Co-localization of integrins and matrix metalloproteinases in the extracellular matrix of chondrocyte cultures

• Schulze-Tanzil, G. ^[1] ; de Souza, P. ^[1] ; Merker, H.-J. ^[1] ; Shakibaei, M. ^[1]
  1. [1] nstitute of Anatomy. Freie Universitat Berlin. Berlin. Germany
• Localización: Histology and histopathology: cellular and molecular biology, ISSN-e 1699-5848, ISSN 0213-3911, Vol. 16, Nº. 4, 2001, págs. 1081-1089
• Idioma: inglés
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• Resumen

  • ßl-integrins were fo und in the cartilage matrix, s uggesting their implication in the assembly of its arc hitectura l scaffold, but the mechanism for this event is not yet cl ear. Matrix metalloproteinases ( MMPs) may be involved in a n integrin-s he dding mechanis m and matrix 131-integrins may ac t t o alte r MMP ac tivity. To begin to address this questi o n, this study w as d esig ne d to de termine whethe r ß1-integrins and MMPs arc co-localize d in the cho ndrocytes o r in the extr acellular matrix of ca rtilage. We investigated high-density cultures of limb buds of 12 -day-old mo use embryos by do ub le immuno -fluo re cence, immunoelectro n mic roscopy and by coimmunoprccipitatio n assays in order to examine the localizati o n o f ßl-integrins and m a trix me tallo -proteinases (MMP-1, MMP-3 and MMP-9) in cartilage. It was found, that all investigated MMPs and 131-integrins were specifically co-localized in hig h-density ca rtilage cultures. Immunogold and immunofluorescence labelling of both ß1-integrins and MMPs were obse rved not only at the surface of chondrocytes but mainly also in th e perice llula r s p ace and di stribute d be tween collagen fibrils in the extracellula r ma trix ( EC M) as we ll. Res ults of immuno precipita ti o n expe rime nt s s uggest a functio nal associati o n of MMPs a nd 13 L-integ rins in chondrocytes as already described for other cell types. Further inves tigatio ns are nee ded to elucidate the functional associatio n betwee n ß1-integrins and MMPs in chondrocytes.