Structural and Functional Plasticity of Collagen Fibrils
| Autor: | Jing-fei Dong, Ying Li, Yuan Zhou, Qi Guo, Yuyang Miao, Jianning Zhang, Fanjian Li, Rongcai Jiang, Xiao Liu, Zengguang Wang, Zilong Zhao, Yanjun Zhang |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Adult Male Protein Expression/Modification/Regulation Biology Collagen Type I Collagen fibril 03 medical and health sciences Protein Aggregates Structure-Activity Relationship 0302 clinical medicine Platelet Adhesiveness Genetics Humans Platelet Molecular Biology Cell Biology General Medicine Hydrogen-Ion Concentration Middle Aged Subendothelial matrix 030104 developmental biology Solubility 030220 oncology & carcinogenesis Structural plasticity Biophysics Female |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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