MOLECULAR-CLONING OF F4 80, A MURINE MACROPHAGE-RESTRICTED CELL-SURFACE GLYCOPROTEIN WITH HOMOLOGY TO THE G-PROTEIN LINKED TRANSMEMBRANE-7 HORMONE-RECEPTOR FAMILY/
Aj. Mcknight et al., MOLECULAR-CLONING OF F4 80, A MURINE MACROPHAGE-RESTRICTED CELL-SURFACE GLYCOPROTEIN WITH HOMOLOGY TO THE G-PROTEIN LINKED TRANSMEMBRANE-7 HORMONE-RECEPTOR FAMILY/, The Journal of biological chemistry, 271(1), 1996, pp. 486-489
F4/80 is a monoclonal antibody that recognizes a murine macrophage-res
tricted cell surface glycoprotein and has been extensively used to cha
racterize macrophage populations in a wide range of immunological stud
ies. Apart from the tightly regulated pattern of expression of the F4/
80 antigen, little is known about its possible role in macrophage diff
erentiation 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 seq
uence demonstrates homology to two protein superfamilies. The NH2-term
inal region consists of seven epidermal growth factor-like domains, se
parated by approximately 300 amino acids from a COOH-terminal region t
hat shows homology to members of the seven transmembrane-spanning fami
ly of hormone receptors, The potential role of these distinct domains
is discussed with respect to the possible function of the F4/80 molecu
le.