Publication: Potential synergies between matrix proteins and soluble factors on resorption and proteinase activities of rabbit bone cells
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Date
2001
Authors
Rousselle, A.V. ; Damiens, C. ; Grimaud, E. ; Fortun, Y. ; Padrines, M. ; Passuti, N. ; Heymann, D.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Human growth hormone (GH) has recently
been found to stimulate osteoclastic resorption, cysteineproteinase
and metalloproteinase activities (MMP-2 and
MMP-9) in vitro via insulin-like growth factor-1 (IGF-1)
produced by stromal cells. The present study
investigated the effects of two extracellular matrix
components (vitronectin and type-1 collagen) on hGHand
hIGF-1-stimulated osteoclastic resorption and
proteinase activities in a rabbit bone cell model. After 4
days of rabbit bone cell culture on dentin slices with
vitronectin coating, hGH and hIGF-1 stimulated bone
resorption and hIGF-1 upmodulated cysteine-proteinase
activities. MMP-2 expression (but not resorption,
cathepsin or MMP-9 activities) was upmodulated by
hGH and hIGF-1 on dentin slices coated with type 1
collagen as compared to those without coating. Then,
vitronectin was synergistic with hIGF-1 in the regulation
of cysteine-proteinase production whereas collagen
showed synergy with hGH and hIGF-1 in the regulation
of MMP-2 production. Anti-avB3 totally abolished the
effects of hGH and hIGF-1 on metalloproteinase release,
but had no influence on cathepsin release. The results
suggest that cysteine-proteinase modulation is not
mediated by avB3 integrin (strongly expressed on
osteoclastic surface) whereas the resorption process and
metalloproteinase modulation are clearly'mediated by
this integrin. Our finding about the collagen coating also
suggests that hGH- and hIGF-1-stimulated MMP-2
activity are mediated, along with avB3 integrin, by
another adhesion molecule.
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