Galectin-9 binds to O-glycans on protein disulfide isomerase
作者： Katrin Schaefer , Nicholas E Webb , Mabel Pang , Jenny E Hernandez-Davies , Katharine P Lee
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摘要: Changes in the T cell surface redox environment regulate critical functions, such as migration, viral entry and cytokine production. Cell protein disulfide isomerase (PDI) contributes to regulation of status. PDI can be released into extracellular milieu or internalized by cells. We have found that galectin-9, a soluble lectin expressed cells, endothelial cells dendritic binds retains on surface. While endogenous galectin-9 is not required for basal expression, exogenous mediated retention shifted disulfide/thiol equilibrium O-glycans are binding, recognition appears specific galectin-1 galectin-3 do bind PDI. Galectin-9 widely immune inflamed tissues, suggesting would exposed abundant cis trans, infectious autoimmune conditions.
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