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The heparin binding PECAM-1 adhesion molecule is expressed by CD34+
hematopoietic precursor cells with early myeloid and B-lymphoid cell
phenotypes
SM Watt, J Williamson, H Genevier, J Fawcett, DL Simmons, A Hatzfeld, SA Nesbitt and DR Coombe
Medical Oncology Laboratory, Imperial Cancer Research Fund, London, UK.
The platelet-endothelial cell adhesion molecule-1 (PE-CAM-1), defined by
the CD31 monoclonal antibody (MoAb), was initially described as a cell-cell
adhesion molecule mediating both homotypic and heterotypic adhesion. In
this report, we show that enriched CD34+ human hematopoietic progenitor
cell populations, containing early myeloid, erythroid, and multipotential
progenitor cells, are CD31+. Analyses of CD34+ cell lines representing
early myeloid, multipotential, and pre- pre-B-lymphoid progenitors indicate
that precursors of both myeloid and B-lymphoid cells express PECAM-1 at
high levels. Three-color flow- cytometric analyses also show that normal
human bone marrow CD31+ CD34+ subsets coexpress myeloid (CD33) or
B-lymphoid (CD19, CD10) markers. Except for the monocytic cell line, U937,
all CD34- cell lines tested, which represent more mature stages of the
myeloid, erythroid, and lymphoid lineages, expressed substantially lower or
negligible levels of PECAM-1. Western blotting studies indicated that the
CD31 MoAb, JC/70A, detected molecules in the 120- to 140-kD molecular
weight range on the monocytic CD34- CD33+ CD31+ cell line, U937; on the
CD34+ CD31+ CD33+ CD19- multipotential/lymphomyeloid precursor cell lines,
KG1 and KG1B; on the CD34+ CD31+ CD19+ CD10+ CD33- precursor pre-pre-B-cell
line, MIK-ALL; and on a CD34(+)-enriched precursor cell population from
normal human bone marrow. A single molecular weight species was generally
observed with enriched membrane preparations, whereas two PECAM-1 molecules
were present in whole-cell lysates of cell lines and the CD34+ bone marrow
cell subset. Preliminary studies show that a proportion of the PECAM-1
molecules on the lymphomyeloid/multipotential progenitor cell line, KG1,
and on the monocytic cell line, U937, binds to heparin-sepharose. A soluble
form of PECAM-1 also binds heparin- sepharose. The high level of expression
of PECAM-1 on CD34+ cells suggests that this glycoprotein may function as a
heterotypic adhesion molecule, possibly mediating multipotential, myeloid,
and early-B- lymphoid precursor cell interactions with stromal cells and
extracellular matrix molecules via heparan sulfate proteoglycans. It may
also act as a homotypic adhesion molecule by interacting with PECAM- 1 on
bone marrow stromal macrophage-like cells and endothelial cells or on
endothelial cells during stem/progenitor cell migration. Thus, this
molecule has the potential importance of directing both lineage commitment
and trafficking of early hematopoietic progenitor cells.
Volume 82,
Issue 9,
pp. 2649-2663,
11/01/1993
Copyright © 1993 by The American Society of Hematology
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