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Department of Biochemistry (Ke.K., C.M., M.I., T.T., T.S.), School of Dentistry, Showa University, Tokyo 142, Japan; Fuji Gotemba Research Laboratories (T.T.), Chugai Pharmaceutical Company, Ltd., Shizuoka 412, Japan; Department of Biochemistry (A.I.), School of Pharmacy, Tokyo University of Pharmacy and Life Science, Tokyo, 192–03, Japan; Department of Biochemistry and Molecular Biology (H.N.), University of Kansas Medical Center, Kansas City, Kansas 66160; and Department of Periodontology (M.I., Ky.K.), School of Dentistry at Tokyo, Nippon Dental University, Tokyo, 102, Japan
Address all correspondence and requests for reprints to: Tatsuo Suda, Department of Biochemistry, School of Dentistry, Showa University, 1–5-8 Hatanodai, Shinagawa-ku, Tokyo 142, Japan.
Interleukin-1 (IL-1) greatly induces osteoclast formation and
stimulates bone resorption of mouse calvaria in culture. In the
presence of soluble IL-6 receptor (sIL-6R), IL-6 similarly induces
osteoclast formation, but the potency of IL-6 in inducing bone
resorption in organ culture is weaker than that of IL-1. To study the
differences in bone-resorbing activity between IL-1 and IL-6, we
examined the effects of the two cytokines on the induction of matrix
metalloproteinases (MMPs). In mouse calvarial cultures, IL-1 markedly
enhanced the messenger RNA (mRNA) expression of MMP-13 (collagenase 3),
MMP-2 (gelatinase A), MMP-9 (gelatinase B), and MMP-3 (stromelysin 1),
which associated with increases in bone matrix degradation. A
hydroxamate inhibitor of MMPs significantly suppressed bone-resorbing
activity induced by IL-1. Gelatin zymography showed that both pro- and
active-forms of MMP-2 and MMP-9 were detected in the conditioned medium
collected from calvarial cultures, and IL-1 markedly stimulated both
pro- and active-forms of the two gelatinases. IL-6 with sIL-6R also
stimulated mRNA expression and biological activities of these MMPs, but
the potency was much weaker than that of IL-1. Conditioned medium
collected from IL-1-treated calvariae degraded native type I collagen,
but 3/4- and 1/4-length collagen fragments were not
detected, suggesting that both collagenases and gelatinases
synergistically degraded type I collagen into smaller fragments. In
mouse osteoblastic cells, the expression of MMP-2, MMP-3, and MMP-13
mRNAs could be detected, and they were markedly enhanced by IL-1
on
days 2 and 5. IL-6 with sIL-6R also induced expression of MMP-13 and
MMP-2 mRNAs on day 2, but the expression was rather transient. These
results demonstrate that the potency of induction of MMPs by IL-1 and
IL-6 is closely linked to the respective bone-resorbing activity,
suggesting that MMP-dependent degradation of bone matrix plays a key
role in bone resorption induced by these cytokines.
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