II型原胶原蛋白中较高的翻译后修饰水平并非三螺旋形成缓慢的结果。
High post-translational modification levels in type II procollagen are not a consequence of slow triple-helix formation.
作者信息
Keller H, Eikenberry E F, Winterhalter K H, Bruckner P
出版信息
Coll Relat Res. 1985 Jun;5(3):245-51. doi: 10.1016/s0174-173x(85)80014-5.
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.
测定了鸡胚胸骨软骨细胞中新合成的II型前胶原三螺旋形成的动力学。所得数据与最近提出的细胞内三螺旋形成模型（Bruckner等人，1981年）一致。软骨细胞中产生完全三螺旋的II型前胶原所需的时间仅比肌腱细胞中I型前胶原的时间长30%。因此，与I型胶原相比，II型胶原翻译后修饰增加的几倍不能仅仅归因于螺旋形成缓慢，而是软骨细胞中存在的翻译后修饰酶活性水平较高的结果。
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