A group from Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi’an, China, etc. has reported about aberrant glycosylation associated with osteoarthritis (OA).
https://arthritis-research.biomedcentral.com/articles/10.1186/s13075-023-03084-w
The abnormal glycopatterns and heterogeneities of site-specific glycosylation associated with Osteoarthritis (OA) were investigated by using Lectin microarrays and LC-MS/MS.
It was found that abnormal glycosylation, including a high level of α-1,3/6 fucosylation and low level of high-mannose type N-glycan, was obsedeved in OA cartilages.
Heterogeneities of glycoforms on Fibronectin(FN1) and Aggrecan core protein (ACAN) were new features of OA cartilage. These proteins were mainly localized in the extracellular region and extracellular space.
In detail, as for Fibronectin(FN1)-N528, N4H5S2 almost disappered and N4H4F1S1 greatly increased,
as for Aggrecan core protein (ACAN)-N333, N5H8F1 almost disappered and N6H4S1, N4H3F1, N5H3F1, N2H5, N6H4 significantly increased,
and as for Aggrecan core protein (ACAN)-N658, N5H4F1S2, N6H6F1, N6H7, N7H6 almost disappered and N2H11 significantly increased.