Biochemical characterization and purification of HILDA, a human lymphokine
active on eosinophils and bone marrow cells
A Godard, H Gascan, J Naulet, MA Peyrat, Y Jacques, JP Soulillou and JF Moreau
National de la Sante et de la Recherche Medicale (U 211-Unite de Recherche
sur les Effecteurs Lymphocytaires T), Faculte de Medecine, Nantes, France.
We previously described a lymphokine termed HILDA (for human interleukin
DA) produced by T-lymphocyte alloreactive clones after antigenic
stimulation. This factor sustains the growth of a murine IL3- sensitive
cell line (DA2). In addition, HILDA is a potent activator of eosinophils
and displays a burst-promoting activity on human bone marrow. In the
present study, HILDA was purified to homogeneity from T- cell clone
supernatant using successively sequential concentration, concanavalin A
(ConA) affinity chromatography with differential elution (alpha-D
glucopyranoside and alpha-D mannopyranoside), high-performance liquid
chromatography (HPLC) gel filtration and reverse-phase HPLC. The pure
material appeared as a 38-kd glycoprotein on sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing or
nonreducing conditions. Biologic activity could be recovered from SDS- PAGE
gel slices corresponding to the 38-kd band. We conclude from the
specificity of the DA-2 cell line and biochemical characteristics described
that this lymphokine is different from other known factors produced by
human T lymphocytes.
Volume 71,
Issue 6,
pp. 1618-1623,
06/01/1988
Copyright © 1988 by The American Society of Hematology
