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Volume 272, Number 50, Issue of December 12, 1997
pp. 31764-31769
(Received for publication, June 12, 1997, and in revised form, October 2, 1997)
From the The IL-1 type II receptor (decoy RII) is a
nonsignaling molecule the only established function of which is to
capture IL-1 and prevent it from interacting with signaling receptor.
The decoy RII is released in a regulated way from the cell surface.
Here, we reported that hydroxamic acid inhibitors of matrix
metalloproteases inhibit different pathways of decoy RII release,
including the following: (a) the slow (18 h) gene
expression-dependent release from monocytes and
polymorphonuclear cells exposed to dexamethasone; (b) rapid
release (minutes) from myelomonocytic cells exposed to tumor necrosis
factor, chemoattractants, or phorbol myristate acetate; (c)
phorbol myristate acetate-induced release from decoy RII-transfected
fibroblasts and B cells. Inhibition of release was associated with
increased surface expression of decoy RII. Inhibitors of other protease
classes did not substantially affect release. However, serine protease
inhibitors increased the molecular mass of the decoy RII released from
polymorphonuclear cells from 45 to 60 kDa. Thus, irrespective of the
pathway responsible for release and of the cellular context, matrix
metalloproteases, rather than differential splicing, play a key role in
production of soluble decoy RII.
Role of Metalloproteases in the Release of the IL-1 type II
Decoy Receptor
,
,
,
,
Department of Immunology and Cell Biology,
Istituto di Ricerche Farmacologiche "Mario Negri," Via Eritrea 62, 20157 Milano, Italy; ¶ British Biotech, Cowley, Oxford OX4 5LY,
United Kingdom; 
Research Center Dompé Spa, I-67100
L'Aquila, Italy; ** Department of Immunology, Pharmacia & Upjohn
Research Center, 20014 Nerviano, Italy; and
Department of Biotechnology, Section of
General Pathology, University of Brescia, 25100 Brescia, Italy
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