Type XII and XIV collagens mediate interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability.
Type XII and XIV collagens mediate interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability.
复制标题
DOI：
10.1016/s0021-9258(18)46913-x
复制
发表时间：
1994-11
期刊：
影响因子：
--
通讯作者：
Toshio Nishiyama;A. M. McDonough;R. Bruns;R. Burgeson
中科院分区：
文献类型：
--
作者：
Toshio Nishiyama;A. M. McDonough;R. Bruns;R. Burgeson
XII型和XIV型胶原蛋白是非常大的分子，含有三个延伸的球状结构域，来自每个α链的氨基末端和一个中断的三螺旋结构。这两种胶原蛋白在遗传学和免疫学上都是独一无二的，在许多组织中都有不同的分布。这些胶原蛋白位于带状胶原纤维表面附近。这些分子的功能尚不清楚。我们已经制备了一种天然的XII型和XIV型胶原蛋白的混合物，按照电泳标准是不受污染的蛋白质。此外，我们还纯化了XII或XIV型胶原蛋白(XII-NC-3或XIV-NC-3)的胶原酶抗性球状结构域。在本研究中，我们研究了XII、XIV和XII-NC-3或XIV-NC-3对成纤维细胞与I型胶原纤维相互作用的影响。我们发现XII型和XIV型胶原都能促进成纤维细胞介导的胶原凝胶收缩，即使在没有血清的情况下也是如此。该活性存在于NC-3结构域。这种作用是剂量依赖的，并被变性抑制。加入抗XII抗血清可抑制XII型NC-3型的作用。为了阐明这一现象的机制，我们通过离心力检测了XII-NC-3或XIV-NC-3对胶原凝胶变形性的影响。XII-NC-3或XIV-NC-3在离心后显著促进凝胶压缩。这种作用也被变性所抑制，XII-NC3型的活性也被抗XII抗血清所抑制。结果表明，XII-NC-3或XIV-NC-3对成纤维细胞胶原凝胶收缩的影响不是由于细胞事件的激活，而是由于水合胶原纤维在凝胶中流动性增加所致。这些研究表明，XII和XIV型胶原可能调节组织的生物力学特性。
Type XII and XIV collagens are very large molecules containing three extended globular domains derived from the amino terminus of each alpha chain and an interrupted triple helix. Both collagens are genetically and immunologically unique and have distinct distributions in many tissues. These collagens localize near the surface of banded collagen fibrils. The function of the molecules is unknown. We have prepared a mixture of native type XII and XIV collagens that is free of contaminating proteins by electrophoretic criteria. In addition, we have purified the collagenase-resistant globular domains of type XII or XIV collagens (XII-NC-3 or XIV-NC-3). In this study, we have investigated the effect of intact type XII and XIV and XII-NC-3 or XIV-NC-3 on the interactions between fibroblasts and type I collagen fibrils. We find that both type XII and XIV collagens promote collagen gel contraction mediated by fibroblasts, even in the absence of serum. The activity is present in the NC-3 domains. The effect is dose-dependent and is inhibited by denaturation. The effect of type XII NC-3 is inhibited by the addition of anti-XII antiserum. To elucidate the mechanism underlying this phenomenon, we examined the effect of XII-NC-3 or XIV-NC-3 on deformability of collagen gels by centrifugal force. XII-NC-3 or XIV-NC-3 markedly promotes gel compression after centrifugation. The effect is also inhibited by denaturation, and the activity of type XII-NC3 is inhibited by the addition of anti-XII antiserum. The results indicate that the effect of XII-NC-3 or XIV-NC-3 on collagen gel contraction by fibroblasts is not due to activation of cellular events but rather results from the increase in mobility of hydrated collagen fibrils within the gel. These studies suggest that collagen types XII and XIV may modulate the biomechanical properties of tissues.