High post-translational modification levels in type II procollagen are not a consequence of slow triple-helix formation.
The kinetics of triple helix formation of newly synthesized type II procollagen in chick embryo sternal cartilage cells were determined. The data obtained were in agreement with a model for triple helix formation in cellulo proposed recently (Bruckner et al., 1981). The time required to produce fully triple helical type II procollagen in cartilage cells was only 30% longer than for type I procollagen in tendon cells. Therefore, the several-fold increase in post-translational modification observed for type II collagen as compared to type I collagen cannot be attributed solely to slow helix formation but rather is a result of higher levels of enzymic activity of post-translational modification present in cartilage cells.
D000818:Animals; D002356:Cartilage / Q000378:metabolism; D002642:Chick Embryo; D066298:In Vitro Techniques; D007700:Kinetics; D011347:Procollagen / Q000378:metabolism*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013710:Tendons / Q000378:metabolism
D011347:Procollagen