Mechanism for the regulation of post-translational modifications of procollagens synthesized by matrix-free cells from chick embryos.

前胶原肽酶 软骨 羟赖氨酸 化学 分泌物 胶原蛋白,I型,α1 角膜 Ⅰ型胶原 肌腱 基质(化学分析) II型胶原 细胞外基质 生物化学 细胞生物学 解剖 分子生物学 生物 内分泌学 氨基酸 赖氨酸 色谱法 神经科学
作者
Winston W.‐Y. Kao,S H,Kou-Lin Lee Chou,Jonathan Ebert
出处
期刊:Journal of Biological Chemistry [Elsevier BV]
卷期号:258 (12): 7779-7787 被引量:23
标识
DOI:10.1016/s0021-9258(18)32247-6
摘要

Three possible mechanisms are considered to account for the variations of post-translational modifications in different collagen types. 1) The cells have different amounts of post-translational modifying enzymes, 2) the rate of prolylhydroxylation of different procollagen types is varied, and 3) the rate of chain association of pro-alpha chains of different collagen types is modulated. In an attempt to examine the three possibilities, we have determined the activities of prolyl hydroxylase and lysyl hydroxylase, and we have examined the kinetics of the secretion of procollagens and the kinetics of pro-gamma chain formation of different procollagen types in matrix-free cells isolated from tissues of 17-day-old chick embryos. Type II collagen synthesized by cartilage cells contains more hydroxylysine than type I collagen synthesized by tendon and cornea cells. It was found, however, that cartilage cells contain significantly less lysyl hydroxylase than tendon and cornea cells. In contrast, we found only a small difference in the amount of prolyl hydroxylase in tendon, cornea, and cartilage cells. The secretion of type I procollagen by tendon and cornea cells can be described by two first order processes. In contrast, the secretion of type II procollagen by cartilage cells, type IV procollagen by lens cells, and type V procollagen by cornea cells can be described by single first order processes. Examination of the formation of pro-gamma components of procollagen types I and II revealed that it occurs via intermediate dimers of two pro-alpha chains. The formation or pro-gamma(I) chains in tendon and cornea cells is about three times faster than the formation of pro-gamma(II) chains in cartilage cells. These results are consistent with the hypothesis that the rate of association of pro-alpha chains regulates the synthesis of procollagens with different degrees of post-translational modifications.

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