Todd R F, Arnaout M A, Rosin R E, Crowley C A, Peters W A, Babior B M
J Clin Invest. 1984 Oct;74(4):1280-90. doi: 10.1172/JCI111538.
Mo1 alpha (formerly gp 110) is a neutrophil glycoprotein whose deficiency is associated with abnormalities in several neutrophil functions, including defects in adherence, chemotaxis, and phagocytosis. Examination of whole cells and subcellular components by the use of both immunological and electrophoretic techniques demonstrated that Mo1 alpha was located primarily in the specific granules but that a small portion was present in the plasma membrane, where it is exposed to the extracellular environment and can bind to anti-Mo1 antibody. During degranulation, Mo1 alpha is translocated from the specific granules to the plasma membrane, resulting in a 5-10-fold increase in the surface expression of this glycoprotein. These findings plus previous work suggest that plasma membrane-associated Mo1 alpha is needed for a normal interaction between neutrophils and underlying surfaces, and raise the possibility that the increase in surface adhesiveness of neutrophils that have discharged their specific granules might be due in part to the increase in the amount of Mo1 alpha in the plasma membranes of these degranulated cells.
Mo1α（以前称为gp 110）是一种中性粒细胞糖蛋白，其缺乏与几种中性粒细胞功能异常有关，包括黏附、趋化和吞噬缺陷。通过免疫和电泳技术对全细胞和亚细胞成分进行检测表明，Mo1α主要位于特定颗粒中，但有一小部分存在于质膜中，在质膜中它暴露于细胞外环境并能与抗Mo1抗体结合。在脱颗粒过程中，Mo1α从特定颗粒转移到质膜，导致这种糖蛋白的表面表达增加5至10倍。这些发现以及先前的研究表明，质膜相关的Mo1α是中性粒细胞与下层表面正常相互作用所必需的，并增加了这样一种可能性，即已排出其特定颗粒的中性粒细胞表面黏附性增加可能部分归因于这些脱颗粒细胞质膜中Mo1α量的增加。
