anti-Peptidyl Arginine Deiminase, Type II (PADI2) Antibodies

Human Peptidyl Arginine Deiminase, Type II (PADI2) interaction partners

1. Chronic gingival inflammation is associated with increased local citrullination and PAD2 and PAD4 expression in periodontitis.

2. In most rheumatoid arthritis patients, PAD2 and PAD4 are equally efficient in generating citrullinated target sites for anti-citrullinated protein antibodies (ACPAs) in fibrinogen and ENO1. The binding of autoantibodies to histone H3 was generally higher after citrullination with PAD4 than with PAD2. Citrullinated human serum albumin is not a target for ACPAs.

3. the mRNA expression of PADI2, PADI4 and Sp1 is upregulated in rheumatoid arthritis bone marrow CD34+ cells independently of the systemic inflammation or treatment regimen.

4. These data suggest that overexpression of the human PAD2 transgene in the epidermis of transgenic mice increases the malignant conversion rate of benign tumors by promoting an inflammatory microenvironment.

5. Brain gene expression of PADI2, ZNF385A, PSD2, and A2ML1 and DNA methylation dysregulations are implicated in the alteration of brain tissue properties associated with late-life cognitive decline above and beyond the influence of common neuropathologic conditions.

6. Peptidyl arginine deiminase 2 (PADI2) is required for activation of androgen receptor (AR) signaling under androgen-deprived condition.

7. Data suggest that protein-arginine deiminase 2 (PADI2) suppresses the proliferation of colonic epithelial cells through catalysis of protein citrullination, and that downregulation of PADI2 expression might therefore contribute to colon carcinogenesis.

8. Downregulation of PADI2 is an early event in the pathogenesis of colorectal cancer associated with poor prognosis and points toward a possible role of citrullination in modulating tumor cells and their microenvironment.

9. Multiple proteins citrullinated by hypoxia-induced PADs were identified. In addition, the extracellular domain of vascular endothelial growth factor receptor 2 was citrullinated by human PAD2 in vitro. CONCLUSION: Our data may contribute to understanding of pathophysiology of malignant gliomas from the aspects of protein citrullination.

10. Deimination of myelin basic protein (MBP) by peptidylarginine deiminase (PAD) prevents its binding to the proteasome and decelerates its degradation by the proteasome in mammalian cells. Potential anticancer drug tetrazole analogue of chloramidine 2, at concentrations greater than 1 microM inhibits the enzymatic activity of PAD in vitro.

11. this study shows that a miR-4728 downregulates PADI2, a novel rheumatoid arthritis risk gene

12. We identified the presence of PADI3 mRNA expression in synovial tissue and PADI2 and PADI4 mRNA expressions in fibroblast-like synoviocytes from patients with rheumatoid arthritis.

13. Protein arginine deiminase 2 binds six calcium ions in an ordered fashion.

14. PAD2 activity was significantly higher in cell-free synovial fluid of rheumatoid arthritis patients compared to osteoarthritis patients.

15. PAD2 activity was detected in synovial fluid samples from patients with rheumatoid arthritis.

16. Report increased levels of extracellular PAD2 in the lungs of smokers.

17. PADI2 and vimentin participate in the apoptotic mechanisms of activated T lymphocytes.

18. these studies provide the first genetic evidence that PAD2 functions as an oncogene and suggest that PAD2 may promote tumor progression by enhancing inflammation within the tumor microenvironment.

19. PAD2 appears to use a substrate-assisted mechanism of catalysis in which the positively charged substrate guanidinium depresses the pKa of the nucleophilic cysteine

20. Data suggest peptidylarginine deiminase 2 (PAD2) as a possible biomarker in various inflammatory diseases.

Cow (Bovine) Peptidyl Arginine Deiminase, Type II (PADI2) interaction partners

1. results describe the role of peptidyl arginine deiminase and arginine metabolism in the formation of amyloid fibrils from beta-amyloid peptides

Mouse (Murine) Peptidyl Arginine Deiminase, Type II (PADI2) interaction partners

1. PADi2 contributes to TNFalpha-induced citrullination and arthritis, but is not required for neutrophil extracellular traps formation

2. Taken together, our study is the first to indicate the potential role of Padi2 as an angiogenesis-regulating gene. The characterization of Padi2 and other genes in associated pathways may provide new understanding of angiogenesis regulation and novel targets for diagnosis and treatment of a wide variety of angiogenesis-dependent diseases.

3. peptidyl-arginine deiminases inhibiion reverses protein-hypercitrullination and disease in mouse models of multiple sclerosis.

4. GPx7 is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys mechanism in which GSH and PDI are alternative substrates.

5. Results suggest that PADI2 may function as an important new biomarker for HER2/ERBB2+ tumors and that Cl-amidine represents a new candidate for breast cancer therapy.

6. Activation of the P2X7 purinergic receptor (P2X7) by the inflammatory danger signal ATP induces PAD2 activity and robust protein citrullination in mast cells.

7. different subcellular compartmentalization of PADi2 and citrullinated proteins may have different physiological roles in normal and neurodegenerative conditions

8. PAD2 interacts with IKKgamma and suppresses NF-kappaB activity.

9. Results suggest that peptidylarginine deiminase 2-catalyzed citrullination is not essential to the development of experimental autoimmune encephalomyelitis.

10. An increase in citrullinated proteins resulting from increased PAD2 and 4 is an important change in the pathogenesis of multiple sclerosis.

11. This study suggests that accumulated citrullinated proteins and abnormal activation of PAD2 may function in the pathogenesis of prion diseases and serve as potential therapeutic targets.

12. elevated levels of the pro-inflammatory cytokine TNF-alpha and nuclear histone deimination support initiation of demyelination by increased PAD activity