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Mechanism of Dimerization of a Recombinant Mature Vascular Endothelial Growth Factor C

机译:重组成熟血管内皮生长因子C的二聚化机理

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The vascular endothelial growth factors (VEGFs) and their tyrosine kinase receptors play a pivotal role in angiogenesis and lymphangiogenesis during development and in pathologies such as tumor growth. The VEGFs function as disulfide-linked antiparallel homodimers. The lymphangiogenic factors, VEGF-C and VEGF-D, exist as monomers and dimers, and dimerization is regulated by a unique unpaired cysteine. In this study, we have characterized the redox state of this unpaired cysteine in a recombinant mature monomeric and dimeric VEGF-C by mass spectrometry. Our findings indicate that the unpaired cysteine regulates dimerization via thioldisulfide exchange involving the interdimer disulfide bond.
机译:血管内皮生长因子(VEGF)及其酪氨酸激酶受体在发育过程中以及诸如肿瘤生长的病理过程中,在血管生成和淋巴管生成中起着关键作用。 VEGF充当二硫键连接的反平行同二聚体。淋巴管生成因子VEGF-C和VEGF-D作为单体和二聚体存在,二聚化受独特的未配对半胱氨酸调控。在这项研究中,我们已通过质谱分析表征了这种未配对的半胱氨酸在重组成熟单体和二聚体VEGF-C中的氧化还原状态。我们的发现表明,未配对的半胱氨酸通过涉及二聚体二硫键的巯基二硫键交换调节二聚化。

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