Collagen synthesis by long-lived mRNA in embryonic chicken lens.
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.
D000367:Age Factors; D000818:Animals; D002454:Cell Differentiation; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism*; D003609:Dactinomycin / Q000494:pharmacology; D004848:Epithelium / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D005786:Gene Expression Regulation / Q000187:drug effects; D007908:Lens, Crystalline / Q000378:metabolism*; D008970:Molecular Weight; D012333:RNA, Messenger / Q000378:metabolism
D012333:RNA, Messenger; D003609:Dactinomycin; D003094:Collagen