ACTIVATION OF HUMAN MONOCYTES AND GRANULOCYTES BY MONOCLONAL-ANTIBODIES TO GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED ANTIGENS
ACTIVATION OF HUMAN MONOCYTES AND GRANULOCYTES BY MONOCLONAL-ANTIBODIES TO GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED ANTIGENS
复制标题
DOI：
10.1002/eji.1830231110
复制
发表时间：
1993-11-01
影响因子：
5.4
通讯作者：
HOREJSI, V
中科院分区：
文献类型：
--
作者：
LUNDJOHANSEN, F;OLWEUS, J;HOREJSI, V
本研究探讨了可能的受体样特征的糖基磷脂酰肌醇（GPI）连接的抗原对人单核细胞和粒细胞通过测量细胞质钙流和氧化爆发后交联的GPI连接的抗原在细胞。细胞结合的抗-CD 14、-CDw 52和-CD 55的交联在未致敏的人单核细胞中诱导细胞质钙通量和氧化爆发，与Fc γ R交联后观察到的相似。在用200 nM N-甲酰基-Met-Leu-Phe（FMLP）引发的粒细胞中，细胞结合的抗-CD 16、-CD 24、-CD 59和-CD 67的交联导致钙通量和氧化爆发的激活。GPI连接的抗原介导的氧化爆发比200 nM FMLP诱导的氧化爆发更强。尽管FMLP诱导了胞浆钙浓度的较大增加。反应可能不依赖于Fc γ R相互作用，因为实验中使用了IgG或IgM抗体的F（ab '）（2）片段。在阵发性睡眠性血红蛋白尿症患者的细胞中未观察到GPI相关抗原单克隆抗体的激活作用，这些患者缺乏GPI相关抗原。此外，治疗与GPI特异性磷脂酶C导致抑制细胞活化通过GPI连接的抗原，但不是通过跨膜受体。许多非GPI连接抗原（CD 11 a、CD 18、CD 31、CD 35、CD 43和CD 45）的交联既不诱导钙流，也不激活氧化爆发。结果表明，大多数，如果不是全部，GPI连接的表面糖蛋白的髓细胞能够介导细胞活化，并建议GPI锚是一种结构，促进信号转导。
The present study investigated possible receptor-like characteristics of glycosylphosphatidylinositol (GPI)-linked antigens on human monocytes and granulocytes by measuring cytoplasmic calcium fluxes and the oxidative burst in cells following cross-linking of GPI-linked antigens. Cross-linking of cell-bound anti-CD14, -CDw52 and -CD55 induced cytoplasmic calcium fluxes and oxidative bursts in unprimed human monocytes similar to those observed following Fc gamma R cross-linking. In granulocytes primed with 200 nM N-formyl-Met-Leu-Phe (FMLP), cross-linking of cell-bound anti-CD16, -CD24, -CD59 and -CD67 led to calcium fluxes and activation of the oxidative burst. The oxidative bursts mediated by GPI-linked antigens were stronger than those induced by 200 nM FMLP. even though FMLP induced a larger increase in cytoplasmic calcium concentration. The responses were likely to be independent of Fc gamma R interactions as F(ab')(2) fragments of IgG or IgM antibodies were used in the experiments. Activating effects of monoclonal antibody to GPI-linked antigens were not observed in cells from patients with paroxysmal nocturnal hemoglobinuria, which are deficient in GPI-linked antigens. In addition, treatment with GPI-specific phospholipase C led to inhibition of cell activation through GPI-linked antigens but not through transmembrane receptors. Cross-linking of a number of non-GPI-linked antigens (CD11a, CD18, CD31, CD35, CD43, and CD45) neither induced calcium fluxes, nor activated the oxidative burst. The results indicate that most, if not all, GPI-linked surface glycoproteins on myeloid cells are capable of mediating cell activation and suggest that the GPI anchor is a structure facilitating signal transduction.