T cell-derived migration-inhibitory factor and colony-stimulating factor
share common structural elements
T Kawaguchi, DW Golde, A Mednis, N Bersch, S Clark and HG Remold
Migration-inhibitory factor (MIF) is a lymphokine that acts to localize
mononuclear phagocytes (monocytes and macrophages) and perhaps to activate
them. Mo cells are a human T cell leukemia virus II-infected T cell line
previously shown to secrete large quantities of MIF upon stimulation with
phytohemagglutinin and phorbol myristate acetate. MIF was purified from Mo
cell-conditioned medium by gel filtration, phenyl- Sepharose affinity
chromatography, isoelectrofocusing, and reverse- phase high-performance
liquid chromatography (RP-HPLC). Overall purification was 6,000-fold. The
purified MIF fraction was found to display potent colony-stimulating factor
(CSF) activity when assayed on human bone marrow cells. The double peak of
MIF activity as shown by C 18-RP-HPLC coincided with the double peak of CSF
activity. A monoclonal antibody selected for its anti-MIF activity absorbed
both the CSF and the MIF activity. These findings indicate that MIF and CSF
are either identical molecules or closely related molecules with common
structural elements.
Volume 67,
Issue 6,
pp. 1619-1623,
06/01/1986
Copyright © 1986 by The American Society of Hematology