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The Journal of Immunology, Vol 144, Issue 11 4231-4234, Copyright © 1990 by American Association of Immunologists

ARTICLES

Purification of MEA, a mast cell growth-enhancing activity, to apparent homogeneity and its partial amino acid sequencing

J Moeller, L Hultner, E Schmitt, M Breuer and P Dormer
Institut fur Experimentelle Hamatologie, Gesellschaft fur Strahlen und Umweltforschung, Munich, FRG.

A novel growth factor for bone marrow derived murine mucosal type mast cells has been isolated from the conditioned medium of the Mlsa- reactive mouse Th cell line MLS-4.2. In proliferation assays this growth factor synergizes, like IL-4, with IL-3 on established mast cell lines and was therefore termed MEA: mast cell growth enhancing activity. MEA was characterized as a glycoprotein with a Mr range between 37,000 and 43,000. Apparent homogeneity was obtained by using a four-step purification scheme including cation exchange chromatography, Procion red affinity chromatography, IEF, and gel filtration. Inasmuch as MEA was N-terminally blocked during automated Edman-degradation, peptide fragments after digestion with trypsin were used for partial amino acid sequence determination. All evaluable MEA peptide fragments showed complete sequence homology to a recently purified and cloned novel T cell growth factor (P40/TCGF III), the mouse homologue of human IL-9.


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L. Hultner, S. Kolsch, M. Stassen, U. Kaspers, J.-P. Kremer, R. Mailhammer, J. Moeller, H. Broszeit, and E. Schmitt
In Activated Mast Cells, IL-1 Up-Regulates the Production of Several Th2-Related Cytokines Including IL-9
J. Immunol., June 1, 2000; 164(11): 5556 - 5563.
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