A novel marker of tissue junctions, collagen XXII
A novel marker of tissue junctions, collagen XXII
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DOI：
10.1074/jbc.m400536200
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发表时间：
2004-05-21
影响因子：
4.8
通讯作者：
Bruckner-Tuderman, L
中科院分区：
文献类型：
--
作者：
Koch, M;Schulze, J;Bruckner-Tuderman, L
在这里，我们描述了一种新的组织连接，胶原蛋白XXII的具体组成部分。它首先通过筛选EST数据库鉴定，随后表达为重组蛋白，并表征为真实的组织组分。人染色体8q24.2上的COL 22 A1基因编码结构上属于FACIT蛋白家族（具有中断的三螺旋的原纤维相关胶原）的胶原。胶原蛋白XXII在组织连接处表现出明显的限制性定位，例如骨骼肌和心肌中的肌腱连接处、关节软骨-滑液连接处或皮肤中生长期毛囊和真皮之间的边界。它沉积在肌腱连接处和毛囊的基底膜区，并与软骨中的纤维外基质结合。肌腱连接处的原位杂交显示，肌肉细胞产生胶原XXII，功能测试表明，胶原XXII作为皮肤上皮细胞和成纤维细胞的细胞粘附配体。这种新的基因产物，胶原蛋白XXII，是第一个特定的细胞外基质蛋白只存在于组织连接。
Here we describe a novel specific component of tissue junctions, collagen XXII. It was first identified by screening an EST data base and subsequently expressed as a recombinant protein and characterized as an authentic tissue component. The COL22A1 gene on human chromosome 8q24.2 encodes a collagen that structurally belongs to the FACIT protein family (fibril-associated collagens with interrupted triple helices). Collagen XXII exhibits a striking restricted localization at tissue junctions such as the myotendinous junction in skeletal and heart muscle, the articular cartilage-synovial fluid junction, or the border between the anagen hair follicle and the dermis in the skin. It is deposited in the basement membrane zone of the myotendinous junction and the hair follicle and associated with the extrafibrillar matrix in cartilage. In situ hybridization of myotendinous junctions revealed that muscle cells produce collagen XXII, and functional tests demonstrated that collagen XXII acts as a cell adhesion ligand for skin epithelial cells and fibroblasts. This novel gene product, collagen XXII, is the first specific extracellular matrix protein present only at tissue junctions.