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表面吸附的α1-微球蛋白对人成纤维细胞铺展和基质金属蛋白酶释放的调节作用

Surface-adsorbed alpha1-microglobulin modulation of human fibroblasts spreading and matrix metalloproteinases release.

作者信息

Renò F, Lombardi F, Cannas M

机构信息

Human Anatomy Laboratory, Medical Sciences Department, University of Eastern Piedmont, A. Avogadro, Via Solaroli 17, 28100 Novara, Italy.

出版信息

Biomaterials. 2004 Aug;25(17):3439-43. doi: 10.1016/j.biomaterials.2003.10.047.

DOI:10.1016/j.biomaterials.2003.10.047
PMID:15020117
Abstract

The lipocalin alpha1-microglobulin (alpha1-m), an immunoregulatory protein produced by human hepatocytes and distributed in various organs and fluids, is physiologically adsorbed onto polymer surfaces from both serum and urine, and its adsorption correlated to the degree of surface hydrophobicity. Starting from the hypothesis that alpha1-m holds a modulatory role at the biomaterials-tissue interface, we have observed a dose-dependent reduction in adhesion of human fibroblasts (cell line MRC-5) seeded onto polystyrene (PS) in a serum-free medium in the presence of adsorbed alpha(1)-m (2.1+/-0.2 x 10(4) cells/cm2 at 200 ng/ml alpha1-m ) compared to cells seeded onto cell grade PS (2.9+/-0.05 x 10(4) cells/cm2) after 72 h. Moreover, in the presence of alpha1-m, adherent MRC-5 cells exhibit an altered shape due to inhibition of cell spreading, and release of matrix metalloproteinase -2 (gelatinase A, MMP-2) by fibroblasts was also increased by 1.6-1.9-fold after 72 h of incubation. These data extend the known spectrum of alpha1-m activities, suggesting a possible role of this protein in the complex series of events occurring at the tissue-biomaterial interface.

摘要

脂钙蛋白α1-微球蛋白(α1-m)是一种由人类肝细胞产生并分布于各种器官和体液中的免疫调节蛋白,在生理状态下可从血清和尿液中吸附到聚合物表面,其吸附作用与表面疏水性程度相关。基于α1-m在生物材料-组织界面发挥调节作用这一假设,我们观察到,在无血清培养基中,当聚苯乙烯(PS)表面吸附有α1-m时,接种于其上的人成纤维细胞(MRC-5细胞系)的黏附能力呈剂量依赖性降低(在α1-m浓度为200 ng/ml时,细胞黏附数量为2.1±0.2×10⁴个细胞/cm²),而接种于细胞级PS上的细胞在72小时后的黏附数量为(2.9±0.05×10⁴个细胞/cm²)。此外,在有α1-m存在的情况下,贴壁的MRC-5细胞由于细胞铺展受到抑制而呈现出改变的形态,并且在培养72小时后,成纤维细胞释放基质金属蛋白酶-2(明胶酶A,MMP-2)的量也增加了1.6至1.9倍。这些数据扩展了已知的α1-m活性谱,表明该蛋白在组织-生物材料界面发生的一系列复杂事件中可能发挥作用。

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