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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Biophysical evidence for differential gallated green tea catechins binding to membrane type-1 matrix metalloproteinase and its interactors
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Biophysical evidence for differential gallated green tea catechins binding to membrane type-1 matrix metalloproteinase and its interactors

机译：差异化的绿茶儿茶素与膜型-1基质金属蛋白酶及其交流剂结合的生物物理证据

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摘要

Membrane type-1 matrix metalloproteinase (MT1-MMP) is a transmembrane MMP which triggers intracellular signaling and regulates extracellular matrix proteolysis, two functions that are critical for tumor-associated angiogenesis and inflammation. While green tea catechins, particularly epigallocatechin gallate (EGCG), are considered very effective in preventing MT1-MMP-mediated functions, lack of structure-function studies and evidence regarding their direct interaction with MT1-MMP-mediated biological activities remain. Here, we assessed the impact in both cellular and biophysical assays of four ungallated catechins along with their gallated counterparts on MT1-MMP-mediated functions and molecular binding partners. Concanavalin-A (ConA) was used to trigger MT1-MMP-mediated proMMP-2 activation, expression of MT1-MMP and of endoplasmic reticulum stress biomarker GRP78 in U87 glioblastoma cells. We found that ConA-mediated MT1-MMP induction was inhibited by EGCG and catechin gallate (CG), that GRP78 induction was inhibited by EGCG, CG, and gallocatechin gallate (GCG), whereas proMMP-2 activation was inhibited by EGCG and GCG. Surface plasmon resonance was used to assess direct interaction between catechins and MT1-MMP interactors. We found that gallated catechins interacted better than their ungallated analogs with MT1-MMP as well as with MT1-MMP binding partners MMP-2, TIMP-2, MTCBP-1 and LRP1-clusterIV. Overall, current structure-function evidence supports a role for the galloyl moiety in both direct and indirect interactions of green tea catechins with MT1-MMP-mediated oncogenic processes.
机译：膜型 - 1基质金属蛋白酶（MT1-MMP）是一种跨膜MMP，其触发细胞内信号传导并调节细胞外基质蛋白水解，这两个功能对于肿瘤相关的血管生成和炎症至关重要。虽然绿茶儿茶素，特别是EpigallocateChin gallate（EGCG），被认为是非常有效的，但在预防MT1-MMP介导的功能中，缺乏结构函数研究和关于它们与MT1-MMP介导的生物活性的直接相互作用的证据仍然存在。在这里，我们评估了四个未凝聚的儿茶素的细胞和生物物理测定的影响以及它们在MT1-MMP介导的功能和分子结合伴侣上的粘附对应物。康丹林-A（CONA）用于触发MT1-MMP介导的PROMMP-2活化，MT1-MMP和内质网胁迫生物标志物GRP78的表达，在U87胶质母细胞瘤细胞中。我们发现Cona介导的MT1-MMP诱导被EGCG和儿茶素诱导（CG）抑制，即EGCG，CG和GallocateChin Gallate（GCG）抑制GRP78诱导，而Prommp-2激活是通过EGCG和GCG抑制的。表面等离子体共振用于评估儿茶素和MT1-MMP交流器之间的直接相互作用。我们发现，与MT1-MMP的未凝聚的类似物以及MT1-MMP结合合作伙伴MMP-2，TIMP-2，MTCBP-1和LRP1-CLOAKIV，我们发现粘附的儿茶素比其未凝聚的类似物相互作用。总体而言，目前的结构函数证据支持Galloyl部分在绿茶儿茶素与MT1-MMP介导的致癌过程中的直接和间接相互作用中的作用。

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