ]. Studies have confirmed that OGT is highly expressed in liver tumors [ 43 ], colon tumors, bladder cancer, and breast cancers [ 44 ].…”

Section: Discussionmentioning

confidence: 99%

LncRNA EBLN3P attributes methotrexate resistance in osteosarcoma cells through miR-200a-3p/O-GlcNAc transferase pathway

Sun

Sun³

et al. 2022

J Orthop Surg Res

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Background Osteosarcoma is highly malignant. The migration, invasion, and chemoresistance contribute to poor prognosis of osteosarcoma. Research reported that endogenous bornavirus-like nucleoprotein 3 pseudogene (EBLN3P) promotes the progression of osteosarcoma. Methods In this study, the expression of EBLN3P in osteosarcoma tissue with different methotrexate (MTX) treatment responses was measured. Osteosarcoma cell lines with MTX resistance were constructed, and bioinformatic analysis was performed to explore the potential involved targets and pathways. Results Higher EBLN3P was associated with MTX resistance. Downregulation of LncEBLN3P decreased the MTX resistance of osteosarcoma cells by sponging miR-200a-3p, an important microRNA that affects epithelial-mesenchymal transition (EMT). The decreased miR-200a-3p resulted in the upregulation of its target gene O-GlcNAc transferase (OGT), which in turn promoted the EMT process of osteosarcoma cells. Further analysis confirmed that the loss of OGT and over-expression of miR-200a-3p could partly abolish the MTX resistance induced by LncEBLN3P. Conclusion LncEBLN3P is upregulated in osteosarcoma and increases the MTX resistance in osteosarcoma cells through downregulating miR-200a-3p, which in turn promoted the EMT process of osteosarcoma cells by increasing the OGT.

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“…O -GlcNAcylation is extremely common, generally underappreciated, and catalyzed within the cytoplasm by a single enzyme, O -GlcNAc transferase (OGT). 15 This modification appears to have fairly rapid on/off rates and competes with phosphorylation at the same or adjacent sites creating a means of intracellular signaling. 16 …”

Section: Oligosaccharide Structure and Biosynthesismentioning

confidence: 99%

Mass Spectrometry-Based Glycoproteomic Workflows for Cancer Biomarker Discovery

Doud

Yeh

2023

Technol Cancer Res Treat

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Glycosylation has a clear role in cancer initiation and progression, with numerous studies identifying distinct glycan features or specific glycoproteoforms associated with cancer. Common findings include that aggressive cancers tend to have higher expression levels of enzymes that regulate glycosylation as well as glycoproteins with greater levels of complexity, increased branching, and enhanced chain length1. Research in cancer glycoproteomics over the last 50-plus years has mainly focused on technology development used to observe global changes in glycosylation. Efforts have also been made to connect glycans to their protein carriers as well as to delineate the role of these modifications in intracellular signaling and subsequent cell function. This review discusses currently available techniques utilizing mass spectrometry-based technologies used to study glycosylation and highlights areas for future advancement.

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Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease

Cited by 8 publications

References 147 publications

O-GlcNAcylation in Renal (Patho)Physiology

O-GlcNAcylation in Renal (Patho)Physiology

LncRNA EBLN3P attributes methotrexate resistance in osteosarcoma cells through miR-200a-3p/O-GlcNAc transferase pathway

Mass Spectrometry-Based Glycoproteomic Workflows for Cancer Biomarker Discovery

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