Results 121 to 130 of about 3,510 (152)

Expression of anti‐Porphyromonas gingivalis peptidylarginine deiminase immunoglobulin G and peptidylarginine deiminase‐4 in patients with rheumatoid arthritis and periodontitis

Journal of Periodontal Research, 2015
Background and ObjectiveAutoimmunity against citrullinated proteins through peptidylarginine deiminase (PAD) may be involved in the pathophysiology of rheumatoid arthritis (RA). The present study evaluated the serum levels of antibodies to citrullinated proteins and to Porphyromonas gingivalis PAD (PPAD), and the endogenous expression of PAD‐4, in ...
A, Shimada, T, Kobayashi, S, Ito, M, Okada, A, Murasawa, K, Nakazono, H, Yoshie   +6 more
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Peptidylarginine deiminase-4: Medico-formulative strategy towards management of rheumatoid arthritis

Biochemical Pharmacology, 2022
Peptidylarginine deiminase-4 (PAD4) is a calcium-dependent enzyme that catalyzes the conversion of arginine into citrulline of macromolecules in the body. It governs several processes including apoptosis, innate immunity (Netosis), and pluripotency.
Indhumathi, Thirugnanasambandham, Arun, Radhakrishnan, Gowthamarajan, Kuppusamy, Sachin, Kumar Singh, Kamal, Dua   +4 more
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Peptidylarginine Deiminase 4 as a Possible Biomarker of Plaque Instability in Carotid Artery Stenosis

Journal of Stroke and Cerebrovascular Diseases, 2021
Neutrophil extracellular traps (NETs) exhibit pro-inflammatory and pro-thrombotic properties. However, they have only been reported as important regulators in atherosclerosis, especially in atherothrombosis. We investigated the presence of NETs and plaque instability in patients with carotid artery stenosis.A total of 39 consecutive patients with ...
Koji Shimonaga, Toshinori Matsushige, Hiroki Takahashi, Yukishige Hashimoto, Michitsura Yoshiyama, Chiaki Ono, Shigeyuki Sakamoto   +6 more
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The enzymology of human peptidylarginine deiminase 4

2005
The human peptidylarginine deiminase 4 gene and several mutations were recently linked to rheumatoid arthritis susceptibility. Though it is known that these mutations can result in a longer lived mRNA, nothing was known as to whether these mutations, 3 of which result in codon changes, affected the enzyme activity of peptidylarginine deiminase 4 (PAD4).
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Peptidylarginine deiminase type 4: identification of a rheumatoid arthritis-susceptible gene

Trends in Molecular Medicine, 2003
Recent studies using linkage disequilibrium and SNPs uncovered a rheumatoid arthritis (RA)-susceptible haplotype in the gene encoding peptidylarginine deiminase (PADI) type 4. This gene is one of four known PADI genes that encode enzymes to change arginine into citrulline in proteins.
Ryo, Yamada, Akari, Suzuki, Xiotian, Chang, Kazuhiko, Yamamoto   +3 more
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Predominance of IgG1 and IgG3 subclasses of autoantibodies to peptidylarginine deiminase 4 in rheumatoid arthritis

Clinical Rheumatology, 2011
Analysis of IgG subclass distribution of antibodies may provide insights into the mechanisms driving antibody production. Here, we have first determined IgG subclass distribution of anti-recombinant peptidylarginine deiminase 4 (anti-hPADI4) antibodies in sera from patients with rheumatoid arthritis (RA).
Wei, Wang, Jinming, Li
openaire   +4 more sources

A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity

Analytical Biochemistry, 2005
A simple, continuous spectrophotometric assay for peptidylarginine deiminase (PAD) is described. Deimination of peptidylarginine results in the formation of peptidylcitrulline and ammonia. The ammonia released during peptidylarginine hydrolysis is coupled to the glutamate-dehydrogenase-catalyzed reductive amination of alpha-ketoglutarate to glutamate ...
Ya-Fan, Liao, Hui-Chieh, Hsieh, Guang-Yaw, Liu, Hui-Chih, Hung   +3 more
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Glycosaminoglycans act as activators of peptidylarginine deiminase 4

Abstract Peptidylarginine deiminase 4 (PAD4) is a citrullinating enzyme that is gathering increasing attention due to its possible involvement in physiological processes as well as in the pathogenesis of diseases like rheumatoid arthritis or thrombosis.
Grzegorz P. Bereta, Ewa Bielecka, Karolina Marzec, Łukasz Pijanowski, Artur Biela, Piotr Wilk, Marta Kamińska, Jakub Nowak, Elżbieta Wątor, Przemysław Grudnik, Dominik Kowalczyk, Joanna Kozieł, Piotr Mydel, Marcin Poręba, Tomasz Kantyka   +14 more
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Localization and expression of peptidylarginine deiminase 4 (PAD4) in mammalian oocytes and preimplantation embryos

Zygote, 2011
SummaryPost-translational modifications generally involve the addition or removal of various functional groups to or from the protein residues. However, citrullination, which is catalyzed by the peptidylarginine deiminases (PADs), involves conversion of one kind of amino acid residue into another. One of five isoforms, PAD4 is a nuclear enzyme known to
Manjula, Brahmajosyula, Masashi, Miyake
openaire   +2 more sources

Role of peptidylarginine deiminase 4 (PAD4) in pig parthenogenetic preimplantation embryonic development

Zygote, 2012
SummaryArginine modification to citrulline (citrullination) is catalyzed by peptidylarginine deiminases (PADs) and one of the isomers PAD4 is shown to be involved in the gene regulation. In our previous paper we studied the localization and expression of PAD4 and the target of PAD4 in mammalian gametes and preimplantation embryos.
Manjula, Brahmajosyula, Masashi, Miyake
openaire   +2 more sources