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Vascular Medicine and Atherosclerosis Unit, Cardiovascular Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115
Biologic activity of IL-1ß requires processing of the inactive
precursor, a function generally ascribed to IL-1ß-converting enzyme
(caspase-1). However, alternative mechanisms of IL-1ß activation have
been postulated in local inflammatory reactions. Expression of IL-1ß
and matrix metalloproteinases (MMPs) frequently occurs simultaneously
at sites of inflammation. We describe here that stromelysin-1 (MMP-3),
as well as the gelatinases A (MMP-2) and B (MMP-9), processes
recombinant human IL-1ß precursor (pIL-1ß) into biologically active
forms. Detection of both pIL-1ß processing and biologic IL-1ß
activity demonstrated different processing capacities of the respective
MMPs. Conversion of pIL-1ß by stromelysin-1 required coincubation for
at least 1 h, and biologic activity faded after 8 h to
24 h. Gelatinase A was less effective in processing pIL-1ß,
requiring at least 24 h of coincubation. In contrast, gelatinase B
processed pIL-1ß within minutes, resulting in immunoreactive products
as well as biologic activity stable for 72 h. In addition,
prolonged incubation of mature IL-1ß with stromelysin-1, and to a
lesser extent also with gelatinases, but not with interstitial
collagenase, resulted in the degradation of mature IL-1ß. None of the
MMPs processed the second isoform of IL-1, IL-1
. The present study
indicates a biphasic regulation of IL-1ß activity by MMPs: a
caspase-1-independent pathway of IL-1ß activation and inhibition of
IL-1ß activity by degrading the mature cytokine. The balance of the
respective MMPs and pIL-1ß might regulate the long term appearance of
IL-1ß activity at sites of acute or chronic
inflammation.
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