Hibbs M L, Selvaraj P, Carpén O, Springer T A, Kuster H, Jouvin M H, Kinet J P
Department of Pathology, Harvard Medical School, Boston, MA 02115.
Science. 1989 Dec 22;246(4937):1608-11. doi: 10.1126/science.2531918.
Granulocyte and natural killer (NK) cell Fc receptors for immunoglobulin G (CD16) differ in only a few amino acids, yet have phosphatidylinositol glycan (PIG) or polypeptide membrane anchors, respectively. Mutagenesis shows that anchoring is regulated by a serine residue near the PIG anchor attachment site in the extracellular domain. The NK cell isoform was not expressed on the surface of COS cells unless cotransfected with a subunit that was expressed in NK cells and that was identical to the gamma subunit of the high affinity IgE Fc receptor (Fc epsilon RI). However, the CD16 sequence and not expression of the gamma subunit is dominant in regulating PIG reanchoring.
粒细胞和自然杀伤（NK）细胞的免疫球蛋白G Fc受体（CD16）仅在少数氨基酸上存在差异，但分别具有磷脂酰肌醇聚糖（PIG）或多肽膜锚定结构。诱变研究表明，锚定作用受细胞外区域中PIG锚定连接位点附近的一个丝氨酸残基调控。除非与在NK细胞中表达且与高亲和力IgE Fc受体（FcεRI）的γ亚基相同的一个亚基共转染，否则NK细胞同种型不会在COS细胞表面表达。然而，在调节PIG重新锚定方面，CD16序列而非γ亚基的表达起主导作用。
