Site-specific immunostaining for type X collagen in noncalcified articular cartilage of canine stifle knee joint.
Type X collagen is a short-chain collagen that is strongly expressed in hypertrophic chondrocytes. In this study, we used an immunohistochemical technique exploiting a prolonged hyaluronidase unmasking of type X collagen epitopes to show that type X collagen is not restricted to calcified cartilage, but is also present in normal canine noncalcified articular cartilage. A 30 degrees valgus angulation procedure of the right tibia was performed in 15 dogs at the age of 3 months, whereas their nonoperated sister dogs served as controls. Samples were collected 7 and 18 months after the surgery and immunostained for type X collagen. The deposition of type X collagen increased during maturation from age 43 weeks to 91 weeks. In the patella, most of the noncalcified cartilage stained for type X collagen, whereas, in the patellar surface of the femur, it was present mainly in the femoral groove close to cartilage surface. In femoral condyles, the staining localized mostly in the superficial cartilage on the lateral and medial sides, but not in the central weight-bearing area. In tibial condyles, type X collagen was often observed close to the cartilage surface in medial parts of the condyles, although staining could also be seen in the deep zone of the cartilage. Staining for type X collagen appeared strongest at sites where the birefringence of polarized light was lowest, suggesting a colocalization of type X collagen with the collagen fibril arcades in the intermediate zone. No significant difference in type X collagen immunostaining was observed in lesion-free articular cartilage between controls and dogs that underwent a 30 degrees valgus osteotomy. In osteoarthritic lesions, however, there was strong immunostaining for both type X collagen and collagenase-induced collagen cleavage products. The presence of type X collagen in the transitional zone of cartilage in the patella, femoropatellar groove, and in tibial cartilage uncovered by menisci suggests that it may involve a modification of collagen fibril arrangement at the site of collagen fibril arcades, perhaps providing additional support to the collagen network.
Lammi
P E
PE
Department of Clinical Chemistry, Kuopio University Hospital, Kuopio, Finland.
Lammi
M J
MJ
Hyttinen
M M
MM
Panula
H
H
Kiviranta
I
I
Helminen
H J
HJ
D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry* / Q000378:metabolism; D024121:Collagen Type X / Q000032:analysis* / Q000096:biosynthesis; D004285:Dogs; D005260:Female; D007150:Immunohistochemistry; D013194:Staining and Labeling; D013264:Stifle / Q000737:chemistry* / Q000378:metabolism
D024121:Collagen Type X