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(Received for publication, February 27, 1997, and in revised form, May 20, 1997)
From the Departments of Osteoclasts form an acidic compartment at their
attachment site in which bone demineralization and matrix degradation
occur. Although both the cysteine proteinases and neutral collagenases participate in bone resorption, their roles have remained unclear. Here
we show that interstitial collagenase has an essential role in
initiating bone resorption, distinct from that of the cysteine proteinases. Treatment of osteoclasts with cysteine proteinase inhibitors did not affect the number of resorption lacunae ("pits") formed on the surface of dentine slices, but it generated abnormal pits
that were demineralized but filled with undegraded matrix. Treatment
with metalloproteinase inhibitors did not alter the qualitative
features of lacunae, but it greatly reduced the number of pits and
surface area resorbed. Treatment of bone cells with an inhibitory
anti-rat interstitial collagenase antiserum reduced bone resorption
markedly. In the presence of collagenase inhibitors, resorption was
restored by pretreatment of dentine slices with rat interstitial
collagenase or by precoating the dentine slices with
collagenase-derived gelatin peptides or heat-gelatinized collagen.
Immunostaining revealed that interstitial collagenase is produced at
high levels by stromal cells and osteoblasts adjacent to osteoclasts.
These results indicate that interstitial collagenase can function as a
"coupling factor," allowing osteoblasts to initiate bone resorption
by generating collagen fragments that activate osteoclasts.
Volume 272, Number 35,
Issue of August 29, 1997
pp. 22053-22058
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
,
and§**
Medicine, § Cell
Biology and Physiology, ¶ Biology, and the ** George M. O'Brien
Center for Kidney and Urological Diseases, Washington University School
of Medicine, St. Louis, Missouri 63110 and the Department of
Biochemistry, Albany Medical College, Albany, New York 12208
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