Biphasic modulation of cell growth by recombinant human galectin-1
Biphasic modulation of cell growth by recombinant human galectin-1
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DOI：
10.1016/0167-4889(96)00031-6
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发表时间：
1996-06-13
影响因子：
5.1
通讯作者：
Weinberg, CS
中科院分区：
文献类型：
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作者：
Adams, L;Scott, GK;Weinberg, CS
通过聚合酶链式反应对从人骨肉瘤细胞系制备的 cDNA 进行扩增后，人可溶性半乳糖结合凝集素 (galectin-1) 已表达为大肠杆菌融合蛋白。该融合蛋白是一种功能性β-半乳糖苷结合凝集素，从切割的融合蛋白中纯化得到的重组半乳糖凝集素也是如此。重组半乳糖凝集素对细胞增殖具有双相作用。与融合蛋白不同，它作为人类细胞生长抑制剂发挥作用，证实了天然人类半乳糖凝集素-1的早期发现，尽管它的效果不如天然半乳糖凝集素。该反应不会被乳糖显着抑制，因此很大程度上独立于β-半乳糖苷结合位点。在较低浓度下，重组半乳糖凝集素-1 具有促有丝分裂作用，这种活性容易受到乳糖的抑制，因此可归因于该蛋白质的 β-半乳糖苷结合能力。一些肿瘤细胞对生长抑制作用敏感，galectin-1基因在正常细胞和肿瘤细胞中均表达。
Human soluble galactose-binding lectin (galectin-1) has been expressed as an Escherichia coli fusion protein, following the amplification by polymerase chain reaction of cDNA prepared from a human osteosarcoma cell line. The fusion protein is a functional beta-galactoside-binding lectin, as is the recombinant galectin when purified from the cleaved fusion protein. The recombinant galectin has a biphasic effect on cell proliferation. Unlike the fusion protein, it functions as a human cell growth inhibitor, confirming earlier findings with natural human galectin-1, though it is less effective than the natural galectin. This reaction is not significantly inhibited by lactose, and is thus largely independent of the beta-galactoside-binding site. At lower concentrations, recombinant galectin-1 is mitogenic, this activity being susceptible to inhibition by lactose, and thus attributable to the beta-galactoside-binding ability of the protein. Some tumour cells are susceptible to the growth-inhibitory effect, and the galectin-1 gene is expressed in both normal and tumour cells.