Zebrafish Collagen Type I: Molecular and Biochemical Characterization of the Major Structural Protein in Bone and Skin

• Published in: Scientific reports 2016-02, Vol.6 (1), p.21540-21540, Article 21540
• Main Authors: Gistelinck, C., Gioia, R., Gagliardi, A., Tonelli, F., Marchese, L., Bianchi, L., Landi, C., Bini, L., Huysseune, A., Witten, P. E., Staes, A., Gevaert, K., De Rocker, N., Menten, B., Malfait, F., Leikin, S., Carra, S., Tenni, R., Rossi, A., De Paepe, A., Coucke, P., Willaert, A., Forlino, A.
• Format: Article
• Language: English
• Subjects: 38/61; 38/77; 631/136/334/1874/763; 631/45/612; 64/116; 82/29; 82/58; 82/80; 82/83; Amino Acid Sequence; Animals; Bone composition; Bone Development - genetics; Collagen; Collagen (type I); Collagen - biosynthesis; Collagen - genetics; Collagen Type I - biosynthesis; Collagen Type I - genetics; Embryogenesis; Gene Expression Regulation, Developmental; Humanities and Social Sciences; Larval development; multidisciplinary; Post-translation; Protein Processing, Post-Translational; Science; Skin; Skin - growth & development; Skin - metabolism; Zebrafish - genetics; Zebrafish - growth & development; Zebrafish Proteins - biosynthesis; Zebrafish Proteins - genetics
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep21540

Over the last years the zebrafish imposed itself as a powerful model to study skeletal diseases, but a limit to its use is the poor characterization of collagen type I, the most abundant protein in bone and skin. In tetrapods collagen type I is a trimer mainly composed of two α1 chains and one α2 chain, encoded by COL1A1 and COL1A2 genes, respectively. In contrast, in zebrafish three type I collagen genes exist , col1a1a , col1a1b and col1a2 coding for α1(I), α3(I) and α2(I) chains. During embryonic and larval development the three collagen type I genes showed a similar spatio-temporal expression pattern, indicating their co-regulation and interdependence at these stages. In both embryonic and adult tissues, the presence of the three α(I) chains was demonstrated, although in embryos α1(I) was present in two distinct glycosylated states, suggesting a developmental-specific collagen composition. Even though in adult bone, skin and scales equal amounts of α1(I), α3(I) and α2(I) chains are present, the presented data suggest a tissue-specific stoichiometry and/or post-translational modification status for collagen type I. In conclusion, this data will be useful to properly interpret results and insights gained from zebrafish models of skeletal diseases.