Ishigami A, Ohsawa T, Watanabe K, Senshu T
Department of Cell Chemistry, Tokyo Metropolitan Institute of Gerontology, Japan.
Biochem Biophys Res Commun. 1996 Jun 14;223(2):299-303. doi: 10.1006/bbrc.1996.0888.
We studied the expression of peptidylarginine deiminases (EC 3.5.3.15) in an immortalized newborn rat keratinocyte cell line. No measurable enzyme activities were noted in either growing or confluent cultures. The enzyme activity was increased by all-trans retinoic acid in dose- and time-dependent manners. The enzyme activity was resolved into two peaks by anion exchange chromatography. The minor peak resembled enzyme preparations obtained from the epidermis in earlier studies. The major peak was indistinguishable from rat muscle peptidylarginine deiminase in the chromatographic and Western blotting profiles. Northern blot hybridization showed a major band in retinoic acid-treated cells migrating slightly behind muscle peptidylarginine deiminase mRNA.
我们研究了肽基精氨酸脱亚氨酶（EC 3.5.3.15）在永生化新生大鼠角质形成细胞系中的表达。在生长或汇合培养物中均未检测到可测量的酶活性。全反式维甲酸以剂量和时间依赖性方式增加了酶活性。通过阴离子交换色谱法将酶活性解析为两个峰。较小的峰类似于早期研究中从表皮获得的酶制剂。在色谱和蛋白质印迹图谱中，较大的峰与大鼠肌肉肽基精氨酸脱亚氨酶无法区分。Northern印迹杂交显示，在维甲酸处理的细胞中出现一条主要条带，其迁移位置略落后于肌肉肽基精氨酸脱亚氨酶mRNA。
