α1(XX) collagen, a new member of the collagen subfamily, fibril-associated collagens with interrupted triple helices
α1(XX) collagen, a new member of the collagen subfamily, fibril-associated collagens with interrupted triple helices
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DOI：
10.1074/jbc.m009912200
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发表时间：
2001-06-22
影响因子：
4.8
通讯作者：
Gordon, MK
中科院分区：
文献类型：
--
作者：
Koch, M;Foley, JE;Gordon, MK
鸡的cDNA克隆的FACIT（纤维相关的胶原蛋白与中断三螺旋）亚家族的新成员已被分离和测序。由这些cDNA编码的胶原蛋白链被赋予下一个连续的数字，使其成为α 1（XX）胶原蛋白链。将XX型胶原分配到FACIT家族是基于与XII型和XIV型胶原的序列相似性。XX型胶原mRNA在鸡胚中不丰富。它最常见于角膜上皮。它也可以通过逆转录聚合酶链反应在胚胎皮肤，胸骨软骨和肌腱中检测到，但在发育的选择阶段，在颅盖骨，脊索或神经视网膜中几乎检测不到，这表明它在这些组织中不表达。cDNA预测α 1（XX）胶原多肽小于短型胶原XII和XIV。通过Western印迹分析，针对合成α 1（XX）肽的多克隆抗体与185、170和135 kDa的多肽条带反应。由于其与XII型和XIV型胶原的相似性，预计XX型与胶原原纤维结合，使氨基末端结构域远离原纤维表面。预测NC 3结构域的长度约为胶原XIV的长度的一半。
Chick cDNA clones for a new member of the FACIT (fibril-associated collagens with interrupted triple helices) subfamily have been isolated and sequenced. The collagen chain encoded by these cDNAs was assigned the next consecutive number, making it the alpha1(XX) collagen chain. Assignment of type XX collagen to the FACIT family was based on sequence similarities to types XII and XIV collagen. Type XX collagen mRNA is not abundant in the chick embryo. It is most prevalent in corneal epithelium. It is also detectable by reverse transcription polymerase chain reaction in embryonic skin, sternal cartilage, and tendon, but is barely detectable in calvaria, notochord, or neural retina at select stages of development, suggesting that it is not expressed in these tissues. The cDNA predicts that the alpha1(XX) collagen polypeptide is smaller than the short forms of collagen XII and XIV. A polyclonal antibody against a synthetic alpha1(XX) peptide reacts with polypeptide bands of 185, 170, and 135 kDa by Western blot analysis. From its similarity to types XII and XIV collagen, type XX is expected to bind to collagen fibrils, projecting the amino-terminal domains away from the fibrillar surface. The projecting NC 3 domains are predicted to be about half the length of those of collagen XIV.