The structure of human collagen type IX and its organization in fetal and infant cartilage fibrils.
Human collagen type IX was isolated from the media of organ cultures of fetal or infant hyaline cartilage. It consisted of three distinct, disulfide-bonded polypeptides of 115, 84, and 72 kDa, respectively. Digestion with chondroitinase ABC reduced the apparent molecular mass of the 115-kDa chain to about 65 kDa demonstrating that also human collagen type IX is a proteoglycan. In the electron microscope, the molecule had a rigid rod-like structure with characteristic kinks and with a globular domain at one end. Digestion of human collagen type IX with pepsin leads to somewhat heterogeneous fragments. Affinity-purified antibodies to the mixture of fragments specifically reacted with the fragment HMW without cross-reaction with chicken HMW. LMW of both species were recognized to the same low extent. Mechanically generated fibril fragments from human fetal cartilage were heterogeneous in diameter. Significantly, they could be immunostained for collagen type IX in a D-periodic pattern and regardless of the fibril diameter. Some fibrils were poorly labeled, again independently of the diameter. Therefore, the role of collagen type IX in cartilage probably is not to control directly the lateral growth during fibrillogenesis but rather to stabilize the fibril network.
D000818:Animals; D002356:Cartilage / Q000032:analysis / Q000196:embryology / Q000648:ultrastructure*; D002645:Chickens; D002808:Chondroitin Lyases / Q000378:metabolism; D003094:Collagen / Q000032:analysis* / Q000648:ultrastructure; D006801:Humans; D008854:Microscopy, Electron; D008970:Molecular Weight; D009924:Organ Culture Techniques; D010434:Pepsin A / Q000378:metabolism
D003094:Collagen; D010434:Pepsin A; D002808:Chondroitin Lyases