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Department of Immunology and Microbiology, Institute of Medical Biology, University of Southern Denmark, Odense, Denmark
We report the cloning of a novel human type I cell surface Ag
mainly expressed by macrophages. The primary structure was established
by molecular cloning, which yielded a 4579-bp cDNA sequence encoding a
polypeptide chain of 1453 amino acid residues with 16 potential
N-glycosylation sites. We designated this molecule M160.
The domain organization features 12 scavenger receptor cysteine-rich
domains followed by a transmembrane region and a cytoplasmic domain
that occurs in two forms, a predominant form (M160-
) of 71 residues
and an alternatively spliced form (M160-
) of 39 residues. M160-
contains three possible phosphorylation sites, which are lost in the
alternatively spliced form. RT-PCR analyses showed M160 to be expressed
by alveolar macrophages and by the monocyte cell lines HL60, U937, and
THP1, but not by Jurkat or Raji cells. Stimulation of U937 cells with
phorbol ester resulted in an increased expression of M160 from day 5
onward. RT-PCR analysis of 19 different human tissues showed signals
for M160- of varying intensity in all tissues, whereas M160- was
confined to the spleen. We conclude that M160 is a new member of the
scavenger receptor cysteine-rich superfamily expressed by the
monocyte/macrophage cell lineage.
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