Macromolecular organization of chicken type X collagen in vitro.
The macromolecular structure of type X collagen in the matrices of primary cultures of chick hypertrophic chondrocytes was initially investigated using immunoelectron microscopy. Type X collagen was observed to assemble into a matlike structure with-in the matrix elaborated by hypertrophic chondrocytes. The process of self assembly was investigated at the molecular level using purified chick type X collagen and rotary-shadowing EM. It was shown that under neutral conditions at 34 degrees C, individual type X collagen molecules associate rapidly into multimeric clusters via their carboxy-terminal globular domains forming structures with a central nodule of carboxy-terminal domains and the triple helices radiating outwards. Prolonged incubation resulted in the formation of a regular hexagonal lattice by lateral association of the juxtaposed triple-helical domains from adjacent multimeric clusters. This extended lattice may play an important role in modifying the cartilage matrix for subsequent events occurring in endochondral bone formation.
Kwan
A P
AP
Department of Biochemistry and Molecular Biology, University of Manchester, United Kingdom.
Cummings
C E
CE
Chapman
J A
JA
Grant
M E
ME
D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D005109:Extracellular Matrix / Q000378:metabolism / Q000648:ultrastructure; D046911:Macromolecular Substances; D016253:Microscopy, Immunoelectron
D046911:Macromolecular Substances; D003094:Collagen