Browse our anti-PYCARD (PYCARD) Antibodies

Human PYD and CARD Domain Containing (PYCARD) interaction partners

1. Monocytes from chronic nonbacterial osteomyelitis patients over-express NLRP3, ASC, and IL-1beta. Gene expression is promoted by DNA hypomethylation at NLRP3 and PYCARD.

2. elevated in amniotic fluid concentrations of women with clinical chorioamnionitis

3. These findings suggest that pyroptotic CD14CD16 classical monocytes of HIV-1-infected patients release ASC specks into the blood stream, a phenomenon that may contribute to HIV-1 induced inflammation and immune activation.

4. increased in amniotic fluid in spontaneous labor at term

5. ASC forms approximately 6-7-nm-wide filaments that stack laterally to form bundles. The structural characteristics and dimensions of the bundles indicate that both PYD and CARD are integral parts of the filament.

6. For the first time, using single-molecule Forster resonance energy transfer, this work studied the relative positions of the CARD and PYD domains of full-length ASC. An unexpectedly large conformational change occurred upon ASC fibrillation, suggesting that the CARD domain folds back onto the PYD domain.

7. High ASC expression is associated with Gastric Cancer.

8. Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1.

9. ASC specks as a putative biomarker of pyroptosis in myelodysplastic syndromes

10. results suggest that ASC, as a negative regulator of the MAVS-mediated innate immunity, may play an important role in host protection upon virus infection

11. PYCARD gene and its transcript variant may play a critical and regulative role in the inflflammatory response of primary gout patients with different phases and Chinese medicine syndromes.

12. ASC may be involved in tumor suppression and cell death via Bcl-2 and phosphor Src.

13. Data show that in HK-2 cells and unilateral nephrectomy model, ASC expression level is significantly augmented after treatment with contrast media. Its silencing attenuates contrast-induced apoptosis in HK-2 cell.

14. ASC specks released by microglia bind to amyloid-beta and increase amyloid-beta oligomer and aggregate formation, acting as an inflammation-driven cross-seed for amyloid-beta pathology

15. ASC contributes to oral cavity squamous cell carcinoma metastasis, and high-level ASC expression is a marker for poor prognosis in OSCC patients

16. ASC CpG methylation may prove to be a primary regulator of the pathogenesis of chronic inflammatory diseases such as heart failure.

17. besides its role in the inhibition of the NF-kappaB pathway, NLRC3 interferes with the assembly and activity of the NALP3 inflammasome complex by competing with ASC for pro-caspase-1 binding

18. ASC Induces Apoptosis via Activation of Caspase-9 by Enhancing Gap Junction-Mediated Intercellular Communication.(

19. These data revealed that cross-linking of ASC(PYD) filaments via ASC(CARD) mediates the assembly of ASC foci.

20. Down-regulation of mRNA expression was found in cases in which CASP8, TMS1 and DAPK were hypermethylated.

Mouse (Murine) PYD and CARD Domain Containing (PYCARD) interaction partners

1. Apoptosis-associated speckle-like protein (Asc) knockout mice have increased susceptibility to Cryptosporidium parvum infection compared to wild-type mice. Susceptibility correlated with a lack of IL-18 either in the intestine or in the sera of caspase-1 knockout mice, whereas IL-18 is significantly elevated in wild-type mice.

2. High ASC expression is associated with Gastric Cancer.

3. ASC has a role in the regulation of renal fibrosis and endoplasmic reticulum stress after unilateral ureter obstruction, strongly indicating that ASC could serve as an attractive target in the treatment of chronic kidney disease

4. both Nlrp3(-/-) and Asc(-/-) mice showed a strongly improved host defense, as reflected by a markedly reduced mortality rate accompanied by diminished bacterial growth and dissemination.

5. Cl(-) channel-dependent formation of dynamic ASC oligomers and inflammasome specks that remain inactive in the absence of K(+) efflux. Formed after Cl(-) efflux exclusively, ASC specks are NLRP3 dependent, reversible, and inactive, although they further prime inflammatory responses.

6. we found that butyrate significantly decreased Nlrp3 inflammasome formation and activation in the carotid arterial wall of wild type mice (Asc(+/+)), which was comparable to the effect of gene deletion of the adaptor protein apoptosis-associated speck-like protein gene (Asc(-/-)).

7. oligomerization of ASC creates a multitude of potential caspase-1 activation sites, thus serving as a signal amplification mechanism for inflammasome-mediated cytokine production

8. Collectively, these results are consistent with a model whereby the type III secretion system apparatus of Pseudomonas aeruginosa activates the caspase-1-dependent inflammasome and caspase-3/7 through an ASC-dependent mechanism.

9. ASC specks released by microglia bind to amyloid-beta and increase amyloid-beta oligomer and aggregate formation, acting as an inflammation-driven cross-seed for amyloid-beta pathology

10. results suggest that although Pyk2 and FAK are involved in inflammasome activation, only Pyk2 directly phosphorylates ASC and brings ASC into an oligomerization-competent state by allowing Tyr146 phosphorylation to participate ASC speck formation and subsequent NLRP3 inflammation.

11. Alendronate (ALN)-augmented IL-1beta production and cell death require Smad3 and ASC activation, and SIS3 and anti-ASC antibodies may serve as palliative agents for necrotizing inflammatory diseases caused by ALN

12. These data provide evidence that the inflammasome components ASC, NLRP3 and AIM2 play a role in regulating macrophage adhesion and activation in response to surface nanotopography and chemistry.

13. SGLT-2 inhibition with dapagliflozin reduces the activation of the Nlrp3/ASC inflammasome and attenuates the development of diabetic cardiomyopathy in mice with type 2 diabetes. Effects are augmentated of the by DPP4 inhibitor Saxagliptin.

14. Elevations of CO2 cause oligomerization of the inflammasome components ASC, NLRP3, caspase 1, thioredoxin interacting protein, and calreticulin - a protein from endoplasmic reticulum, leading to IL-1beta synthesis. An increased production rate of MPs containing elevated amounts of IL-1beta persists for hours after short-term exposures to elevated CO2

15. Our cumulative findings indicate that ASC suppresses cancer metastasis and progression via the modulation of cytoskeletal remodeling and the Src-caspase-8 signaling pathway.

16. these findings suggest that p205 controls expression of Asc mRNA to regulate inflammasome responses. These findings expand on our understanding of immune-regulatory roles for the PYHIN protein family.

17. this study shows that ASC-dependent Inflammasomes do not shape the commensal gut microbiota composition

18. Our data identify RIPK3 and the ASC inflammasome as key tumor suppressors in AML.

19. Data show that T cell-intrinsic PYD and CARD domain containing protein ASC is required for TH17-mediated experimental autoimmune encephalomyelitis (EAE).

20. Data suggest that interleukin 22 (IL-22) plays a pro-inflammatory/pathogenic role in the onset of antigen-induced arthritis (AIA) through apoptosis-associated speck-like Pycard protein (ASC)-dependent stimulation of interleukin-1 beta (IL-1beta) production.

Zebrafish PYD and CARD Domain Containing (PYCARD) interaction partners

1. The fish caspase-1 homolog Caspy, but not the caspase-4/11 homolog Caspy2, interacts with zebrafish ASC through homotypic PYD-PYD interactions, which differ from those in mammals.