Pommier C G, O'Shea J, Chused T, Takahashi T, Ochoa M, Nutman T B, Bianco C, Brown E J
Blood. 1984 Oct;64(4):858-66.
Plasma fibronectin (Fn) induces phagocytosis of C3b-opsonized sheep erythrocytes (EC3b) by human peripheral blood monocytes. However, Fn does not induce erythrophagocytosis of EC3b by human polymorphonuclear leukocytes (PMN), unless the PMN have been exposed to C5a or N-formyl-methionyl-leucyl-phenylalanine. Because of this difference, it is of great interest to examine Fn binding to cells that possess the capacity to differentiate into either granulocytes or monocytes. Hence, we have examined the consequences of Fn binding to the human myelomonocytic cell line, HL-60, both before and after in vitro differentiation of the HL-60, along a monocytoid or a granulocytoid pathway. Fn receptors were not found on undifferentiated HL-60, but several differentiating agents promoted the HL-60 binding of Fn-coated microspheres (Fn-ms). The peak of Fn-ms binding occurred four to five days after the induction of differentiation with dimethylsulfoxide (DMSO), and two days after induction by PMA. In addition, cells that differentiated along either the monocytoid or the granulocytoid pathway showed a marked increase in the phagocytosis of both IgG-coated erythrocytes (EA) and EC3b when they were exposed to Fn. Comparison of the effects of anti-Fn monoclonals on the binding of Fn-ms to the monocytes, PMN, and HL-60 showed that the same monoclonals block Fn-ms-binding and Fn-induced EC3b phagocytosis by all three cell types. Two monoclonal antibodies, M1/70 and A6F10, directed against membrane antigens on PMN and monocytes, inhibited Fn-ms binding. Both also blocked Fn-induced EC3b ingestion by these cells. However, neither antibody blocked Fn-ms binding or EC3b ingestion by differentiated HL-60. We conclude that differentiated HL-60 cells express functionally active Fn receptors, similar to monocytes and activated PMN, which, nonetheless, differ from normal cells in their association with the antigens recognized by M1/70 and A6F10.
血浆纤连蛋白(Fn)可诱导人外周血单核细胞对C3b调理的绵羊红细胞(EC3b)进行吞噬作用。然而,Fn不会诱导人多形核白细胞(PMN)对EC3b进行红细胞吞噬作用,除非PMN已暴露于C5a或N-甲酰甲硫氨酰-亮氨酰-苯丙氨酸。由于这种差异,研究Fn与具有分化为粒细胞或单核细胞能力的细胞的结合情况就变得非常有趣。因此,我们研究了在体外将HL-60沿单核细胞样或粒细胞样途径分化之前和之后,Fn与人类骨髓单核细胞系HL-60结合的后果。未分化的HL-60上未发现Fn受体,但几种分化剂可促进HL-60对Fn包被微球(Fn-ms)的结合。在用二甲基亚砜(DMSO)诱导分化后四到五天,以及用佛波酯(PMA)诱导后两天,Fn-ms结合达到峰值。此外,沿单核细胞样或粒细胞样途径分化的细胞在暴露于Fn时,对IgG包被的红细胞(EA)和EC3b的吞噬作用均显著增加。抗Fn单克隆抗体对Fn-ms与单核细胞、PMN和HL-60结合的影响比较表明,相同的单克隆抗体可阻断所有三种细胞类型的Fn-ms结合和Fn诱导的EC3b吞噬作用。两种针对PMN和单核细胞膜抗原的单克隆抗体M1/70和A6F10可抑制Fn-ms结合。两者还可阻断这些细胞对Fn诱导EC3b摄取。然而,这两种抗体均未阻断分化的HL-60对Fn-ms的结合或EC3b摄取。我们得出结论,分化的HL-60细胞表达功能活跃的Fn受体,类似于单核细胞和活化的PMN,尽管如此,它们与M1/70和A6F10识别的抗原的关联与正常细胞不同。