Cartilage contains mixed fibrils of collagen types II, IX, and XI.
The distribution of collagen XI in fibril fragments from 17-d chick embryo sternal cartilage was determined by immunoelectron microscopy using specific polyclonal antibodies. The protein was distributed throughout the fibril fragments but was antigenically masked due to the tight packing of collagen molecules and could be identified only at sites where the fibril structure was partially disrupted. Collagens II and IX were also distributed uniformly along fibrils but, in contrast to collagen XI, were accessible to the antibodies in intact fibrils. Therefore, cartilage fibrils are heterotypically assembled from collagens II, IX, and XI. This implies that collagen XI is an integral component of the cartilage fibrillar network and homogeneously distributed throughout the tissue. This was confirmed by immunofluorescence.
Mendler
M
M
Laboratorium für Biochemie, Eidgenössische Technische Hochschule, Zürich, Switzerland.
Eich-Bender
S G
SG
Vaughan
L
L
Winterhalter
K H
KH
Bruckner
P
P
D000085:Acetates; D019342:Acetic Acid; D000818:Animals; D002356:Cartilage / Q000032:analysis* / Q000648:ultrastructure; D002642:Chick Embryo; D003094:Collagen / Q000032:analysis* / Q000276:immunology; D000939:Epitopes / Q000032:analysis; D007150:Immunohistochemistry; D008854:Microscopy, Electron; D010434:Pepsin A; D014357:Trypsin
D000085:Acetates; D000939:Epitopes; D003094:Collagen; D014357:Trypsin; D010434:Pepsin A; D019342:Acetic Acid