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Anti-Peptidylarginine Deiminase 4 Autoantibodies Derived From Patients With Rheumatoid Arthritis Exert Pathogenic Effects by Activating Monocytes and Exacerbating Inflammatory Arthritis. [PDF]

Arthritis Rheumatol
Won T, Naik P, Wood MK, Wang H, Talor MV, Shi J, Bracamonte-Baran W, Thomas MA, Jaime CM, Jo W, Ray S, Foss CA, Andrade F, Čiháková D, Darrah E.   +14 more
europepmc   +1 more source

IL-22 Downregulates Peptidylarginine Deiminase-1 in Human Keratinocytes: Adding Another Piece to the IL-22 Puzzle in Epidermal Barrier Formation

Journal of Investigative Dermatology, 2022
International audienceIncreased presence of IL-22+ cells in the skin is a characteristic finding in skin barrier defects, such as psoriasis and atopic dermatitis.
Ankit Srivastava, Liv Eidsmo, Josefin Lysell   +2 more
exaly   +2 more sources

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Peptidylarginine Deiminase and Alzheimer’s Disease

Journal of Alzheimer's Disease, 2022
Peptidylarginine deiminases (PADs) are indispensable enzymes for post-translational modification of proteins, which can convert Arg residues on the surface of proteins to citrulline residues. The PAD family has five isozymes, PAD1, 2, 3, 4, and 6, which have been found in multiple tissues and organs.
Lai, Wang, Hongyang, Chen, Jing, Tang, Zhengwei, Guo, Yanming, Wang   +4 more
openaire   +2 more sources

Citrullination by Peptidylarginine Deiminase in Rheumatoid Arthritis

Annals of the New York Academy of Sciences, 2007
Abstract:  Rheumatoid arthritis (RA) is a complex, multifactorial disease with genetic and immunological aspects. Because RA is an autoimmune condition, dysregulation of the immune system is implied. Many linkage and association studies have also indicated that multiple genetic factors are associated with RA.
Akari, Suzuki, Ryo, Yamada, Kazuhiko, Yamamoto   +2 more
openaire   +2 more sources

Peptidylarginine deiminase 4 and citrullination in health and disease

Autoimmunity Reviews, 2010
Deimination is catalyzed by a family of calcium binding enzymes, called peptidylarginine deiminases (PADs). Among these, the PAD4 isoform has been more extensively studied for its role in some autoimmune diseases. PAD4 is localized in the cytoplasm of monocytes, T and B cells, neutrophils, eosinophils and NK cells and can move to the nucleus upon cell ...
Paola Migliorini, Federico Pratesi, Consuelo Anzilotti   +2 more
exaly   +3 more sources

The developmental expression and activity of peptidylarginine deiminase in the mouse

Neuroscience Letters, 1999
We have measured the expression and activity of peptidylarginine deiminase (PAD, EC 3.5.3.15), the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate. PAD transcripts were detected as early as five days and were maximal at one month of age. The enzyme protein was also detected at 5 days in an
L B, Pritzker, T A, Nguyen, M A, Moscarello   +2 more
openaire   +2 more sources

Peptidylarginine deiminase in rat and mouse hemopoietic cells

Experientia, 1990
Peptidylarginine (protein-L-arginine) deiminase activities have been demonstrated in extracts of rat and mouse peritoneal macrophages, bone marrow cells, splenic adherent cells, neutrophils, and mouse monocyte/macrophage cell lines. The enzyme in these cells is indistinguishable from the skeletal muscle enzyme with respect to immunochemical properties.
T Senshu
exaly   +3 more sources

Porphyromonas gingivalis peptidylarginine deiminase substrate specificity

Anaerobe, 2013
While a group of oral commensals have been implicated in the aetiology of chronic periodontitis; the asaccharolytic Gram negative anaerobe Porphyromonas gingivalis is most commonly reported to be associated with severe forms of the disease. Although a variety of human tissues can produce a number of peptidylarginine deiminase (PAD), enzymes that ...
Abdullah, S., Farmer, E., Spargo, L., Logan, R., Gully, N.   +4 more
openaire   +3 more sources

Peptidylarginine deiminases 4 as a promising target in drug discovery

European Journal of Medicinal Chemistry, 2021
Peptidylarginine deaminase 4 (PAD4) is a crucial post-translational modifying enzyme catalyzing the conversion of arginine into citrulline residues, and mediating the formation of neutrophil extracellular traps (NETs). PAD4 plays a vital role in the occurrence and development of cardiovascular diseases, autoimmune diseases, and various tumors ...
Chao, Yang, Zhen-Zhen, Dong, Jing, Zhang, Dehong, Teng, Xinzhi, Luo, Dan, Li, Yingtang, Zhou   +6 more
openaire   +2 more sources

Structures and Functions of Peptidylarginine Deiminases

2017
Molecular structures of peptidylarginine deiminase (PAD) isozymes are strongly associated with their functions. This chapter summarizes the X-ray structures of PAD1, PAD2, and PAD4 as well as that of the PAD from the periodontal pathogen Porphyromonas gingivalis.
Masaki Unno, Kenji Kizawa, Hidenari Takahara   +2 more
openaire   +1 more source