Aramburu J, Azzoni L, Rao A, Perussia B
Department of Microbiology and Immunology, Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
J Exp Med. 1995 Sep 1;182(3):801-10. doi: 10.1084/jem.182.3.801.
The putative factors that couple the signal transduction from surface receptors to the activation of cytokine synthesis in natural killer (NK) cells have not been elucidated. We report here that the nuclear factor of activated T cells (NFATp), a cyclosporin A (CsA)-sensitive factor that regulates the transcription of several cytokines, mediates CD16-induced activation of cytokine genes in human NK cells. CD16 (Fc gamma RIIIA)-induced expression of cytokine mRNA in NK cells occurs via a CsA-sensitive and Ca(2+)-dependent mechanism. Stimulation of NK cells with CD16 ligands induces NFAT-like DNA binding activity in the nuclear extracts from these cells, as detected in electrophoretic mobility shift assays. This occurs with fast kinetics after stimulation, via a CsA-sensitive and Ca(2+)-dependent mechanism that does not require de novo protein synthesis. NK cell NFAT is present in the cytosol of nonstimulated cells, migrates to the nucleus upon stimulation, and can associate with AP-1. Two distinct molecules, NFATp and NFATc, have been reported to mediate NFAT activity. The results of supershift assays using NFATp- and NFATc- specific antibodies indicate that NK cell activation early after CD16 ligand binding involves primarily, if not exclusively, NFATp, and Western blot analysis shows that this has the same electrophoretic mobility (approximately 120 kD) as that of T lymphocytes. NK cells do not express NFATc constitutively, but NFATc mRNA accumulation is induced in these cells within 2 h of stimulation with CD16 ligands. However, supershift assays using the available mAb recognizing the T cell NFATc revealed no detectable NFATc protein in nuclear and cytoplasmic extracts from CD16- or phorbol ester-stimulated cells at any time tested, up to 4 h. These results provide the first direct evidence that both CsA-sensitive transcription factors, NFATp and NFATc, are expressed in human NK cells, and that their activation and/or expression can be regulated in primary cells by a single stimulus, that, in the case of CD16 in NK cells, results in early activation of NFATp and subsequently induced expression of NFATc mRNA.
将自然杀伤(NK)细胞表面受体的信号转导与细胞因子合成激活联系起来的假定因子尚未阐明。我们在此报告,活化T细胞核因子(NFATp),一种对环孢素A(CsA)敏感且调节多种细胞因子转录的因子,介导人NK细胞中CD16诱导的细胞因子基因激活。CD16(FcγRIIIA)诱导NK细胞中细胞因子mRNA的表达是通过一种对CsA敏感且依赖Ca²⁺的机制实现的。用CD16配体刺激NK细胞会在这些细胞的核提取物中诱导出类似NFAT的DNA结合活性,这在电泳迁移率变动分析中可以检测到。刺激后这种情况快速发生,通过一种对CsA敏感且依赖Ca²⁺的机制,该机制不需要从头合成蛋白质。NK细胞NFAT存在于未刺激细胞的胞质溶胶中,刺激后迁移到细胞核,并可与AP-1结合。据报道,两种不同的分子NFATp和NFATc介导NFAT活性。使用NFATp和NFATc特异性抗体的超迁移分析结果表明,CD16配体结合后早期NK细胞的激活主要(如果不是唯一)涉及NFATp,蛋白质印迹分析表明其电泳迁移率(约120 kD)与T淋巴细胞相同。NK细胞不组成性表达NFATc,但在用CD16配体刺激这些细胞后2小时内会诱导NFATc mRNA积累。然而,使用识别T细胞NFATc的现有单克隆抗体进行的超迁移分析在测试的任何时间(长达4小时)都未在CD16或佛波酯刺激细胞的核提取物和细胞质提取物中检测到可检测到的NFATc蛋白。这些结果提供了首个直接证据,证明对CsA敏感的转录因子NFATp和NFATc都在人NK细胞中表达,并且它们的激活和/或表达可以在原代细胞中通过单一刺激进行调节,就NK细胞中的CD16而言,这种刺激会导致NFATp的早期激活以及随后诱导NFATc mRNA的表达。