MOLECULAR-CLONING OF F4 80, A MURINE MACROPHAGE-RESTRICTED CELL-SURFACE GLYCOPROTEIN WITH HOMOLOGY TO THE G-PROTEIN LINKED TRANSMEMBRANE-7 HORMONE-RECEPTOR FAMILY/

Citation
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
Citations number
23
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
271
Issue
1
Year of publication
1996
Pages
486 - 489
Database
ISI
SICI code
0021-9258(1996)271:1<486:MOF8AM>2.0.ZU;2-#
Abstract
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.