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The protein encoded by APCS is a glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization.
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The findings suggest that the F57I mutation affects the aggregation process of lysozyme (show LYZ ELISA Kits) resulting in the formation of cytotoxic species and that SAP is able to prevent cell death in the F57I flies by preventing accumulation of toxic F57I structures.
Data suggest that SAP (serum amyloid P-component) interacts with at least 33 proteins/ligands in plasma containing physiological calcium levels; these ligands can be categorized to include apolipoproteins, complement system proteins, coagulation proteins, and components that regulate proteolysis.
Data suggest that serum haptoglobin, fetuin-A, platelet factor-4, hs-CRP (high sensitive-C-reactive protein), SAP (serum amyloid P), AGP (alpha1-acid glycoprotein) levels of adolescents with metabolic syndrome are significantly higher than those of controls subjects.
SNPs in APCS were associated with late age at onset in familial amyloid polyneuropathy.
Data suggest that serum amyloid P (SAP) activates CD209 DC-SIGN (show CD209 ELISA Kits) to regulate the innate immune system differently from C-reactive protein (CRP (show CRP ELISA Kits)), and that DC-SIGN (show CD209 ELISA Kits) is a target for antifibrotics.
Here, it is reported that X-ray analysis of the SAP complex with CPHPC and cadmium ions provides higher resolution detail of the interaction than is observed with calcium ions.
Compared to wildtype C57BL/6 mice, we find that in Apcs-/- "SAP knock-out" mice, bleomycin induces a more persistent inflammatory response and increased fibrosis.
The effects of SAP and Xiapex (Collagenase Clostridium histolyticum) on fibrocytes derived from Dupuytren's disease, was evaluated.
plasma protein serum amyloid P binds to FcgammaRI (show FCGR1A ELISA Kits) on monocytes to inhibit fibrocyte differentiation, and binds to FcgammaRIIa on neutrophils to reduce neutrophil adhesion.
In the late phase post-myocardial infarct there is a coordinated decrease in immune response-inflammation proteins, except for SAP which showed an increase related to the specific activation of the classical complement pathway.
SAP deficiency mitigated foam cell formation and atherosclerotic development in apoE (show APOE ELISA Kits)(-/-) mice, due to reduction in macrophages recruitment, polarization and pro-inflammatory cytokines
observations suggest that serum amyloid P, at least in part, uses FcgammaRI (show FCGR1A ELISA Kits) and FcRgamma (show FCER1G ELISA Kits) to inhibit fibrocyte differentiation
Bglu3 is confirmed to be a locus affecting diabetes susceptibility, and Apcs is a probable candidate gene.
binding of SAP to ALD (show ABCD1 ELISA Kits)-DNA could switch macrophage phenotypic polarization from proinflammatory M2b to anti-inflammatory M2a via PI3K/Akt (show AKT1 ELISA Kits)-ERK (show EPHB2 ELISA Kits) signaling activation, thus exerting protective and therapeutic interventions on murine lupus nephritis
SAP has an effect on macrophages in fibrotic lung disease
sFRP4 (show SFRP4 ELISA Kits) negatively regulates bone formation without disrupting phosphorus homeostasis.
Binding of mouse and human SAP to immobilized influenza virus was compared. Mouse SAP bound much less avidly than human SAP.mouse SAP apparently plays no significant role during infection of mice with influenza virus.
Targeted pharmacological depletion of serum amyloid P component for treatment of amyloidosis
during murine tuberculosis (TB) SAP levels were increased; purified mouse SAP inhibited the intra-alveolar macrophage M. tuberculosis growth, in vitro; SAP may thus contribute both to the pathogenesis and pulmonary innate immunity in TB
The protein encoded by this gene is a glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization. These family members have considerable sequence homology which is thought to be the result of gene duplication. The binding of the encoded protein to proteins in the pathological amyloid cross-beta fold suggests its possible role as a chaperone. This protein is also thought to control the degradation of chromatin. It has been demonstrated that this protein binds to apoptotic cells at an early stage, which raises the possibility that it is involved in dealing with apoptotic cells in vivo.
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