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A NEW ALTERNATIVE SPLICE VARIANT OF THE MOUSE FAS ANTIGEN WITH A DELETION IN THE N-TERMINAL PORTION OF THE EXTRACELLULAR DOMAIN

机译:小鼠FAS抗原的新替代变异体,其在胞外域的N末端部分缺失

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The Fas antigen (Fas/APO-1/CD95) has been shown to induce apoptosis when bound to a monoclonal anti-Fas antibody or Fas ligands. Recently, a new soluble human Fas isoform which lacks the transmembrane domain due to alternative splicing has been isolated; however, no mouse Fas isoforms have been reported so far. Analysis of Fas transcripts by RT-PCR detected no Fas transcripts corresponding, to the human soluble Fas isoform iii mouse thymus, spleen, and liver. However, we detected a new isoform with a 117-bp deletion in the second exon in various mouse tissues and cell lines. This isoform, termed truncated Fas (T-Fas), can be generated by alternative splicing and lacks the N-terminal portion of the extracellular domain just after the signal sequence. Since the deletion involves the first cysteine-rich motif believed to be necessary for binding to the Fas ligand, the T-Fas protein may lack the ability to induce apoptosis. The expression of T-Fas relative to that of the normal Fas varies considerably among mouse tissues and cell lines, suggesting preferential transcription of the T-Fas isoform in certain cell types. [References: 16]
机译:Fas抗原(Fas / APO-1 / CD95)已显示与单克隆抗Fas抗体或Fas配体结合时诱导凋亡。最近,已分离出一种新的可溶性人Fas亚型,该亚型由于选择性剪接而缺乏跨膜结构域。但是,到目前为止,尚无小鼠Fas亚型的报道。通过RT-PCR对Fas转录本进行分析,未检测到与人类可溶性Fas亚型iii小鼠胸腺,脾脏和肝脏相对应的Fas转录本。但是,我们在各种小鼠组织和细胞系的第二个外显子中检测到一个新的亚型,该亚型缺失117 bp。这种同种型称为截短Fas(T-Fas),可以通过选择性剪接生成,并且在信号序列之后就缺少细胞外域的N端部分。由于缺失涉及第一个富含半胱氨酸的基序,该基序被认为是与Fas配体结合所必需的,因此T-Fas蛋白可能缺乏诱导细胞凋亡的能力。在小鼠组织和细胞系中,T-Fas的表达相对于正常Fas的表达差异很大,这表明T-Fas同种型在某些细胞类型中优先转录。 [参考:16]

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