An evolutionarily conserved enzyme degrades transforming growth factor-alpha as well as insulin.
An evolutionarily conserved enzyme degrades transforming growth factor-alpha as well as insulin.
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DOI：
10.1083/jcb.109.3.1301
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发表时间：
1989-09
期刊：
影响因子：
--
通讯作者：
Rosner MR
中科院分区：
文献类型：
--
作者：
Garcia JV;Gehm BD;Rosner MR
在果蝇和哺乳动物细胞中发现的一种酶能够选择性地结合和降解转化生长因子（TGF）-α和胰岛素，但不能在生理浓度下降解EGF。这些生长因子还能够抑制酶对彼此的结合和降解。尽管哺乳动物和果蝇的酶之间存在显著的免疫学差异，但底物特异性高度保守。这些结果表明，在果蝇和哺乳动物细胞中存在选择性TGF-α降解酶。降解胰岛素和TGF-α的能力的进化保守性表明，这种性质对于酶的生理作用及其调节生长因子水平的潜力是重要的。
A single enzyme found in both Drosophila and mammalian cells is able to selectively bind and degrade transforming growth factor (TGF)-alpha and insulin, but not EGF, at physiological concentrations. These growth factors are also able to inhibit binding and degradation of one another by the enzyme. Although there are significant immunological differences between the mammalian and Drosophila enzymes, the substrate specificity has been highly conserved. These results demonstrate the existence of a selective TGF-alpha-degrading enzyme in both Drosophila and mammalian cells. The evolutionary conservation of the ability to degrade both insulin and TGF-alpha suggests that this property is important for the physiological role of the enzyme and its potential for regulating growth factor levels.