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- W2127305145 abstract "CD8+ T-cell apoptosis is essential for the contraction phase of the immune response, yet the initiating signals and precise pathways involved are unresolved. The ST3Gal-I sialyltransferase is a candidate mechanistic component and catalyzes sialic acid addition to core 1 O-glycans during protein O glycosylation. ST3Gal-I inactivation or enzymatic removal of its product renders CD8+ T cells, but not CD4+ T cells, susceptible to apoptosis by differential cross-linking of O-glycoproteins in the absence of interleukin-2 and T-cell receptor (TCR) signaling. This results in caspase activation, DNA fragmentation, and phosphatidylserine externalization prior to cell death. We further show that ST3Gal-I function is regulated by a posttranscriptional mechanism operating distal to Golgi core 2 O glycosylation and is invariably linked to CD8+ T-cell contraction following viral (lymphocytic choriomeningitis virus) infection and bacterial (staphylococcal enterotoxin B) antigen immunization. The mechanism does not involve the ST3Gal-I substrate CD43 or core 2 O-glycan induction and overcomes the ability of Bcl-2 to inhibit the contraction phase in vivo. Loss of ST3Gal-I function further reduces Bim-deficient CD8+ T-cell accumulation without diminishing apoptotic sensitivity. We propose that an endogenous lectin activates an apoptotic pathway constructed in CD8+ T cells following TCR stimulation and enables contraction upon attenuation of immune signaling." @default.
- W2127305145 created "2016-06-24" @default.
- W2127305145 creator A5022635870 @default.
- W2127305145 creator A5054758763 @default.
- W2127305145 creator A5091291146 @default.
- W2127305145 date "2007-02-01" @default.
- W2127305145 modified "2023-10-18" @default.
- W2127305145 title "Structural and Mechanistic Features of Protein O Glycosylation Linked to CD8<sup>+</sup> T-Cell Apoptosis" @default.
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- W2127305145 doi "https://doi.org/10.1128/mcb.01750-06" @default.
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