Laurent M, Romquin N, Counis M F, Muel A S, Courtois Y
Dev Biol. 1987 May;121(1):166-73. doi: 10.1016/0012-1606(87)90149-7.
Lens capsule collagen synthesis by epithelial and fiber cells was examined by immunoprecipitation and collagenase digestion in embryonic and posthatch chicken eye lens. Epithelial cells and lens fibers in the process of terminal differentiation produce alpha 1 and alpha 2 type IV collagen chains. At 6 days of embryonic development in addition to the alpha 1 (IV) and alpha 2 (IV) collagen chains, lens cells produce high molecular weight collagenase-sensitive proteins not immunologically related to type IV collagen. Lens capsule collagen components have been identified in central and outer fibers isolated from 18-day embryos and from 10-day posthatch chicken eyes. At these stages, fibers which have an increasing number of picnotic nuclei still show collagen synthesis due to long-lived mRNA. Analysis of collagen synthesis by lens cells incubated with actinomycin D suggests that stabilization of collagen mRNA occurs in lens fiber cells and to a lesser extent in epithelial cells as early as 6 days of embryonic development.
通过免疫沉淀和胶原酶消化法，对胚胎期和孵化后鸡眼晶状体中上皮细胞和纤维细胞的晶状体囊膜胶原蛋白合成进行了检测。处于终末分化过程中的上皮细胞和晶状体纤维产生α1和α2 IV型胶原链。在胚胎发育6天时，除了α1（IV）和α2（IV）胶原链外，晶状体细胞还产生高分子量的对胶原酶敏感的蛋白，这些蛋白与IV型胶原无免疫相关性。已在从18天胚胎和孵化后10天鸡眼中分离出的中央纤维和外周纤维中鉴定出晶状体囊膜胶原成分。在这些阶段，具有越来越多固缩核的纤维由于存在长寿命mRNA仍显示出胶原蛋白合成。用放线菌素D孵育晶状体细胞后对胶原蛋白合成的分析表明，早在胚胎发育6天时，胶原蛋白mRNA的稳定化就发生在晶状体纤维细胞中，而在上皮细胞中程度较小。
