首页> 外文会议>ASME summer bioengineering conference;SBC2011 >COLLAGEN NETWORK TOPOLOGY IS INFLUENCED BY COLLAGEN CONCENTRATION, BUT NOT BY CO-GELATION WITH FIBRIN
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COLLAGEN NETWORK TOPOLOGY IS INFLUENCED BY COLLAGEN CONCENTRATION, BUT NOT BY CO-GELATION WITH FIBRIN

机译:胶原蛋白网络拓扑结构受胶原蛋白浓度影响,但不与纤维蛋白共凝胶化

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Extracellular matrix (ECM) proteins (e.g. collagen, elastin) play an important role in biological tissues. In addition to conferring mechanical strength to a tissue, the ECM provides a biochemical environment essential for modulation of cellular responses such as growth and migration. Collagens are the dominant protein of the ECM, with collagen type I being most abundant. Our group and others have shown that the mechanical properties of a collagen I matrix change with collagen concentration, and when formed in the presence of a secondary fibril network such as fibrin [1].
机译:细胞外基质(ECM)蛋白(例如胶原蛋白,弹性蛋白)在生物组织中起重要作用。除了赋予组织机械强度外,ECM还提供了调节细胞反应(例如生长和迁移)必不可少的生化环境。胶原蛋白是ECM的主要蛋白质,其中I型胶原蛋白含量最高。我们的小组和其他人已经表明,胶原蛋白I基质的机械性能会随着胶原蛋白浓度的变化而变化,并且在存在诸如纤维蛋白的次要纤维网的情况下会形成[1]。

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