title: [Localization of vigilin and type I, II procollagen mRNAs in chick embryos by in situ hybridization].
abstract: Using a 35S-labeled RNA-RNA in situ hybridization technique, we found that vigilin mRNA was abundant in osteoblasts. It disappeared following the transition of osteoblasts to osteocytes. The amount of vigilin mRNA increased with proliferation and hypertrophy of chondrocytes. Fibroblasts contained moderate vigilin mRNA signals. Weak signals were observed in early chick embryos. Type I procollagen mRNAs were abundant in osteoblasts and fibroblasts of the periosteum, perichondrium, tendon and ligament. Type II procollagen mRNA was restricted to chondrocytes. Interestingly, a significant amount of pro alpha 1 (I) mRNA was observed in late proliferative and hypertrophic chondrocytes, which could not be blocked by an excess amount of unlabeled pro alpha 1 (II) antisense RNA. No signal was found in chondrocytes of human fetal cartilage. Vigilin mRNA had a similar distribution to type II procollagen mRNA in chondrocytes, and in other instances it showed a codistribution with type I procollagen mRNAs.
authors.affiliation: Cancer Institute, Zhejiang Branch of CAMS.
authors.forename: Y
authors.initials: Y
authors.lastname: Gan
mesh_terms: D000818:Animals; D002352:Carrier Proteins; D002642:Chick Embryo; D005347:Fibroblasts / Q000737:chemistry; D017403:In Situ Hybridization; D010006:Osteoblasts / Q000737:chemistry; D010011:Osteocytes / Q000737:chemistry; D011347:Procollagen / Q000145:classification / Q000235:genetics*; D011506:Proteins / Q000235:genetics*; D012333:RNA, Messenger / Q000032:analysis*; D016601:RNA-Binding Proteins
chemical_list: D002352:Carrier Proteins; D011347:Procollagen; D011506:Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; C075197:high density lipoprotein binding protein