Developmental and age-related changes of peptidylarginine deiminase 2 in the mouse brain.

Peptidylarginine deiminases (PADs) are a group of posttranslational modification enzymes that citrullinate (deiminate) protein arginine residues in a Ca(2+)-dependent manner. Enzymatic citrullination abolishes positive charges of native protein molecules, inevitably causing significant alterations in their structure and functions. Among the five isoforms of PADs, PAD2 and PAD4 are proved occupants of the central nervous system (CNS), and especially PAD2 is a main PAD enzyme expressed in the CNS.

Microglial expression of peptidylarginine deiminase 2 in the prenatal rat brain.

Peptidylarginine deiminases (PADs) are Ca(2+)-dependent 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. In this study, we found PAD2-positive cells in rat cerebra in 19-to 21-day old embryos, i.

Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease.

Citrullinated proteins are the products of a posttranslational process in which arginine residues undergo modification into citrulline residues when catalyzed by peptidylarginine deiminases (PADs) in a calcium ion-dependent manner. In our previous report, PAD2 expressed mainly in the rat cerebrum became activated early in the neurodegenerative process. To elucidate the involvement of protein citrullination in human neuronal degeneration, we examined whether citrullinated proteins are produced during Alzheimer's disease (AD).

Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin.

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 specificity. In fact, the only tissue in which all four PAD mRNAs have been detected is the epidermis.

Increased and type II-specific expression of peptidylarginine deiminase in activated microglia but not hyperplastic astrocytes following kainic acid-evoked neurodegeneration in the rat brain.

Peptidylarginine deiminases (PADs) are a group of posttranslational modification enzymes that convert protein arginine residues to citrulline residues. In the rat cerebrum, the type II PAD is thought to be expressed mainly in glial cells, especially astrocytes, and to become activated early in the neurodegenerative process. To determine whether hyperplastic glial cells express PAD type II, we examined the rat brain after kainic acid-evoked neurodegeneration.

Two-Dimensional Gel Electrophoretic Analysis of the Cerebella from Neuro-Pathologically-Mutant Weaver, Nervous and Staggerer Mice : (cerebellum/cerebellar mutant mice/Purkinje cell staggerer/nervous/weaver).

We have analysed the proteins of the cerebella from mutant and control mice by applying high resolution two-dimensional polyacrylamide gel electrophoresis. The tissue of each cerebellum and also the pallium cerebri were fractionated into water-soluble and particulate fractions, and these were used in gel electrophoresis. In order to augment the sensitivity for detection of protein spots, we applied silver staining.