The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.

The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.
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DOI:
10.3390/ijms23042040
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发表时间:
2022-02-12
影响因子:
5.6
通讯作者:
Koide T
Koide T
中科院分区:
生物学2区
文献类型:
--
作者:
Fujii KK;Taga Y;Takagi YK;Masuda R;Hattori S;Koide T

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前胶原的三螺旋形成发生在内质网(ER)中,其中前胶原的单链α链经历广泛的翻译后修饰。修饰包括脯氨酰4-和3-羟基化、赖氨酰羟基化和随后的糖基化。修饰,特别是脯氨酰4-羟基化,增强了前胶原三螺旋的热稳定性。在ER中形成三螺旋后,前胶原分子被转运到高尔基体并从细胞分泌。在这项研究中,我们研究了胶原三螺旋的热稳定性与环境温度之间的关系。我们分析了在不同温度(18、23、28和33 °C)下培养的斑马鱼胚胎成纤维细胞(ZF 4)中胶原蛋白翻译后修饰的数量以及分泌的I型胶原蛋白的热熔融温度和α链组成。结果表明,在低于28 °C的温度下培养,ZF 4细胞胶原蛋白的热稳定性和其他性质几乎不变。相比之下,在较高温度(33 °C)下,观察到I型胶原蛋白的翻译后修饰数量增加和α链组成变化;因此,胶原蛋白获得较高的热稳定性。结果表明,在变温条件下,胶原蛋白的热稳定性可以根据环境温度进行自主调节。
Triple helix formation of procollagen occurs in the endoplasmic reticulum (ER) where the single-stranded α-chains of procollagen undergo extensive post-translational modifications. The modifications include prolyl 4- and 3-hydroxylations, lysyl hydroxylation, and following glycosylations. The modifications, especially prolyl 4-hydroxylation, enhance the thermal stability of the procollagen triple helix. Procollagen molecules are transported to the Golgi and secreted from the cell, after the triple helix is formed in the ER. In this study, we investigated the relationship between the thermal stability of the collagen triple helix and environmental temperature. We analyzed the number of collagen post-translational modifications and thermal melting temperature and α-chain composition of secreted type I collagen in zebrafish embryonic fibroblasts (ZF4) cultured at various temperatures (18, 23, 28, and 33 °C). The results revealed that thermal stability and other properties of collagen were almost constant when ZF4 cells were cultured below 28 °C. By contrast, at a higher temperature (33 °C), an increase in the number of post-translational modifications and a change in α-chain composition of type I collagen were observed; hence, the collagen acquired higher thermal stability. The results indicate that the thermal stability of collagen could be autonomously tuned according to the environmental temperature in poikilotherms.
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