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Targeted T-cell therapy for human leukemia: cytotoxic T lymphocytes
specific for a peptide derived from proteinase 3 preferentially lyse human
myeloid leukemia cells
J Molldrem, S Dermime, K Parker, YZ Jiang, D Mavroudis, N Hensel, P Fukushima and AJ Barrett
Bone Marrow Transplant Unit, National Heart, Lung and Blood Institute,
Bethesda, MD 20892-1652, USA.
Proteinase 3 is present in high concentration in the primary granules of
acute and chronic myeloid leukemia blasts, and may represent a potential
T-cell target antigen. We screened proteinase 3 against the binding motif
of HLA-A2.1. Based on its high predicted binding, a 9-mer peptide, "PR-1,"
was synthesized and tested for binding to HLA-A2.1 using the T2 cell line.
PR-1 at 100 micrograms/mL significantly increased expression of HLA-A2.1,
with median channel of fluorescence increasing from 22 to 294. Binding
half-life was determined to be 1,460 minutes by I125-labeled beta
2-microglobulin incorporation. HLA-A2.1+ peripheral blood mononuclear cells
from a normal donor were used to generate a T-cell line specific for PR-1.
The line demonstrated 85% PR- 1-specific lysis at an E:T ratio of 50:1,
compared with 20% lysis without PR-1, using T2 cells as targets. It also
showed 79% specific lysis to fresh chronic myelogenous leukemia blasts, 54%
to fresh acute myelogenous leukemia blasts, and only background lysis (<
20%) to HLA- A2.1+ normal allogeneic marrow cells. The amount of lysis of
HLA-A2.1+ myeloid cells was proportional to cytoplasmic proteinase 3
expression. Thus, HLA-A2.1-restricted cytotoxic T cells, raised against a
peptide contained in proteinase 3, preferentially lysed fresh human
leukemic cells.
Volume 88,
Issue 7,
pp. 2450-2457,
10/01/1996
Copyright © 1996 by The American Society of Hematology
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