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2018 ; 19
(2
): ä Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
Unravelling Immunoglobulin G Fc N-Glycosylation: A Dynamic Marker Potentiating
Predictive, Preventive and Personalised Medicine
#MMPMID29382131
Russell A
; Adua E
; Ugrina I
; Laws S
; Wang W
Int J Mol Sci
2018[Jan]; 19
(2
): ä PMID29382131
show ga
Multiple factors influence immunoglobulin G glycosylation, which in turn affect
the glycoproteins' function on eliciting an anti-inflammatory or pro-inflammatory
response. It is prudent to underscore these processes when considering the use of
immunoglobulin G N-glycan moieties as an indication of disease presence,
progress, or response to therapeutics. It has been demonstrated that the altered
expression of genes that encode enzymes involved in the biosynthesis of
immunoglobulin G N-glycans, receptors, or complement factors may significantly
modify immunoglobulin G effector response, which is important for regulating the
immune system. The immunoglobulin G N-glycome is highly heterogenous; however, it
is considered an interphenotype of disease (a link between genetic predisposition
and environmental exposure) and so has the potential to be used as a dynamic
biomarker from the perspective of predictive, preventive, and personalised
medicine. Undoubtedly, a deeper understanding of how the multiple factors
interact with each other to alter immunoglobulin G glycosylation is crucial.
Herein we review the current literature on immunoglobulin G glycoprotein
structure, immunoglobulin G Fc glycosylation, associated receptors, and
complement factors, the downstream effector functions, and the factors associated
with the heterogeneity of immunoglobulin G glycosylation.