Differences in submicroscopic structure of the extracellular matrix of canine femoral and tibial condylar articular cartilages as revealed by polarization microscopical analysis.
The submicroscopic orientation patterns of sulfated glycosaminoglycan side chains of proteoglycan molecules and collagen fibrils were compared in different extracellular matrix areas of femoral and tibial articular cartilages of young adult beagle dogs using qualitative and quantitative polarization microscopic analytical methods. Paraffin sections were cut perpendicularly to the articular surfaces from the femoral and tibial condyles and stained. Picrosirius red F38 staining combined with an antecedent digestion with testicular hyaluronidase was used to enhance the optical anisotropy of collagen. Birefringence of sulfated glycosaminoglycan molecules was selectively amplified by a combination of carboxymethylation with CH3I and a subsequent staining with toluidine blue. The specimens were analysed in a polarization microscope equipped with compensator plates, and retardation values of birefringence were determined in territorial and interterritorial matrix areas of different zones using monochromatic plane polarized light. It was found that besides some similarities there were significant differences in the submicroscopic organization of extracellular matrix between femoral and tibial articular cartilages. Common structural features of the femoral and tibial cartilages were the sulfated glycosaminoglycans and collagen fibrils which were circularly oriented in the territorial matrix, and these components were longitudinally arranged within the trabeculae of the interterritorial matrix. Furthermore, the territorial matrix was a more densely packed structure than the interterritorial matrix. Our results revealed the following major differences between the two cartilages: The degree of orientation of sulfated glycosaminoglycans was higher in the femoral cartilage matrix areas as compared to the identical structures of the tibial cartilage; the collagen structure was more densely packed in the interterritorial matrix of the superficial and mineralization zones of the femoral cartilage than in the tibial cartilage, and except for the zone of mineralization, the degree of collagen orientation was higher in the territorial matrix of the femoral than the tibial cartilage. These findings suggest that the extracellular matrix of femoral condylar cartilage has a more densely packed molecular structure than the softer tibial cartilage matrix. This structural difference may have an influence on the pathogenesis of diseases involving articular cartilage.
Módis
L
L
Department of Anatomy, Histology and Embryology, University Medical School, Debrecen, Hungary.
Botos
A
A
Kiviranta
I
I
Lukácskó
L
L
Helminen
H J
HJ
D000818:Animals; D001718:Birefringence; D002358:Cartilage, Articular / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D003094:Collagen / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D004285:Dogs; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D005260:Female; D005269:Femur; D006025:Glycosaminoglycans / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008859:Microscopy, Polarization; D015394:Molecular Structure; D013977:Tibia; D014018:Tissue Distribution
D006025:Glycosaminoglycans; C013786:A73025; D003094:Collagen