Specific blockers of myoblast fusion inhibit a soluble and not the membrane-associated metalloendoprotease in myoblasts.
Specific blockers of myoblast fusion inhibit a soluble and not the membrane-associated metalloendoprotease in myoblasts.
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成肌细胞融合的特异性阻断剂抑制成肌细胞中的可溶性金属内蛋白酶，而不抑制膜相关金属内蛋白酶。
DOI：
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发表时间：
1984
影响因子：
4.8
通讯作者：
W. Strittmatter
中科院分区：
文献类型：
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作者：
C. Couch;W. Strittmatter
我们之前报道过，在肌肉发育过程中，当单核成肌细胞融合形成多核肌管时，细胞融合需要内源性金属内源性蛋白酶的活性。我们在这里报道成肌细胞含有可溶性和膜相关的金属内源性蛋白酶，并且这些蛋白酶具有不同的抑制剂特异性。一些抑制剂，先前显示阻断成肌细胞融合，仅抑制可溶性而非膜相关的成肌细胞金属内蛋白酶活性。另一种金属内源性蛋白酶抑制剂，磷酰胺，对融合没有影响，只抑制膜相关的金属内源性蛋白酶。这些观察结果暗示成肌细胞融合中存在可溶性金属内源性蛋白酶。两种可溶性金属内源性蛋白酶通过柱层析聚焦得到，其pI值分别为pH值5.9和4.8。在pH值为5.9时洗脱的可溶性金属内源性蛋白酶不受阻断融合的抑制剂的抑制，而在pH值为4.8时洗脱的可溶性金属内源性蛋白酶则受到抑制。在成肌细胞中发现的三种金属内源性蛋白酶活性中，成肌细胞融合所需的金属内源性蛋白酶似乎是可溶性金属内源性蛋白酶，pI为4.8。
We previously reported that the cell fusion that occurs during muscle development, when mononucleated myoblasts fuse to form multinucleated myotubes, requires endogenous metalloendoprotease activity at the time of fusion. We report here that myoblasts contain both soluble and membrane-associated metalloendoproteases, and that these proteases have different inhibitor specificities. Several inhibitors, previously shown to block myoblast fusion, inhibit only soluble and not membrane-associated metalloendoprotease activity in myoblasts. Another metalloendoprotease inhibitor, phosphoramidon, which had no effect on fusion, inhibits only the membrane-associated metalloendoprotease. These observations implicate a soluble metalloendoprotease in myoblast fusion. Two soluble metalloendoproteases can be demonstrated by column chromatofocusing, with pI values at pH 5.9 and 4.8. The soluble metalloendoprotease eluted at pH 5.9 is not inhibited by an inhibitor which blocks fusion, while the soluble metalloendoprotease eluted at pH 4.8 is inhibited. Of the three metalloendoprotease activities identified in myoblasts, the metalloendoprotease required in myoblast fusion appears to be the soluble metalloendoprotease with a pI of 4.8.