Molecular cloning of F4/80, a murine macrophage-restricted cell surface glycoprotein with homology to the G-protein-linked transmembrane 7 hormone receptor family

Andrew J. McKnight*, Alison J. Macfarlane, Pietro Dri, Laurence Turley, Anthony C. Willis, Siamon Gordon

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

200 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)486-489
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number1
DOIs
StatePublished - 05 01 1996
Externally publishedYes

Fingerprint

Dive into the research topics of 'Molecular cloning of F4/80, a murine macrophage-restricted cell surface glycoprotein with homology to the G-protein-linked transmembrane 7 hormone receptor family'. Together they form a unique fingerprint.

Cite this