McKnight A J, Macfarlane A J, Dri P, Turley L, Willis A C, Gordon S
Sir William Dunn School of Pathology, University of Oxford, United Kingdom.
J Biol Chem. 1996 Jan 5;271(1):486-9. doi: 10.1074/jbc.271.1.486.
F4/80 is a monoclonal antibody that recognizes a murine macrophage-restricted cell surface glycoprotein and has been extensively used to characterize macrophage populations in a wide range of immunological studies. Apart from the tightly regulated pattern of expression of the F4/80 antigen, little is known about its possible role in macrophage differentiation and function. We have sought to characterize the molecule at the molecular level, through the isolation of cDNA clones, and now describe the sequence of the F4/80 protein. The primary amino acid sequence demonstrates homology to two protein superfamilies. The NH2-terminal region consists of seven epidermal growth factor-like domains, separated by approximately 300 amino acids from a COOH-terminal region that shows homology to members of the seven transmembrane-spanning family of hormone receptors. The potential role of these distinct domains is discussed with respect to the possible function of the F4/80 molecule.
F4/80是一种单克隆抗体,可识别一种小鼠巨噬细胞限制性细胞表面糖蛋白,并且已在广泛的免疫学研究中被广泛用于表征巨噬细胞群体。除了F4/80抗原严格调控的表达模式外,人们对其在巨噬细胞分化和功能中可能发挥的作用知之甚少。我们试图通过分离cDNA克隆在分子水平上对该分子进行表征,现在描述F4/80蛋白的序列。一级氨基酸序列显示出与两个蛋白质超家族的同源性。NH2末端区域由七个表皮生长因子样结构域组成,与COOH末端区域相隔约300个氨基酸,该COOH末端区域与七跨膜激素受体家族的成员具有同源性。针对F4/80分子的可能功能讨论了这些不同结构域的潜在作用。