Potential synergies between matrix proteins and soluble factors on resorption and proteinase activities

• Rousselle, A.V. ^[1] ; Damiens, C. ^[1] ; Grimaud, E. ^[1] ; Fortun, Y. ^[1] ; Padrines, M. ^[1] ; Passuti, N. ^[2] ; Heymann, D. ^[3]
  1. [1] Laboratory of Physiopathology of Bone Resorption, Faculty of Medicine, Nantes
  2. [2] Department of Orthopaedic Surgery, Nantes Hospital, Nantes, France
  3. [3] Faculty of Medicine, Nantes

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• Localización: Histology and histopathology: cellular and molecular biology, ISSN-e 1699-5848, ISSN 0213-3911, Vol. 16, Nº. 3, 2001, págs. 727-734
• Idioma: inglés
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  • 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-I (lGF-I) produced by stromal cells. The present study inve tigated the effects of two extracellular matrix components (vitronectin and type-I collagen) on hGHand hIGF-1-stimulated osteoclastic re orption and proteinase activities in a rabbit bone cell model. After 4 day of rabbit bone cell culture on dentin slices with vitronectin coating, hGH and hIGF-1 stimul ated bone resorption and hlGF-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 I collagen as compared to those without coating. Then, vitronectin was synergistic with hIGF-1 in the regulation of cysteine-prote in ase production whereas collagen howed synergy with hGH and hIGF-1 in the regulation of MMP-2 production. Anti-avID tota lly abolished the effect of hGH and hIGF-1 on metalloproteinase relea e, but had no influence on cathepsin release. The results suggest that cysteine-p roteinase modulation is not mediated by avl33 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 activ it y are mediated, along with aviD integrin, by another adhesion molecule.