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• W2156598730 abstract "Abstract The two known isoforms of IL-15 contain either a long signal peptide (LSP) or a short signal peptide (SSP), and are produced by alternatively spliced transcripts. It has been proposed that SSP IL-15 remains exclusively intracellular, and its function is unclear. In this study, we show that, similar to LSP IL-15, the SSP IL-15 is stabilized and secreted efficiently upon coexpression of IL-15Rα. Coinjection of SSP IL-15- and IL-15Rα-expressing plasmids into mice resulted in increased plasma levels of bioactive heterodimeric IL-15 and mobilization and expansion of NK and T cells. Therefore, SSP IL-15 is secreted and bioactive when produced as a heterodimer with IL-15Rα in the same cell. The apparent t1/2 of this heterodimer is lower compared with LSP IL-15/IL-15Rα, due to different intracellular processing. Coexpression of both LSP IL-15 and SSP IL-15 in the presence of IL-15Rα results in lower levels of bioactive IL-15, indicating that LSP and SSP IL-15 compete for the binding to IL-15Rα when expressed in the same cell. Because the SSP IL-15 interaction to IL-15Rα leads to a complex with lower apparent stability, SSP IL-15 functions as competitive inhibitor of LSP IL-15. The data suggest that usage of alternative splicing is an additional level of control of IL-15 activity. Expression of both SSP and LSP forms of IL-15 appears to be conserved in many mammals, suggesting that SSP may be important for expressing a form of IL-15 with lower magnitude or duration of biological effects." @default.
• W2156598730 created "2016-06-24" @default.
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• W2156598730 date "2009-09-01" @default.
• W2156598730 modified "2023-10-11" @default.
• W2156598730 title "Secretion and Biological Activity of Short Signal Peptide IL-15 Is Chaperoned by IL-15 Receptor Alpha In Vivo" @default.
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• W2156598730 doi "https://doi.org/10.4049/jimmunol.0900693" @default.
• W2156598730 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7250482" @default.
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• W2156598730 hasPublicationYear "2009" @default.
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