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首页> 外文期刊>Matrix biology: Journal of the International Society for Matrix Biology >Carbamylation differentially alters type I collagen sensitivity to various collagenases.
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Carbamylation differentially alters type I collagen sensitivity to various collagenases.

机译：氨甲酰化差异地改变了I型胶原对各种胶原酶的敏感性。

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摘要

Carbamylation is a post-translational modification due to nonenzymatic binding of cyanate, a by-product of urea, on free amino groups of proteins. Post-translational modifications are known to induce alterations in structural and functional properties of proteins, thus disturbing protein-protein or cell-protein interactions. We report the impact of carbamylation on type I collagen sensitivity to enzymatic proteolysis. Type I collagen was extracted from rat tail tendons and carbamylated by incubation with 0.1 M potassium cyanate at 37 degrees C for 2, 6 or 24 h. Degradation assays revealed that carbamylated collagen exhibited a greater resistance to collagenases (i.e. bacterial collagenase, matrix metalloproteinase(MMP)-1, MMP-8 and MMP-13), together with an increased sensitivity to MMP-2. Evaluation of collagen triple helix conformation by polarimetry indicated that local destabilizations of triple helix structure related to carbamylation could be responsible for the observed differences in sensitivity. These results confirm the crucial role of triple helix integrity in the degradation of type I collagen by MMPs, and support the deleterious impact of post-translational modifications in vivo by altering the balanced remodeling of collagen within connective tissue.
机译：氨基甲酸酯化是翻译后的修饰，这是由于尿素的副产物氰酸酯在蛋白质的游离氨基上的非酶结合。已知翻译后修饰可诱导蛋白质结构和功能特性的改变，从而干扰蛋白质-蛋白质或细胞-蛋白质的相互作用。我们报告了氨基甲酸酯化对I型胶原酶解蛋白敏感性的影响。从大鼠尾部肌腱中提取I型胶原，并通过与0.1 M氰酸钾在37°C下孵育2、6或24 h进行氨甲酰化。降解试验表明，氨基甲酸酯化的胶原对胶原酶（即细菌胶原酶，基质金属蛋白酶（MMP）-1，MMP-8和MMP-13）表现出更大的抵抗力，并且对MMP-2的敏感性增加。极化法评估胶原三螺旋构象表明，与氨基甲酰化有关的三螺旋结构的局部失稳可能是造成敏感性差异的原因。这些结果证实了三螺旋完整性在MMP降解I型胶原中的关键作用，并通过改变结缔组织中胶原的平衡重塑来支持体内翻译后修饰的有害影响。

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