## Abstract Peptidylarginine deiminases (PADs) are a group of posttranslational modification enzymes that citrullinate (deiminate) protein arginine residues in a Ca^2+^βdependent manner. Enzymatic citrullination abolishes positive charges of native protein molecules, inevitably causing significant
Age-related increase in peptidylarginine deiminase in the male rat pituitary
β Scribed by Kyoichi Akiyama; Saburou Nagata; Kazutada Watanabe; Gen Watanabe; Kazuyoshi Taya; Shuji Sasamoto; Tatsuo Senshu
- Book ID
- 116084821
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 850 KB
- Volume
- 81
- Category
- Article
- ISSN
- 0047-6374
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π SIMILAR VOLUMES
Insulin and type I insulin-like growth factor (IGF-I) suppressed growth hormone (GH) expression followed by the induction of prolactin (PRL) biosynthesis in MtT/S cells cultured with normal sera. Insulin also increased the peptidylarginine deiminase activity in a dose-dependent manner. The increase
## Abstract Peptidylarginine deiminases (PADs) are Ca2t+-dependant post-translational modification enzymes that catalyze the citrullination of protein arginyl residues. PAD type 2 (PAD2) is thought to be involved in some processes of neurodegeneration and myelination in the central nervous system.
## Abstract We have studied the expression of peptidylarginine deiminase in rat pituitaries during pregnancy. Both the enzyme protein and its mRNA decreased to low levels after the onset of gestation. Both started to increase markedly during mid pregnancy reaching their maxima on day 18 and decline