Collagen breakdown in soft connective tissue explants is associated with the level of active gelatinase A (MMP-2) but not with collagenase

Recent data suggest that gelatinase A (matrix metalloproteinase-2, MMP-2) plays an important role in the degradation of collagen of soft connective tissues. In an attempt to investigate its participation in more detail we assessed the digestion of collagen in cultured rabbit periosteal explants and...

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Veröffentlicht in:Matrix biology 1999-08, Vol.18 (4), p.373-380
Hauptverfasser: Kerkvliet, Erica H.M, Docherty, Andrew J.P, Beertsen, Wouter, Everts, Vincent
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container_issue 4
container_start_page 373
container_title Matrix biology
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creator Kerkvliet, Erica H.M
Docherty, Andrew J.P
Beertsen, Wouter
Everts, Vincent
description Recent data suggest that gelatinase A (matrix metalloproteinase-2, MMP-2) plays an important role in the degradation of collagen of soft connective tissues. In an attempt to investigate its participation in more detail we assessed the digestion of collagen in cultured rabbit periosteal explants and compared this with the level of active MMP-2 and collagenases. The data demonstrated that both collagen degradation and MMP activity increased with time. Conditioned medium obtained from explants cultured for 72 h showed that the level of active MMP-2 correlated with collagen degradation ( r=0.80, d.f.=23, P
doi_str_mv 10.1016/S0945-053X(99)00032-3
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In an attempt to investigate its participation in more detail we assessed the digestion of collagen in cultured rabbit periosteal explants and compared this with the level of active MMP-2 and collagenases. The data demonstrated that both collagen degradation and MMP activity increased with time. Conditioned medium obtained from explants cultured for 72 h showed that the level of active MMP-2 correlated with collagen degradation ( r=0.80, d.f.=23, P&lt;0.0001). Such a relationship was not found with collagenase activity ( r=−0.08, d.f.=21, NS). The possible involvement of MMP-2 in collagen degradation was investigated further by incubating explants with selective gelatinase inhibitors (CT1166, CT1399 and CT1746). In the presence of these compounds breakdown of collagen was almost completely abolished (≈80%). Finally we assessed whether periosteal fibroblasts had the capacity to degrade collagen type I that conferred resistance to collagenase activity. Breakdown of this collagen did not differ from degradation of normal collagen. 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source MEDLINE; Elsevier ScienceDirect Journals
subjects Animals
Collagen - metabolism
Collagen degradation
Collagenases - metabolism
Connective Tissue - enzymology
Connective Tissue - metabolism
Culture Techniques
Data Interpretation, Statistical
Hydroxyproline - metabolism
Immunohistochemistry
Matrix Metalloproteinase 1 - metabolism
Matrix Metalloproteinase 13
Matrix Metalloproteinase 2 - metabolism
Matrix Metalloproteinase 8 - metabolism
Matrix metalloproteinases
Matrix Metalloproteinases - metabolism
MMP-inhibitors
Periosteal explants
Periosteum - enzymology
Rabbits
Skull - enzymology
title Collagen breakdown in soft connective tissue explants is associated with the level of active gelatinase A (MMP-2) but not with collagenase
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