Abstract：
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.
摘要：
由于胶原蛋白在食品中的广泛应用，多年来对胶原蛋白的需求一直在增加，化妆品和生物医药行业。鱼类胶原蛋白的合成取决于胶原蛋白提供的说明，I型,α1(COL1A1)基因。然而,克隆,目前尚不清楚产生凝胶的楚氏大鱼（Nibeacoibor）中COL1A1基因的组织分布和mRNA表达。本研究从6种N.coibor鱼中克隆了COL1A1基因的cDNA（GenBank登录号：MK641512）。分析了COL1A1在8个组织中的分布和mRNA表达模式。COL1A1cDNA的全长为6130bp，并包含一个4344bp的开放阅读框（ORF），编码1448个氨基酸的多肽。N.coiborCOL1A1氨基酸的同源性与大黄鱼有98%的相似性，表明与同一家庭中的其他成员（Sciaenidae）的保守主义。推导的多肽含有相同的信号肽，C-前肽和N-前肽结构域，和三螺旋结构域，这是脊椎动物中I型胶原蛋白的特征。COL1A1基因的mRNA在N.coibor脊柱中的表达明显高于所有其他组织（P<0.05），其次是游泳膀胱，皮肤和鳞片。膀胱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>和>皮肤(P<0.05)。我们的研究首次成功克隆了N.coibor的COL1A1基因。COL1A1基因包含胶原蛋白pro-α1（I）链蛋白的所有特征，并与其他海洋硬骨鱼具有很高的同源性。COL1A1基因在脊柱和游泳膀胱中高表达，与胶原蛋白分布一致。我们的研究有助于更好地了解各种工业用途的N.coibor组织中胶原蛋白的生物合成。
