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Fas Ligand Is Present in Human Erythroid Colony-Forming Cells and
Interacts With Fas Induced by Interferon  to Produce Erythroid Cell
Apoptosis
Chun-Hua Dai,
James O. Price,
Thomas Brunner, and
Sanford B. Krantz
From the Hematology Division, Department of Medicine and Department
of Pathology, Department of Veterans Affairs Medical Center (DVAMC) and
Vanderbilt University School of Medicine, Nashville, TN; and the
Division of Cellular Immunology, La Jolla Institute for Allergy and
Immunology, San Diego, CA.
Interferon  (IFN) inhibits the growth and differentiation of
highly purified human erythroid colony-forming cells (ECFCs) and
induces erythroblast apoptosis. These effects are dose- and time-dependent. Because the cell surface receptor known as Fas (APO-1;
CD95) triggers programmed cell death after activation by its ligand and
because incubation of human ECFCs with IFN produces apoptosis, we
have investigated the expression and function of Fas and Fas ligand
(FasL) in highly purified human ECFCs before and after incubation with
IFN in vitro. Only a small percentage of normal human ECFCs express
Fas and this is present at a low level as detected by Northern blotting
for the Fas mRNA and flow cytometric analysis of Fas protein using a
specific mouse monoclonal antibody. The addition of IFN markedly
increased the percentage of cells expressing Fas on the surface of the
ECFCs as well as the intensity of Fas expression. Fas mRNA was
increased by 6 hours, whereas Fas antigen on the cell surface increased
by 24 hours, with a plateau at 72 hours. This increase correlated with
the inhibitory effect of IFN on ECFC proliferation. CH-11 anti-Fas antibody, which mimics the action of the natural FasL, greatly enhanced
IFN-mediated suppression of cell growth and production of apoptosis,
indicating that Fas is functional. Expression of FasL was also
demonstrated in normal ECFCs by reverse transcriptase-polymerase chain
reaction and flow cytometric analysis with specific monoclonal antibody. FasL was constitutively expressed among erythroid progenitors as they matured from day 5 to day 8 and IFN treatment did not change
this expression. Apoptosis induced by IFN was greatly reduced by the
NOK-2 antihuman FasL antibody and an engineered soluble FasL receptor,
Fas-Fc, suggesting that Fas-FasL interactions among the ECFCs produce
the erythroid inhibitory effects and apoptosis initiated by IFN.
Blood, Vol. 91 No. 4 (February 15), 1998:
pp. 1235-1242
© 1998 by The American Society of Hematology.
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