Moingeon P, Lucich J L, Reinherz E L
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA.
Int Immunol. 1992 Aug;4(8):955-8. doi: 10.1093/intimm/4.8.955.
We report the characterization of the Fc epsilon RI gamma chain which associates with the transmembrane form of CD16 to form the low affinity receptor for IgG (Fc gamma RIII) expressed on human natural killer (NK) cells. cDNA cloning and sequence analysis of Fc epsilon RI gamma from a polyclonal CD3-CD16+ NK line established that this molecule is identical to Fc epsilon RI gamma previously identified in human basophils as part of a high affinity receptor for IgE. Polymerase chain reaction analysis of Fc epsilon RI gamma gene expression in a series of CD3+CD16- and CD3-CD16+ NK clones reveals that Fc epsilon RI gamma is not directly linked to NK activity since clones of the CD3+CD16- phenotype lack Fc epsilon RI gamma RNA but nevertheless mediate cytotoxicity. Taken together, these results demonstrate that the Fc epsilon RI gamma molecule is expressed in various types within the hematopoietic system as part of multimeric surface receptors involved in different biological functions.
我们报告了FcεRIγ链的特征，它与CD16的跨膜形式结合，形成人类自然杀伤（NK）细胞上表达的IgG低亲和力受体（FcγRIII）。从一个多克隆CD3 - CD16 + NK细胞系克隆FcεRIγ的cDNA并进行序列分析，结果表明该分子与先前在人类嗜碱性粒细胞中鉴定为IgE高亲和力受体一部分的FcεRIγ相同。对一系列CD3 + CD16 - 和CD3 - CD16 + NK克隆中FcεRIγ基因表达的聚合酶链反应分析显示，FcεRIγ与NK活性没有直接联系，因为CD3 + CD16 - 表型的克隆缺乏FcεRIγRNA，但仍能介导细胞毒性。综上所述，这些结果表明FcεRIγ分子作为参与不同生物学功能的多聚体表面受体的一部分，在造血系统的各种类型细胞中表达。
