PAD2 is a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. PAD2 has peptidylarginine deiminase activity against synthetic substrates. PAD2 is mainly expressed in the central nervous system, skeletal muscle, spinal cord, cerebrum, cerebellum, and submaxillary gland. PAD2 play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis.
The Journal of biological chemistry, 264(26), 15255-15260 (1989-09-15)
Various mammalian tissues contain protein-arginine deiminases (EC 3.5.3.15), which convert the arginine residues in normal peptide bonds to the citrulline residues in calcium ion-dependent manners. Here, we describe the complete primary structure of rat skeletal muscle peptidylarginine deiminase deduced from
Archives of biochemistry and biophysics, 407(1), 25-31 (2002-10-24)
Peptidylarginine deiminases (PADs) are posttranslational modification enzymes that convert protein arginine to citrulline residues in a calcium ion-dependent manner. Rodents have four isoforms of PAD (types I, II, III, and IV), each of which is distinct in substrate and tissue
Journal of neuroinflammation, 18(1), 305-305 (2021-12-29)
Microglia are the primary phagocytes of the central nervous system and are responsible for removing damaged myelin following demyelination. Previous investigations exploring the consequences of myelin phagocytosis on microglial activation overlooked the biochemical modifications present on myelin debris. Such modifications
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