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

Zebrafish Collagen Type I: Molecular and Biochemical Characterization of the Major Structural Protein in Bone and Skin.
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DOI:
10.1038/srep21540
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发表时间:
2016-02-15
期刊:
影响因子:
4.6
通讯作者:
Forlino A
Forlino A
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Gistelinck C;Gioia R;Gagliardi A;Tonelli F;Marchese L;Bianchi L;Landi C;Bini L;Huysseune A;Witten PE;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

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在过去的几年里,斑马鱼将自己打造成研究骨骼疾病的强大模型,但其使用的限制是对 I 型胶原蛋白(骨骼和皮肤中最丰富的蛋白质)的表征较差。在四足动物中,I 型胶原蛋白是主要由两条 α1 链和一条 α2 链组成的三聚体,分别由 COL1A1 和 COL1A2 基因编码。相比之下,斑马鱼存在三种 I 型胶原蛋白基因:col1a1a、col1a1b 和 col1a2,编码 α1(I)、α3(I) 和 α2(I) 链。在胚胎和幼虫发育过程中,三种 I 型胶原蛋白基因表现出相似的时空表达模式,表明它们在这些阶段的共同调节和相互依赖。在胚胎和成人组织中,均证明存在三个 α(I) 链,尽管在胚胎中 α1(I) 以两种不同的糖基化状态存在,表明存在发育特异性的胶原蛋白组成。尽管在成人骨骼、皮肤和鳞片中存在等量的 α1(I)、α3(I) 和 α2(I) 链,但所提供的数据表明 I 型胶原蛋白具有组织特异性化学计量和/或翻译后修饰状态。总之,这些数据将有助于正确解释从斑马鱼骨骼疾病模型中获得的结果和见解。
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.