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J. Biol. Chem., Vol. 265, Issue 29, 17416-17419, 10, 1990
JG Giri, RC Newton and R Horuk
This study describes the identification and characterization of a soluble
interleukin-1 (IL-1) binding protein in the conditioned media from Raji
human B-lymphoma cells. The soluble IL-1 binding material was isolated by
IL-1 affinity chromatography, and treatment with trypsin decreased its
ability to bind to IL-1 demonstrating its protein nature. The soluble IL-1
binding protein was specific for IL-1 and was able to discriminate between
Il-1 alpha and IL-1 beta in a manner analogous to the membrane-bound Raji
IL-1 receptor. The specificity of the IL-1 binding protein was further
established in two ways. 1) Cell-free supernatants from Raji
"receptor-negative" cells did not contain any IL- 1 binding protein, thus
ruling out nonspecific interactions between IL- 1 and a serum or other
protein present in the conditioned medium; and 2) the soluble binding
protein inhibited IL-1 binding to Raji cells in a dose-dependent manner.
Scatchard analysis of IL-1 beta binding showed the dissociation constant
(KD) to be 5.1 nM for the soluble IL-1 binding protein compared with 0.8 nM
for the membrane-bound IL-1 receptor. Gel chromatography of the soluble
binding protein yielded a major peak of IL-1 binding activity with a
molecular mass of 35-45 kDa. The characteristics of the soluble IL-1
binding protein described above are consistent with those of the
extracellular binding domain of the membrane-bound Raji IL-1 receptor.
Identification of soluble interleukin-1 binding protein in cell-free supernatants. Evidence for soluble interleukin-1 receptor
Medical Products Division, E. I. Du Pont De Nemours & Co., Glenolden Laboratory, Pennsylvania 19036.
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