Kwiatkowska K, Sobota A
Nencki Institute of Experimental Biology, Department of Cell Biology, Warsaw, Poland.
Bioessays. 1999 May;21(5):422-31. doi: 10.1002/(SICI)1521-1878(199905)21:5<422::AID-BIES9>3.0.CO;2-#.
Phagocytosis is an uptake of large particles governed by the actin-based cytoskeleton. Binding of particles to specific cell surface receptors is the first step of phagocytosis. In higher Eucaryota, the receptors able to mediate phagocytosis are expressed almost exclusively in macrophages, neutrophils, and monocytes, conferring immunodefence properties to these cells. Receptor clustering is thought to occur upon particle binding, that in turn generates a phagocytic signal. Several pathways of phagocytic signal transduction have been identified, including the activation of tyrosine kinases and (or) serine/threonine kinase C in pivotal roles. Kinase activation leads to phosphorylation of the receptors and other proteins, recruited at the sites of phagocytosis. Monomeric GTPases of the Rho and ARF families are likely to be engaged downstream of activated receptors. The GTPases, in cooperation with phosphatidylinositol 4-phosphate 5-kinase and phosphatidylinositol 3-kinase lipid modifying enzymes, can modulate locally the assembly of the submembranous actin filament system leading to particle internalization.
吞噬作用是由基于肌动蛋白的细胞骨架控制的对大颗粒的摄取。颗粒与特定细胞表面受体的结合是吞噬作用的第一步。在高等真核生物中,能够介导吞噬作用的受体几乎只在巨噬细胞、中性粒细胞和单核细胞中表达,赋予这些细胞免疫防御特性。受体聚集被认为发生在颗粒结合时,这反过来又产生吞噬信号。已经确定了几种吞噬信号转导途径,包括关键作用的酪氨酸激酶和(或)丝氨酸/苏氨酸激酶C的激活。激酶激活导致受体和其他在吞噬部位募集的蛋白质的磷酸化。Rho和ARF家族的单体GTP酶可能在活化受体的下游起作用。这些GTP酶与磷脂酰肌醇4-磷酸5-激酶和磷脂酰肌醇3-激酶脂质修饰酶协同作用,可以局部调节膜下肌动蛋白丝系统组装,导致颗粒内化。