BACKGROUND: Interleukin-17 receptor-like protein (IL-17RL) expressed in prostate tissues changes with advanced cancers due to extensive alternative splicing, which affects the final protein. Predominant IL-17RL splice isoform variants have not been identified, hindering functional studies. METHODS: A cDNA library of IL-17RL transcripts was arrayed onto nylon membranes. Individual transcript exon structures were determined by successively probing membranes with exon-specific oligonucleotides. The most common variants were transiently over-expressed in 293T cells. RESULTS: We detected >90 different IL-17RL isoforms. Three most abundant isoforms account for approximately half the total transcripts; the full-length variant just over 11%. Surprisingly, most alternative splicing does not alter the reading frame of the full-length molecule; therefore, resulting proteins vary mostly in N-terminal domains. CONCLUSIONS: IL-17RL exists as multiple isoforms due to extensive alternative splicing. We identified the most abundant splices in prostate tissue and established a technique to investigate changes in RNA IL-17RL splicing that occur in advanced cancers. (c) 2006 Wiley-Liss, Inc.
BACKGROUND:Interleukin-17 receptor-like protein (IL-17RL) expressed in prostate tissues changes with advanced cancers due to extensive alternative splicing, which affects the final protein. Predominant IL-17RL splice isoform variants have not been identified, hindering functional studies. METHODS: A cDNA library of IL-17RL transcripts was arrayed onto nylon membranes. Individual transcript exon structures were determined by successively probing membranes with exon-specific oligonucleotides. The most common variants were transiently over-expressed in 293T cells. RESULTS: We detected >90 different IL-17RL isoforms. Three most abundant isoforms account for approximately half the total transcripts; the full-length variant just over 11%. Surprisingly, most alternative splicing does not alter the reading frame of the full-length molecule; therefore, resulting proteins vary mostly in N-terminal domains. CONCLUSIONS:IL-17RL exists as multiple isoforms due to extensive alternative splicing. We identified the most abundant splices in prostate tissue and established a technique to investigate changes in RNA IL-17RL splicing that occur in advanced cancers. (c) 2006 Wiley-Liss, Inc.
Authors: Jill M Kramer; Walter Hanel; Fang Shen; Nilgun Isik; James P Malone; Amarnath Maitra; Wade Sigurdson; David Swart; Joel Tocker; Tian Jin; Sarah L Gaffen Journal: J Immunol Date: 2007-11-15 Impact factor: 5.422
Authors: Madhu V Singh; Michael Z Cicha; Santosh Kumar; David K Meyerholz; Kaikobad Irani; Mark W Chapleau; François M Abboud Journal: J Allergy Clin Immunol Date: 2017-01-16 Impact factor: 10.793