Galectin-9 binds to O-glycans on protein disulfide isomerase.
Glycobiology
; 27(9): 878-887, 2017 09 01.
Article
em En
| MEDLINE
| ID: mdl-28810662
ABSTRACT
Changes in the T cell surface redox environment regulate critical cell functions, such as cell migration, viral entry and cytokine production. Cell surface protein disulfide isomerase (PDI) contributes to the regulation of T cell surface redox status. Cell surface PDI can be released into the extracellular milieu or can be internalized by T cells. We have found that galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface. While endogenous galectin-9 is not required for basal cell surface PDI expression, exogenous galectin-9 mediated retention of cell surface PDI shifted the disulfide/thiol equilibrium on the T cell surface. O-glycans on PDI are required for galectin-9 binding, and PDI recognition appears to be specific for galectin-9, as galectin-1 and galectin-3 do not bind PDI. Galectin-9 is widely expressed by immune and endothelial cells in inflamed tissues, suggesting that T cells would be exposed to abundant galectin-9, in cis and in trans, in infectious or autoimmune conditions.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Linfócitos T
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Membrana Celular
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Isomerases de Dissulfetos de Proteínas
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Galectinas
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Galectina 1
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article