Cloning and expression of an alternatively spliced mRNA encoding a soluble form of the human interleukin-6 signal transducer gp130.

摘要: The membrane-bound gp130 glycoprotein acts as an affinity converting and signal transducing receptor (R) for interleukin-6 several other cytokines. In this work, we RT-PCR amplified cDNA using primers flanking the sequence encoding transmembrane domain of gp130. We observed in blood mononuclear cells, addition to expected 333-bp length fragment, a second major band 418 bp. Sequencing 418-bp fragment its genomic counterpart showed new 85-bp exon located extracellular region protein. This is most likely due alternative splicing leads frame-shift resulting stop-codon 1 bp before coding region. Correspondingly, supernatants from chinese hamster ovary cells transfected with contained 4-5 times more soluble (s) than Both alternatively spliced sgp130 were also transcribed by myeloma cell lines XG-1, XG-2, XG-4, XG-4CNTF XG-6, XG-7, XG-9, XG-10, U266 RPMI 8226. However, XG-4A derived XG-4 but growing independently exogenous IL-6, did not transcribe mRNA. A possible interference intracrine stimulatory factors needs be further investigated.