Deimination of 70-kD nuclear protein during epidermal apoptotic events in vitro
Deimination of 70-kD nuclear protein during epidermal apoptotic events in vitro
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DOI：
10.1177/002215549804601110
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发表时间：
1998-11-01
影响因子：
3.2
通讯作者：
Ogawa, H
中科院分区：
文献类型：
--
作者：
Mizoguchi, M;Manabe, M;Ogawa, H
肽基精氨酸脱亚胺酶（PAD）是负责将蛋白质结合的精氨酸残基转化为瓜氨酸的酶。最近已经表明，许多表皮蛋白，包括聚丝蛋白、透明质蛋白和角蛋白，通过PAD的作用被脱亚氨基化，这表明蛋白脱亚氨基化在表皮分化的最后阶段可能起作用。我们在这里报告了一种新的PAD基板过程中发现的脱亚胺蛋白在培养的大鼠表皮角质形成细胞。我们发现，一个70 kD的蛋白质定位于细胞核的周边优先脱亚胺离子霉素治疗后，在2 mM的钙的存在下，并与这些细胞中的凋亡事件。此外，我们发现，核蛋白的脱亚胺化可以通过将PAD cDNA转染到大鼠表皮角质形成细胞中来诱导。这些数据表明，PAD可能作用于70 kD的核蛋白，诱导解体的核板层，并促进细胞凋亡在终末表皮分化。
Peptidylarginine deiminase (PAD) is the enzyme responsible for converting protein-bound arginine residues to citrulline. it has recently been shown that a number of epidermal proteins, including filaggrin, trichohyalin, and keratins, are deiminated by the action of PAD, suggesting a possible role for protein deimination during the final stages of epidermal differentiation. We report here a novel PAD substrate found during the course of identifying deiminated proteins in cultured rat epidermal keratinocytes. We found that a 70-kD protein localized to the periphery of the nucleus was preferentially deiminated after ionomycin treatment in the presence of 2 mM calcium and was associated with apoptotic events in these cells. Furthermore, we discovered that the deimination of nuclear protein could be induced by transfection of a PAD cDNA into rat epidermal keratinocytes. These data suggest that PAD may act on the 70-kD nuclear protein to induce disassembly of the nuclear lamina and promote apoptosis during terminal epidermal differentiation.