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首页> 外文期刊>Biochemistry >Biologically Active Sequences in the Mouse Laminin α3 Chain G Domain
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Biologically Active Sequences in the Mouse Laminin α3 Chain G Domain

机译：小鼠层粘连蛋白α3链G结构域中的生物活性序列

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摘要

The laminin α3 chain is mainly expressed at the skin, and its C-terminal G domain has a critical role in multiple biological functions. We screened for biologically active sites on the mouse laminin α3 chain G domain using 107 synthetic peptides on coated plates and conjugated to Sepharose beads with HT1080 human fibrosarcoma cells, HaCaT human skin keratinocyte cells, and human dermal fibroblasts (HDFs). Eleven peptides exhibited cell attachment activity with respect to the peptide-coated plates and/or peptide−Sepharose beads. MA3G28 (WTIQTTVDRGLL) strongly binds to HaCaT cells. Four peptides promoted PC12 cell neurite outgrowth. Heparin inhibited attachment of HDFs to eight peptides on the coated plates. In contrast, EDTA significantly inhibited attachment of HDFs to MA3G27 (NAPFPKLSWTIQ) and MA3G28 but had no effect on the attachment of the other peptides. HDF cells formed well-organized actin stress fibers and focal contacts with vinculin accumulation on MA3G27. Additionally, attachment of HDFs to MA3G27 was inhibited by anti-α6 and anti-β1 integrin antibodies, suggesting that MA3G27 promotes α6β1 integrin-mediated cell adhesion. MA3G57 (NQRLASFSNAQQS) exhibited cell attachment activity only in the peptide bead assay. MA3G57 conjugated to a chitosan membrane promoted HDF attachment and spreading with well-organized actin stress fibers. The anti-β1 integrin antibody partially inhibited attachment of HDFs to the MA3G57−chitosan membrane, suggesting that the MA3G57 site is involved in β1 integrin-mediated cell attachment. These active sites are likely important in the biological activities of the laminin α3 chain G domain and would be useful for the study of molecular mechanisms of laminin−receptor interactions.
机译：层粘连蛋白α3链主要在皮肤上表达，其C端G结构域在多种生物学功能中起关键作用。我们在包被的板上使用107种合成肽筛选了小鼠层粘连蛋白α3链G结构域上的生物学活性位点，并将其与HT1080人纤维肉瘤细胞，HaCaT人皮肤角质形成细胞和人皮肤成纤维细胞（HDF）偶联到琼脂糖凝胶珠上。相对于肽包被的板和/或肽-琼脂糖珠，十一种肽表现出细胞附着活性。 MA3G28（WTIQTTVDRGLL）与HaCaT细胞牢固结合。四种肽促进PC12细胞神经突生长。肝素抑制HDF与包被平板上的8种肽的结合。相反，EDTA显着抑制HDF与MA3G27（NAPFPKLSWTIQ）和MA3G28的结合，但对其他肽的结合没有影响。 HDF细胞形成组织良好的肌动蛋白应激纤维，并与MA3G27上的纽蛋白积累形成局部接触。此外，HDF与MA3G27的结合受到抗α6和抗β1整联蛋白抗体的抑制，这表明MA3G27促进了α6β1整联蛋白介导的细胞粘附。 MA3G57（NQRLASFSNAQQS）仅在肽珠测定中表现出细胞附着活性。与壳聚糖膜缀合的MA3G57促进HDF附着并通过组织良好的肌动蛋白应力纤维扩散。抗β1整联蛋白抗体部分抑制HDF附着于MA3G57-壳聚糖膜，表明MA3G57位点参与β1整联蛋白介导的细胞附着。这些活性位点可能在层粘连蛋白α3链G结构域的生物学活性中很重要，并且对层粘连蛋白-受体相互作用的分子机制的研究很有用。

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