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首页> 外文期刊>Journal of Neuroimmunology: Official Bulletin of the Research Committee on Neuroimmunology of the World Federation of Neurology >Cleavage of myelin associated glycoprotein by matrix metalloproteinases.
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Cleavage of myelin associated glycoprotein by matrix metalloproteinases.

机译：基质金属蛋白酶切割髓鞘相关糖蛋白。

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摘要

Derivative myelin associated glycoprotein (dMAG) results from proteolysis of transmembrane MAG and can inhibit axonal growth. We have tested the ability of certain matrix metalloproteinases (MMPs) elevated with inflammatory and demyelinating diseases to cleave MAG. We show MMP-2, MMP-7 and MMP-9, but not MMP-1, cleave recombinant human MAG. Cleavage by MMP-7 occurs at Leu 509, just distal to the transmembrane domain and, to a lesser extent, at Met 234. We also show that MMP-7 cleaves MAG expressed on the external surface of CHO cells, releasing fragments that accumulate in the medium over periods of up to 48 h or more and that are able to inhibit outgrowth by dorsal root ganglion (DRG) neurons. We conclude that MMPs may have the potential both to disrupt MAG dependent axon-glia communication and to generate bioactive fragments that can inhibit neurite growth.
机译：衍生性髓磷脂相关糖蛋白（dMAG）由跨膜MAG的蛋白水解产生，可抑制轴突生长。我们已经测试了某些炎症和脱髓鞘疾病引起的基质金属蛋白酶（MMP）裂解MAG的能力。我们显示MMP-2，MMP-7和MMP-9，但不是MMP-1，裂解重组人MAG。 MMP-7的切割发生在Leu 509，恰好在跨膜结构域的远端，在较小的程度上发生在Met 234。在长达48小时或更长时间的时间内，该培养基能够抑制背根神经节（DRG）神经元的生长。我们得出的结论是，MMPs可能具有破坏MAG依赖的轴突-胶质细胞通讯和产生可抑制神经突生长的生物活性片段的潜力。

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