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Molecular cloning of CD68, a human macrophage marker related to lysosomal
glycoproteins
CL Holness and DL Simmons
Imperial Cancer Research Fund, John Radcliffe Hospital, Headington, Oxford,
UK.
CD68 is a 110-Kd transmembrane glycoprotein of unknown function highly
expressed by human monocytes and tissue macrophages. We have isolated cDNA
clones encoding CD68 from a U937 cDNA library by transient expression in
COS cells and panning with the anti-CD68 monoclonal antibodies (MoAbs)
Y2/131, Y1/82A, EBM11, and Ki-M6. CD68 transcripts are constitutively
present in the promonocyte cell line U937 and are upregulated by phorbol
myristic acid (PMA). By contrast, CD68 transcripts are absent or present at
very low levels in many hematopoietic lines including KG1, CEM, and K562,
but can be induced by exposure to PMA. The cDNA sequence predicts a type I
integral membrane protein of 354 residues with a heavily glycosylated
extracellular domain of 298 residues containing nine potential N-linked
glycosylation sites and numerous potential O-linked glycosylation sites.
The extracellular domain consists of two distinct regions separated by an
extended proline hinge: a membrane-distal mucin-like domain containing
short peptide repeats and consisting of 54% serine and threonine residues;
and a membrane proximal domain that has significant sequence homology to a
family of lysosomal/plasma membrane shuttling proteins known as the lamp 1
group. CD68 is a member of a growing family of hematopoietic mucin-like
molecules, including leukosialin/CD43, the stem cell antigen CD34, and the
lymph node high endothelial ligand for L-selectin GlyCAM-1.
Volume 81,
Issue 6,
pp. 1607-1613,
03/15/1993
Copyright © 1993 by The American Society of Hematology
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