Structural and Functional Plasticity of Collagen Fibrils.

Structural and Functional Plasticity of Collagen Fibrils.
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胶原原纤维的结构和功能可塑性。

DOI:
10.1089/dna.2018.4494
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发表时间:
2019-04
影响因子:
3.1
通讯作者:
Zhang Yanjun
Zhang Yanjun
中科院分区:
生物学4区
文献类型:
--
作者:
Zhao Zilong;Li Fanjian;Guo Qi;Zhou Yuan;Miao Yuyang;Li Ying;Wang Zengguang;Jiang Rongcai;Dong Jing Fei;Liu Xiao;Zhang Jianning;Zhang Yanjun

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胶原蛋白是内皮下基质的主要成分,通过激活和聚集血管损伤部位的血小板参与止血。最常见的I型胶原蛋白以可溶性和纤维状两种形式存在,但两种形式之间的结构交换目前尚不清楚。使用原子力显微镜,我们表明,I型胶原蛋白之间的开关可溶性和纤维状的形式在pH值依赖性和离子无关的方式。纤维状胶原蛋白呈绳状,具有特征性的“D带”。“胶原纤维可以用0.1 M乙酸破坏,当pH值调节到7.4时将改革。这种结构可塑性导致截然不同的活性,其中纤维状胶原蛋白在静态和流动条件下对血小板的活性显著更高。更重要的是,通过探测与非接触跳跃探针离子电导显微镜,我们发现,血小板粘附到纤维胶原蛋白主要是作为高密度的气泡形状,经历了快速的微泡。
Collagen is a major component of the subendothelial matrix and participates in bleeding arrest by activating and aggregating platelets at the site of vascular injury. The most common type I collagen exists in both soluble and fibrillar forms, but structural exchangeability between the two forms is currently unknown. Using atomic force microscopy, we show that type I collagen switches between soluble and fibrillar forms in a pH-dependent and ion-independent manner. Fibrillar collagen is rope like with characteristic "D-bands." The collagen fibrils can be disrupted with 0.1 M acetic acid and will reform when the pH is adjusted to 7.4. This structural plasticity leads to drastically different activities, with fibrillar collagen being significantly more active for platelets under static and flow conditions. More important, by probing with noncontact hopping probe ion-conductance microscopy, we find that platelets adherent to fibrillar collagen present primarily as high-density bubble shapes that have undergone rapid microvesiculation.
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