The bioactivity of transforming growth factor-β1 can be regulated via binding to dermal collagens in mink lung epithelial cells
The bioactivity of transforming growth factor-β1 can be regulated via binding to dermal collagens in mink lung epithelial cells
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DOI：
10.1016/j.jdermsci.2005.10.005
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发表时间：
2006-03-01
影响因子：
4.6
通讯作者：
Fujiwara, S
中科院分区：
文献类型：
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作者：
Shibuya, H;Okamoto, O;Fujiwara, S
工作背景：转化生长因子β 1的生物活性TGF-β 1（TGF-β 1）受细胞外基质（ECM）某些成分的调节，但胶原蛋白是ECM中含量最丰富的成分，对TGF-β 1的调节作用尚未见报道。目的：探讨不同类型胶原蛋白对TGF-β 1生物活性的影响。I-125-TGF-β 1和各种类型的胶原蛋白的相互作用通过固相测定法和共沉淀测定法进行检查。TGF-β 1的生物活性进行了评估，其中貂肺上皮细胞进行了检查，在存在和不存在的collagens.Results：激活的天然二聚体TGF-β 1结合I型胶原蛋白的剂量依赖性的方式，而单体TGF-β 1结合不良的胶原蛋白的增殖试验。III型胶原和I型明胶（一种热变性的I型胶原）也显示出与TGF-β 1类似的相互作用，然而，IV型胶原显示出弱相互作用。在I型和III型胶原存在下，TGF-β 1对水貂肺上皮细胞增殖的抑制作用持续，从而表明TGF-β 1的生物活性已被增强。I型明胶也增强了对细胞生长的抑制作用，但与I型胶原相比，其作用较弱。在存在I型和III型胶原的情况下与MLEC孵育后，在条件培养基中保持完整的TGF-β 1的量多于在没有胶原的情况下孵育的量。我们的研究结果表明，I型和III型胶原是间质胶原中最丰富的两种成分，可以潜在地与活化的TGF-β 1结合并调节这种生长因子的生物活性，从而可能维持生物学上可利用的TGF-β 1水平。(c)2005年日本皮肤病研究学会。由Elsevier爱尔兰有限公司出版。保留所有权利。
Background: The bioactivity of transforming growth factor-beta 1 (TGF-beta 1) is known to be regulated by some components of the extracellular matrix (ECM), but the possibility that it might be regulated by collagen, the richest ECM component, has never been previously reported.Objective: This study was designed to investigate the possible role that different types of collagens might play on the bioactivity of TGF-beta 1.Methods: The interaction of I-125-TGF-beta 1 and various types of collagen was examined by a solid-phase assay and by a co-precipitation assay. The bioactivity of TGF-beta 1 was assessed by a proliferation assay in which mink lung epithelial cells were examined in the presence and absence of collagens.Results: Activated native dimeric TGF-beta 1 bound to type I collagen in a dose-dependent manner, while monomeric TGF-beta 1 bound poorly to the collagen. Type III collagen, and type I gelatin, a heat-denatured type I collagen, also showed a similar interaction with TGF-beta 1, however, type IV collagen showed a weak interaction. In the presence of types I and III collagens, the inhibitory effect of TGF-beta 1 on the proliferation of mink lung epithelial cells was sustained, thus suggesting that the bioactivity of TGF-beta 1 had been enhanced. Type I gelatin also enhanced the inhibition of cell growth, but its effect was weak in comparison with that of type I collagen. The amount of TGF-beta 1 which remained intact in the conditioned medium after incubation with MLEC in the presence of types I and III collagens was more than that incubated without collagen.Conclusions: Our results suggest that types I and III collagens, the two most abundant components of the interstitial collagens, can potentially bind to activated TGF-beta 1 and regulate the bioactivity of this growth factor, thereby possibly maintaining the biologically available TGF-beta 1 level. (c) 2005 Japanese Society for Investigative Dermatology. Published by Elsevier Ireland Ltd. All rights reserved.