Structural colocalisation of type VI collagen and fibronectin in agarose cultured chondrocytes and isolated chondrons extracted from adult canine tibial cartilage.
Cell-matrix and matrix-matrix interactions are of critical importance in regulating the development, maintenance and repair of articular cartilage. In this study, we examined the structural colocalisation of type VI collagen and fibronectin in isolated chondrons and long-term agarose cultured chondrocytes extracted from normal adult canine articular cartilage. Using double labelling immunohistochemistry in conjunction with dual channel confocal microscopy and digital image processing we demonstrate that type VI collagen and fibronectin are distributed in a similar staining pattern and are colocalised at the surface of cultured chondrocytes and isolated chondrons. The results suggest that type VI collagen and fibronectin may play a role in both cell-matrix adhesion and matrix-matrix cohesion in the pericellular microenvironment surrounding articular cartilage chondrocytes.
Chang
J
J
Department of Anatomy, Faculty of Medicine and Health Sciences, University of Auckland, New Zealand. j.chang@auckland.ac.nz
Nakajima
H
H
Poole
C A
CA
D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry* / Q000648:ultrastructure; D002478:Cells, Cultured; D003094:Collagen / Q000032:analysis*; D004285:Dogs; D005109:Extracellular Matrix / Q000737:chemistry; D005353:Fibronectins / Q000032:analysis*; D007091:Image Processing, Computer-Assisted; D007150:Immunohistochemistry; D018613:Microscopy, Confocal; D013977:Tibia
D005353:Fibronectins; D003094:Collagen