Enzymatic insights into an inherited genetic disorder

Zhang, Liping; Hagen, Karl S.

doi:10.7554/elife.31127

Cited by 2 publications

(1 citation statement)

References 11 publications

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“…The level of protein loss (that is, loss of PNGase, encoded by NGLY1) correlates with neurological dysfunction, abnormal tear production and liver disease 40 ; a nonsense mutation is associated with a particularly severe disease phenotype. PNGase is responsible for the translocation of misfolded proteins across the ER membrane into the cytosol for subsequent degradation by the proteasome 41 . A Drosophila model of PNGase deficiency led to the identification of various cellular processes associated with PNGase deficiency, including disruption of mitochondrial physiology, reduced cellular respiratory capacity and altered regulation of bone morphogenetic protein 42–44 .…”

Section: Congenital Disorders Of Glycosylationmentioning

confidence: 99%

Glycosylation in health and disease

et al. 2019

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The glycom e describes the complete repertoire of glycoconjugates com posed of carbohydrate chains, or glycans, that are covalently linked to lipid or protein molecules. Glycoconjugates are formed through a process called glycosylation and can differ in their glycan sequences, the connections between them and their length. Glycoconjugate synthesis is a dynamic process that depends on the local milieu of enzymes, sugar precursors and organelle structures as well as the cell types involved and cellular signals. Studies of rare genetic disorders that affect glycosylation first highlighted the biological importance of the glycome, and technological advances have improved our understanding of its heterogeneity and complexity. Researchers can now routinely assess how the secreted and cell-surface glycom es reflect overall cellular status in health and disease. In fact, changes in glycosylation can modulate inflammatory responses, enable viral immune escape, promote cancer cell metastasis or regulate apoptosis; the com position of the glycom e also affects kidney function in health and disease. New insights into the structure and function of the glycom e can now be applied to therapy developm ent and could improve our ability tofine-tune im m unological responses and inflammation, optimize the performance of therapeutic antibodies and boost immune responses to cancer. These examples illustrate the potential of the emerging field of 'glycomedicine'.

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