College of Marine Sciences, South China Agricultural University, Guangzhou 510642, China; College of Animal Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Guangdong Provincial Key Laboratory of Marine Biotechnology, Institute of Marine Sciences, Shantou University, Shantou 515063, China.
Gene. 2022 May 25;824:146441. doi: 10.1016/j.gene.2022.146441. Epub 2022 Mar 23.
The demand for collagen has been increasing over years due to its wide application in food, cosmetics and biomedicine industries. The synthesis of collagen protein in fish depends on instructions provided by collagen, type I, alpha 1 (COL1A1) gene. However, cloning, tissue distribution and mRNA expression of COL1A1 gene in a gel-producing Chu's croaker (Nibea coibor) is currently unknown. This study cloned the cDNA of COL1A1 gene (GenBank accession number: MK641512) from six N. coibor fish. The distribution and mRNA expression pattern of COL1A1 was analyzed in eight tissues of N. coibor. The COL1A1 cDNA had a full length of 6130 bp and contained a 4344 bp open reading frame (ORF) encoding a polypeptide of 1448 amino acids. The homology of N. coibor COL1A1 amino acid had 98% similarity with Larimichthys crocea, indicating conservatism with other members in same family (Sciaenidae). The deduced polypeptide contained the same signal peptides, C-propeptide and N-propeptide domains, and triple helix domains, which are the characteristics of type I collagen in vertebrates. The mRNA of COL1A1 gene was expressed significantly higher in the spine of N. coibor than in all other tissues (P < 0.05), followed by swim bladder, skin and scales. The swim bladder had higher collagen and hydroxyproline contents than other tissues, followed by spine >, scales > and > skin (P < 0.05). Our study successfully cloned the COL1A1 gene from N. coibor for the first time. The COL1A1 gene contained all the features of collagen pro-α1(I) chain proteins, and shared high homology with other marine teleost. COL1A1 gene in N. coibor is highly expressed in spine and swim bladder, consistent with collagen distribution. Our study contributes to better understanding on collagen biosynthesis in N. coibor tissues for various industrial uses.
由于胶原蛋白在食品、化妆品和生物医学行业中的广泛应用，其需求多年来一直在增长。鱼类胶原蛋白的合成取决于胶原蛋白、I 型、α1（COL1A1）基因提供的指令。然而，凝胶生产的黄颡鱼（Nibea coibor）COL1A1 基因的克隆、组织分布和 mRNA 表达目前尚不清楚。本研究从 6 条黄颡鱼中克隆了 COL1A1 基因的 cDNA（GenBank 登录号：MK641512）。分析了 COL1A1 在黄颡鱼 8 种组织中的分布和 mRNA 表达模式。COL1A1 cDNA 全长 6130bp，包含一个 4344bp 的开放阅读框（ORF），编码 1448 个氨基酸的多肽。N. coibor COL1A1 氨基酸的同源性与 Larimichthys crocea 有 98%的相似性，表明与同科（Sciaenidae）的其他成员具有保守性。推导的多肽含有相同的信号肽、C 端前肽和 N 端前肽结构域以及三螺旋结构域，这是脊椎动物 I 型胶原蛋白的特征。COL1A1 基因在黄颡鱼脊柱中的 mRNA 表达明显高于其他所有组织（P<0.05），其次是鳔、皮肤和鳞片。鳔的胶原蛋白和羟脯氨酸含量高于其他组织，其次是脊柱>、鳞片>、皮肤（P<0.05）。本研究首次成功从黄颡鱼中克隆出 COL1A1 基因。COL1A1 基因包含胶原蛋白 pro-α1（I）链蛋白的所有特征，与其他海洋硬骨鱼具有高度同源性。黄颡鱼 COL1A1 基因在脊柱和鳔中高度表达，与胶原蛋白分布一致。本研究有助于更好地了解黄颡鱼组织中胶原蛋白的生物合成，以用于各种工业用途。
