NCBI Summary:
The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolyisis. Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is presently unknown.
This gene was found in bovine oocyte by Dalbies-Tran R, Mermillod P. 2003 . The authors have analyzed gene expression in bovine oocytes before and after in vitro maturation (IVM) using heterologous hybridization onto cDNA array. Total RNA was purified from pools of over 200 oocytes either immediately after aspiration from follicles at the surface of slaughterhouse cow ovaries or following in vitro maturation. Radiolabeled cDNA probes were generated by reverse-transcription followed by linear PCR amplification and were hybridized to Atlas human cDNA arrays. To our knowledge, this is the first report of gene expression profiling by this technology in the mammalian female germ cell. Our results demonstrate that cDNA array screening is a suitable method for analyzing the transcription pattern in oocytes. About 300 identified genes were reproducibly shown to be expressed in the bovine oocyte, the largest profile available so far in this model. The relative abundance of most messenger RNAs appeared stable during IVM. However, 70 transcripts underwent a significant differential regulation (by a factor of at least two). Their potential role in the context of oocyte maturation is discussed. Together they constitute a molecular signature of the degree of oocyte cytoplasmic maturation achieved in vitro.