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首页> 外文期刊>Journal of cellular biochemistry. >A protease storm cleaves a cell-cell adhesion molecule in cancer: Multiple proteases converge to regulate PTPmu in glioma cells
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A protease storm cleaves a cell-cell adhesion molecule in cancer: Multiple proteases converge to regulate PTPmu in glioma cells

机译：蛋白酶风暴在癌症中裂解细胞粘附分子：多种蛋白酶聚合以调节神经胶质瘤细胞中的PTPmu

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Cleavage of the cell-cell adhesion molecule, PTPμ, occurs in human glioblastoma multiforme brain tumor tissue and glioma cell lines. PTPμ cleavage is linked to increased cell motility and growth factor independent survival of glioma cells in vitro. Previously, PTPμ was shown to be cleaved by furin in the endoplasmic reticulum to generate membrane associated E- (extracellular) and P- (phosphatase) subunits, and by ADAMs and the gamma secretase complex at the plasma membrane. We also identified the presence of additional extracellular and intracellular PTPμ fragments in brain tumors. We set out to biochemically analyze PTPμ cleavage in cancer cells. We determined that, in addition to the furin-processed form of PTPμ, a pool of 200kDa full-length PTPμ exists at the plasma membrane that is cleaved directly by ADAM to generate a larger shed form of the PTPμ extracellular segment. Notably, in glioma cells, full-length PTPμ is also subject to calpain cleavage, which generates novel PTPμ fragments not found in other immortalized cells. We also observed glycosylation and phosphorylation differences in the cancer cells. Our data suggest that an additional serine protease also contributes to PTPμ shedding in glioma cells. We hypothesize that a "protease storm" occurs in cancer cells whereby multiple proteases converge to reduce the presence of cell-cell adhesion molecules at the plasma membrane and to generate protein fragments with unique biological functions. As a consequence, the "protease storm" could promote the migration and invasion of tumor cells. J. Cell. Biochem. 115: 1609-1623, 2014.
机译：细胞-细胞粘附分子PTPμ的切割发生在人成胶质细胞瘤多形性脑肿瘤组织和神经胶质瘤细胞系中。 PTPμ裂解与胶质瘤细胞的体外细胞运动性和独立于生长因子的存活有关。以前，PTPμ被内质网中的弗林蛋白酶切割以产生与膜相关的E-（细胞外）和P-（磷酸酶）亚基，并被ADAM和质膜上的γ-分泌酶复合物切割。我们还确定了脑肿瘤中其他细胞外和细胞内PTPμ片段的存在。我们着手进行生化分析癌细胞中PTPμ的裂解。我们确定，除了弗林蛋白酶处理过的PTPμ形式外，在质膜上还存在200kDa全长PTPμ的池，该池直接被ADAM裂解以生成较大的PTPμ细胞外节段。值得注意的是，在神经胶质瘤细胞中，全长PTPμ也要进行钙蛋白酶切割，这会产生在其他永生化细胞中未发现的新型PTPμ片段。我们还观察到癌细胞中糖基化和磷酸化的差异。我们的数据表明，另外一种丝氨酸蛋白酶也有助于神经胶质瘤细胞中PTPμ的脱落。我们假设在癌细胞中发生“蛋白酶风暴”，从而多种蛋白酶聚合以减少质膜上细胞粘附分子的存在并产生具有独特生物学功能的蛋白质片段。结果，“蛋白酶风暴”可能促进肿瘤细胞的迁移和侵袭。 J.细胞。生化。 115：1609-1623，2014。

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