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ABSTRACT: Purpose
N-Glycan profiling provides an indicator of the cellular potential for functional pairing with tissue lectins. Following the discovery of galectin expression by chondrocytes as a factor in osteoarthritis pathobiology, mapping of N-glycans upon their phenotypic dedifferentiation in culture and in fibroblast-like synoviocytes is a step to better understand glycobiological contributions to disease progression.Experimental design
The profiles of cellular N-glycans of human osteoarthritic chondrocytes and fibroblast-like synoviocytes were characterized by mass spectrometry. RT-qPCR experiments determined mRNA levels of 16 glycosyltransferases. Responsiveness of cells to galectins was quantified by measuring the mRNA level for interleukin-1β.Results
The shift of chondrocytes to a fibroblastic phenotype (dedifferentiation) is associated with changes in N-glycosylation. The N-glycan profile of chondrocytes at passage 4 reflects characteristics of synoviocytes. Galectins-1 and -3 enhance expression of interleukin-1β mRNA in both cell types, most pronounced in primary culture. Presence of interleukin-1β leads to changes in sialylation in synoviocytes that favor galectin binding.Conclusions and clinical relevance
N-Glycosylation reflects phenotypic changes of osteoarthritic cells in vitro. Like chondrocytes, fibroblast-like synoviocytes express N-glycans that are suited to bind galectins, and these proteins serve as inducers of pro-inflammatory markers in these cells. Synoviocytes can thus contribute to disease progression in osteoarthritis in situ.
SUBMITTER: Fuehrer J
PROVIDER: S-EPMC8548877 | biostudies-literature |
REPOSITORIES: biostudies-literature