title: Zebrafish Collagen Type I: Molecular and Biochemical Characterization of the Major Structural Protein in Bone and Skin.
abstract: 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.
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: C
authors.initials: C
authors.lastname: Gistelinck
authors.affiliation: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Pavia, Italy.
authors.forename: R
authors.initials: R
authors.lastname: Gioia
authors.affiliation: Functional Proteomics Lab., Department of Life Sciences, University of Siena, Siena, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Gagliardi
authors.affiliation: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Pavia, Italy.
authors.forename: F
authors.initials: F
authors.lastname: Tonelli
authors.affiliation: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Pavia, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Marchese
authors.affiliation: Functional Proteomics Lab., Department of Life Sciences, University of Siena, Siena, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Bianchi
authors.affiliation: Functional Proteomics Lab., Department of Life Sciences, University of Siena, Siena, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Landi
authors.affiliation: Functional Proteomics Lab., Department of Life Sciences, University of Siena, Siena, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Bini
authors.affiliation: Biology Department, Ghent University, Ghent, Belgium.
authors.forename: A
authors.initials: A
authors.lastname: Huysseune
authors.affiliation: Biology Department, Ghent University, Ghent, Belgium.
authors.forename: P E
authors.initials: PE
authors.lastname: Witten
authors.affiliation: Department of Medical Protein Research, VIB, Ghent, Belgium.|Department of Biochemistry, Ghent University, Ghent, Belgium.
authors.forename: A
authors.initials: A
authors.lastname: Staes
authors.affiliation: Department of Medical Protein Research, VIB, Ghent, Belgium.|Department of Biochemistry, Ghent University, Ghent, Belgium.
authors.forename: K
authors.initials: K
authors.lastname: Gevaert
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: N
authors.initials: N
authors.lastname: De Rocker
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: B
authors.initials: B
authors.lastname: Menten
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: F
authors.initials: F
authors.lastname: Malfait
authors.affiliation: Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
authors.forename: S
authors.initials: S
authors.lastname: Leikin
authors.affiliation: Department of Biosciences, University of Milano, Milan, Italy.
authors.forename: S
authors.initials: S
authors.lastname: Carra
authors.affiliation: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Pavia, Italy.
authors.forename: R
authors.initials: R
authors.lastname: Tenni
authors.affiliation: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Pavia, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Rossi
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: A
authors.initials: A
authors.lastname: De Paepe
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: P
authors.initials: P
authors.lastname: Coucke
authors.affiliation: Center for Medical Genetics Ghent, Ghent University, Ghent, Belgium.
authors.forename: A
authors.initials: A
authors.lastname: Willaert
authors.affiliation: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, Pavia, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Forlino
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001846:Bone Development / Q000235:genetics*; D003094:Collagen / Q000096:biosynthesis / Q000235:genetics*; D024042:Collagen Type I / Q000096:biosynthesis / Q000235:genetics*; D018507:Gene Expression Regulation, Developmental; D011499:Protein Processing, Post-Translational; D012867:Skin / Q000254:growth & development / Q000378:metabolism; D015027:Zebrafish / Q000235:genetics* / Q000254:growth & development; D029961:Zebrafish Proteins / Q000096:biosynthesis / Q000235:genetics*
chemical_list: C471154:COL1A2 protein, zebrafish; D024042:Collagen Type I; D029961:Zebrafish Proteins; D003094:Collagen