A novel splicing variant of mouse interleukin (IL)-24 antagonizes IL-24-induced apoptosis.

The Journal of Biological Chemistry
Anupama SahooSin-Hyeog Im

Abstract

Alternative splicing of mRNA enables functionally diverse protein isoforms to be expressed from a single gene, allowing transcriptome diversification. Interleukin (IL)-24/MDA-7 is a member of the IL-10 gene family, and FISP (IL-4-induced secreted protein), its murine homologue, is selectively expressed and secreted by T helper 2 lymphocytes. A novel splice variant of mouse IL-24/FISP, designated FISP-sp, lacks 29 nucleotides from the 5'-end of exon 4 of FISP. The level of FISP-sp expression is 10% of the level of total primary FISP transcription. Unlike FISP, FISP-sp does not induce growth inhibition and apoptosis. FISP-sp is exclusively localized in endoplasmic reticulum, and its expression is up-regulated by endoplasmic reticulum stress. Our results suggest that the novel splicing variant FISP-sp dimerizes with FISP and blocks its secretion and inhibits FISP-induced apoptosis in vivo.

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Citations

Aug 17, 2011·Cytokine·Erin L WhitakerPenelope J Duerksen-Hughes
Jun 9, 2016·International Journal of Molecular Sciences·Leah PersaudMoira Sauane
Oct 25, 2016·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Hongdan CaoXiaolan Huang
Jan 11, 2018·Journal of Immunology Research·Mihaela SurcelMonica Neagu
Sep 28, 2018·Journal of Leukocyte Biology·Jun ChenWai Po Chong
Jan 27, 2010·International Reviews of Immunology·Anupama Sahoo, Sin-Hyeog Im
Jun 23, 2018·Oncology Letters·Haimeng YanZhen Cai
Mar 27, 2020·Heliyon·Igor ShilovskiyMusa Khaitov

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