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首页> 外文期刊>Matrix biology: Journal of the International Society for Matrix Biology >Modification and functional inactivation of the tropoelastin carboxy-terminal domain in cross-linked elastin.
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Modification and functional inactivation of the tropoelastin carboxy-terminal domain in cross-linked elastin.

机译：弹性蛋白中原弹性蛋白羧基末端结构域的修饰和功能失活。

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摘要

The carboxy-terminus of tropoelastin is a highly conserved, atypical region of the molecule with sequences that define both cell and matrix interactions. This domain also plays a critical but unknown role in the assembly and crosslinking of tropoelastin during elastic fiber maturation. Using a competitive ELISA with an antibody to an elastase-resistant epitope in the carboxy-terminus of tropoelastin (domain-36), we quantified levels of the domain-36 sequence in elastase-derived peptides from mature, insoluble elastin. We found that the amount of carboxy-terminal epitope in elastin is approximately 0.2% of the expected value, assuming each tropoelastin monomer that is incorporated into the insoluble polymer has an intact carboxy-terminus. The low levels suggest that the majority of domain-36 sequence is either removed at some stage of elastin assembly or that the antigenic epitope is altered by posttranslational modification. Biochemical evidence is presented for a potential lysine-derived cross-link inthis region, which would alter the extractability and antigenicity of the carboxy-terminal epitope. These results show that there is little or no unmodified domain-36 in mature elastin, indicating that the cell and matrix binding activities associated with this region of tropoelastin are lost or modified as elastin matures. A crosslinking function for domain-36 may serve to help register the multiple crosslinking sites in elastin and explains why mutations that alter the domain-36 sequence have detrimental effects on elastic fiber assembly.
机译：原弹性蛋白的羧基末端是分子的高度保守的非典型区域，其序列定义了细胞和基质的相互作用。在弹性纤维成熟期间，该结构域在原弹性蛋白的组装和交联中也起着关键但未知的作用。使用针对原弹性蛋白（结构域36）羧基端的弹性蛋白酶抗性表位抗体的竞争性ELISA，我们定量了来自成熟的，不可溶的弹性蛋白的弹性蛋白酶衍生肽中的结构域36序列水平。我们发现，假定掺入不溶性聚合物中的每个原弹性蛋白单体均具有完整的羧基末端，弹性蛋白中羧基末端表位的数量约为预期值的0.2％。低水平表明大多数域-36序列在弹性蛋白装配的某个阶段被去除，或者抗原表位被翻译后修饰所改变。生物化学证据表明，该区域可能存在赖氨酸衍生的交联，这将改变羧基末端表位的可提取性和抗原性。这些结果表明，在成熟的弹性蛋白中几乎没有或没有未修饰的结构域-36，这表明与弹性蛋白的该区域相关的细胞和基质结合活性随着弹性蛋白的成熟而丢失或被修饰。结构域36的交联功能可能有助于在弹性蛋白中注册多个交联位点，并解释了为什么更改结构域36序列的突变对弹性纤维组装有不利影响。

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