Results 21 to 30 of about 3,510 (152)

Glycosaminoglycans activate peptidylarginine deiminase 4 by enhancing calcium affinity. [PDF]

Proc Natl Acad Sci U S A
Rheumatoid arthritis is a chronic inflammatory disease driven by abnormal protein modifications. These include citrullination of arginine residues by the calcium-activated enzyme peptidylarginine deiminase 4 (PAD4). However, calcium in body fluids may not fully activate PAD4, suggesting the potential involvement of other activators.
Bereta GP, Bielecka E, Marzec K, Pijanowski Ł, Biela AP, Wilk P, Kamińska M, Nowak J, Wątor-Wilk E, Grudnik P, Kowalczyk D, Kozieł J, Mydel P, Poręba M, Kantyka T.   +14 more
europepmc   +5 more sources

Peptidylarginine deiminase 4 and ADAMTS13 activity in Staphylococcus aureus bacteraemia. [PDF]

Philos Trans R Soc Lond B Biol Sci, 2023
Staphylococcus aureus infection is associated with increased levels of neutrophil extracellular traps (NETs) and von Willebrand factor (VWF), and with reduced activity of ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motifs, member 13).
Martens CP, Peetermans M, Vanassche T, Verhamme P, Jacquemin M, Martinod K.   +5 more
europepmc   +3 more sources

Peptidylarginine deiminase 4 promotes age-related organ fibrosis. [PDF]

J Exp Med, 2017
Aging promotes inflammation, a process contributing to fibrosis and decline in organ function. The release of neutrophil extracellular traps (NETs [NETosis]), orchestrated by peptidylarginine deiminase 4 (PAD4), damages organs in acute inflammatory models.
Martinod K, Witsch T, Erpenbeck L, Savchenko A, Hayashi H, Cherpokova D, Gallant M, Mauler M, Cifuni SM, Wagner DD.   +9 more
europepmc   +7 more sources

Regulation of p53 Target Gene Expression by Peptidylarginine Deiminase 4 [PDF]

Molecular and Cellular Biology, 2008
Histone Arg methylation has been correlated with transcriptional activation of p53 target genes. However, whether this modification is reversed to repress the expression of p53 target genes is unclear. Here, we report that peptidylarginine deiminase 4, a histone citrullination enzyme, is involved in the repression of p53 target genes.
Li, Pingxin, Yao, Hongjie, Zhang, Zhiqiang, Li, Ming, Luo, Yuan, Thompson, Paul R, Gilmour, David S., Wang, Yanming   +7 more
openaire   +3 more sources

Potential protein targets of the peptidylarginine deiminase 2 and peptidylarginine deiminase 4 enzymes in rheumatoid synovial tissue and its possible meaning. [PDF]

Eur J Rheumatol, 2016
Abstract Objective: The molecular mechanism of citrullination involves the calcium-dependent peptidylarginine deiminase (PAD) family of enzymes. These enzymes induce a stereochemical modification of normal proteins and transform them into autoantigens, which in rheumatoid arthritis trigger a complex cascade of joint inflammatory events followed by ...
Badillo-Soto MA, Rodríguez-Rodríguez M, Pérez-Pérez ME, Daza-Benitez L, Bollain-Y-Goytia JJ, Carrillo-Jiménez MA, Avalos-Díaz E, Herrera-Esparza R.   +7 more
europepmc   +4 more sources

Expression of peptidylarginine deiminase 4 in an alkali injury model of retinal gliosis. [PDF]

Biochem Biophys Res Commun, 2017
Citrullination is an important posttranslational modification that occurs during retinal gliosis. We examined the expression of peptidyl arginine deiminases (PADs) to identify the PADs that mediate citrullination in a model of alkali-induced retinal gliosis.
Wizeman JW, Mohan R.
europepmc   +3 more sources

Neutrophil Extracellular Traps Exacerbate Secondary Injury via Promoting Neuroinflammation and Blood–Spinal Cord Barrier Disruption in Spinal Cord Injury

Frontiers in Immunology, 2021
As the first inflammatory cell recruited to the site of spinal cord injury (SCI), neutrophils were reported to be detrimental to SCI. However, the precise mechanisms as to how neutrophils exacerbate SCI remain largely obscure.
Zhou Feng, Lingxia Min, Liang Liang, Beike Chen, Hui Chen, Yi Zhou, Weiwei Deng, Hongliang Liu, Jingming Hou   +8 more
doaj   +1 more source

Role of peptidylarginine deiminase type 4 in gastric cancer

Experimental and Therapeutic Medicine, 2016
Peptidylarginine deiminase type 4 (PADI4) post-translationally converts peptidylarginine to citrulline, appearing to be overexpressed in numerous carcinomas. The current study aimed to investigate the expression of PADI4 in gastric cancer tissues and its effect on the biological activities of SGC-7901 and AGS tumor cell lines.
Xin, Jiang, Song, Xiuqi
openaire   +3 more sources

Association of cross-reactive antibodies targeting peptidyl-arginine deiminase 3 and 4 with rheumatoid arthritis-associated interstitial lung disease. [PDF]

PLoS ONE, 2014
A subset of rheumatoid arthritis (RA) patients have detectable antibodies directed against the peptidyl-arginine deiminase (PAD) enzyme isoforms 3 and 4. Anti-PAD3/4 cross-reactive antibodies (anti-PAD3/4XR) have been shown to lower the calcium threshold
Jon T Giles, Erika Darrah, Sonye Danoff, Cheilonda Johnson, Felipe Andrade, Antony Rosen, Joan M Bathon   +6 more
doaj   +1 more source

Functional roles of the non-catalytic calcium-binding sites in the N-terminal domain of human peptidylarginine deiminase 4. [PDF]

PLoS ONE, 2013
This study investigated the functional roles of the N-terminal Ca(2+) ion-binding sites, in terms of enzyme catalysis and stability, of peptidylarginine deiminase 4 (PAD4).
Yi-Liang Liu, I-Chen Tsai, Chia-Wei Chang, Ya-Fan Liao, Guang-Yaw Liu, Hui-Chih Hung   +5 more
doaj   +1 more source