Yamamoto Y, Yamaguchi T, Sato K, Nishikawa Y, Hiragun A
Section of Tumor Cell Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
Exp Hematol. 1988 Jan;16(1):12-20.
SGP140, which has been isolated as the major sialoglycoprotein of 140 kd molecular weight from a human T-leukemic cell line, was identified on the cell surface of polymorphonuclear leukocytes (PMNs). Specific antibody against SGP140 was prepared in rabbits and was used to probe the function of SGP140 on PMNs in this study. PMNs from healthy donors that were treated with the anti-SGP140 IgG showed remarkably diminished chemotactic as well as phagocytic activity. Phagocytosis of both C3- and IgG-opsonized particles were affected similarly by the antibody treatment. The antibody neither affected cell adhesion and spreading over substrate, nor did it disturb the other functions of PMNs, i.e., enzyme release and superoxide generation. N-formyl-methionyl-leucyl-phenylalanine did not stimulate SGP140 expression on cell surfaces. We present evidence that SGP140 is distinct from the glycoprotein family (Mac-1, LFA-1, and p150/95 [CDw 18]) that performs adhesive reactions of leukocytes. We propose that SGP140 is a novel molecule on the human PMN cell surface that is involved both in chemotactic and phagocytic activities.
SGP140是从人T白血病细胞系中分离出的一种分子量为140kd的主要唾液糖蛋白，在多形核白细胞（PMN）的细胞表面被鉴定出来。本研究中，用兔制备了抗SGP140特异性抗体，并用于探究SGP140在PMN上的功能。用抗SGP140 IgG处理的健康供体的PMN表现出趋化活性和吞噬活性显著降低。抗体处理对C3和IgG调理颗粒的吞噬作用影响相似。该抗体既不影响细胞在底物上的黏附和铺展，也不干扰PMN的其他功能，即酶释放和超氧化物生成。N-甲酰甲硫氨酰亮氨酰苯丙氨酸不会刺激细胞表面SGP140的表达。我们提供的证据表明，SGP140不同于执行白细胞黏附反应的糖蛋白家族（Mac-1、LFA-1和p150/95 [CDw 18]）。我们提出，SGP140是人类PMN细胞表面的一种新分子，参与趋化和吞噬活动。
