Stocks S C, Albrechtsen M, Kerr M A
Department of Pathology, University of Dundee, Ninewells Hospital, Scotland, U.K.
Biochem J. 1990 Jun 1;268(2):275-80. doi: 10.1042/bj2680275.
The expression of the carbohydrate antigen 3-fucosyl-N-acetyl-lactosamine (CD15, LeX) on human neutrophil glycoproteins has been studied by immunoprecipitation and immunoblotting by using monoclonal antibody MC2. The antigen is expressed on membrane glycoproteins of approximate molecular mass 165 and 105 kDa. These glycoproteins include the complement receptor and adhesion molecule, CR3, in which the beta-chain (CD18, 105 kDa) shows much greater expression than the alpha-chain (CD11b, 165 kDa). Most of the 165 kDa CD15 antigen is accounted for by expression on the carcinoembryonic antigen (CEA)-related molecule NCA160. Other members of this family, NCA95, NCA90 and NCA55, which are also found in neutrophils, do not express the CD15 antigen. There is a marked increase in the surface expression of CD15, CR3 and the antigen recognized by anti-CEA antibodies upon activation of neutrophils by the chemotactic peptide N-formylmethionyl-leucylphenylalanine.
通过使用单克隆抗体MC2进行免疫沉淀和免疫印迹，对人中性粒细胞糖蛋白上的碳水化合物抗原3-岩藻糖基-N-乙酰乳糖胺（CD15，LeX）的表达进行了研究。该抗原表达于分子量约为165 kDa和105 kDa的膜糖蛋白上。这些糖蛋白包括补体受体和粘附分子CR3，其中β链（CD18，105 kDa）的表达比α链（CD11b，165 kDa）高得多。165 kDa的CD15抗原大部分是由癌胚抗原（CEA）相关分子NCA160上的表达所致。该家族的其他成员，即也存在于中性粒细胞中的NCA95、NCA90和NCA55，不表达CD15抗原。在用趋化肽N-甲酰甲硫氨酰-亮氨酰-苯丙氨酸激活中性粒细胞后，CD15、CR3以及抗CEA抗体识别的抗原的表面表达显著增加。
