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Purpose To study the relationship between exposure to airborne particles in a pulp and paper mill and markers of inflammation and coagulation in blood. Methods Personal sampling of inhalable dust was performed for 72 subjects working in a Swedish pulp and paper mill. Stationary measurements were used to study concentrations of total dust, respirable dust, PM 10 and PM 2.5 , the particle surface area and the particle number concentrations. Markers of inflammation, interleukins (IL-1b, IL-6, IL-8, and IL-10), C-reactive protein (CRP), serum amyloid A (SAA), and fibrinogen and markers of coagulation factor VIII, von Willebrand, plasminogen activator inhibitor, and D-dimer were measured in plasma or serum. Sampling was performed on the last day of the work free period of 5 days, before and after the shift the first day of work and after the shifts the second and third day. In a mixed model analysis, the relationship between particulate exposures and inflammatory markers was determined. Sex, age, smoking, and BMI were included as covariates. Results The average 8-h time-weighted average (TWA) air concentration levels of inhalable dust were 0.30 mg/m 3 , range 0.005–3.3 mg/m 3 . The proxies for average 8-h TWAs of respirable dust were 0.045 mg/m 3 . Significant and consistent positive relations were found between several exposure metrics (PM 10, total and inhalable dust) and CRP, SAA and fibrinogen taken post-shift, suggesting a dose–effect relationship. Conclusion This study supports a relationship between occupational particle exposure and established inflammatory markers, which may indicate an increased risk of cardiovascular disease.

Extracellularly released molecular inflammasome assemblies -ASC specks- cross-seed Aβ amyloid in Alzheimer’s disease. Here we show that ASC governs the extent of inflammation-induced amyloid A (AA) amyloidosis, a systemic disease caused by the aggregation and peripheral deposition of the acute-phase reactant serum amyloid A (SAA) in chronic inflammatory conditions. Using super-resolution microscopy, we found that ASC colocalized tightly with SAA in human AA amyloidosis. Recombinant ASC specks accelerated SAA fibril formation and mass spectrometry after limited proteolysis showed that ASC interacts with SAA via its pyrin domain (PYD). In a murine model of inflammatory AA amyloidosis, splenic amyloid load was conspicuously decreased in Pycard −/− mice which lack ASC. Treatment with anti-ASC PYD antibodies decreased amyloid loads in wild-type mice suffering from AA amyloidosis. The prevalence of natural anti-ASC IgG (−logEC 50  ≥ 2) in 19,334 hospital patients was <0.01%, suggesting that anti-ASC antibody treatment modalities would not be confounded by natural autoimmunity. These findings expand the role played by ASC and IL-1 independent inflammasome employments to extraneural proteinopathies and suggest that anti-ASC immunotherapy may contribute to resolving such diseases. Synopsis ASC scaffolds and cross-seeds Aβ amyloid and is considered an actionable target against Alzheimer’s disease. This study investigated the role of ASC in amyloid A (AA) amyloidosis, a systemic disease in which serum amyloid A (SAA) aggregates invade internal organs due to chronic inflammation. ASC and SAA were found to colocalize in inflammatory amyloidosis in humans and mice. ASC interacts with SAA via its pyrin domain (PYD) and was found to accelerate SAA/AA fibril formation in a dose-dependent manner. Ablation of Pycard ( Asc ) was found to reduce amyloid deposition in mice. Immunotherapy with an anti-ASC antibody targeting the PYD diminished SAA-derived amyloid deposition and its sequelae in vivo. A large-scale human anti-ASC autoantibody screening of 23,450 plasma samples from 19,334 patients revealed rare immunoreactivity towards ASC, indicating high tolerance for employing anti-ASC modalities in inflammatory diseases. ASC scaffolds and cross-seeds Aβ amyloid and is considered an actionable target against Alzheimer’s disease. This study investigated the role of ASC in amyloid A (AA) amyloidosis, a systemic disease in which serum amyloid A (SAA) aggregates invade internal organs due to chronic inflammation.

Pseudoexfoliation syndrome (PE), which is often unilateral in 60% of cases, is a risk for exfoliation glaucoma (EXG) with elevated inflammatory cytokines. This study aimed to clarify the dynamics of these cytokines in unilateral PE (u-PE) patients. This study included 20 eyes from 10 u-PE patients (PE+ eyes and fellow PE− eyes) and 20 eyes from 10 cataract patients without PE (control group). Clinical parameters, including age, visual acuity, and intraocular pressure, were assessed. Anterior chamber aqueous humor cytokine levels (IL-8, SAA, ET-1, VEGF) were measured and compared among groups. SAA was elevated in PE+ eyes compared to PE− and control eyes. IL-8 and ET-1 were elevated in both PE+ and PE− eyes compared to controls. IL-8 was associated with worsening visual acuity, while ET-1 correlated inversely. Our findings suggest that SAA is associated with the manifest disease while IL-8 and ET-1 could be early biomarkers for PE and therapeutic targets to prevent glaucomatous damage, as these markers appear in the aqueous humor even before pseudoexfoliation material becomes clinically evident. These results may enable earlier diagnosis and therapeutic intervention before the clinical onset of PE in patients with risk factors.

Objective To evaluate the impact of Human Immunodeficiency Virus (HIV) infection on serum amyloid A (SAA) levels in acute pulmonary infections and assess correlations between SAA and other inflammatory markers in HIV-associated pneumonia. Methods In this retrospective case-control study, 48 HIV-positive patients with pulmonary infections (HIV group) and 55 age-matched HIV-negative controls (control group) were enrolled from Shanghai Public Health Clinical Center (2021.5–2025.5). Demographic, hospitalization duration and laboratory parameters - including SAA, white blood cell count (WBC), C-reactive protein (CRP), procalcitonin (PCT), lactate dehydrogenase (LDH), platelet count (PLT), CD4 + T cell count, and absolute lymphocyte count(ALC) - were systematically collected from both patient cohorts. For intergroup comparisons, the Mann-Whitney U test was employed, while Spearman’s rank correlation analysis was conducted to assess biomarker associations within the HIV-positive subgroup. Results Among 103 patients, the HIV group had higher male predominance (83.3% vs. 54.5%, P  = 0.02) and lower CD4 + T cell count (215.17 vs. 443.41 cells/µL, P  < 0.05). SAA (178.39 vs. 122.93 mg/L, P  = 0.032), CRP (64.27 vs. 37.07 mg/L, P  = 0.031), LDH (310.65 vs. 235.96 U/L, P  = 0.024), and hospitalization duration (16.83 vs. 13.05 days, P  = 0.013) were significantly elevated in HIV patients. SAA correlated positively with CRP ( r  = 0.4807), PCT ( r  = 0.3554), LDH ( r  = 0.3564), and PLT ( r  = 0.3094) ( P  < 0.05 for all). Conclusions Patients with HIV-associated pulmonary infections exhibited significantly elevated levels of SAA, CRP, and LDH, along with prolonged hospital stays, compared to non-HIV-infected individuals. These findings suggest that HIV infection amplifies systemic inflammatory responses, potentially contributing to extended hospitalization. The robust correlations between SAA and other biomarkers (including CRP, PCT, LDH, PLT) highlight its potential as a key component in early diagnostic panels for HIV-associated pulmonary infections.

Inflammatory bowel disease (IBD) and primary sclerosing cholangitis (PSC) are chronic immune-mediated inflammatory diseases (IMIDs) that affect the gastrointestinal and hepatobiliary systems. They are characterized by persistent inflammation, potentially progressive fibrosis, and an elevated risk of developing cholangiocarcinoma and colorectal cancer. IBD and PSC share phenotypical, genetic, and immunological features, largely due to the central role of immune cell dysregulation. Despite their increasing global prevalence, the underlying drivers remain poorly understood, and effective treatment options are still lacking. Efforts towards an improved comprehension of their pathogenic mechanisms are therefore pivotal. Emerging evidence highlights the role of canonical ASC-dependent inflammasomes—multiprotein bioactive Interleukin (IL)-1-producing complexes of the innate immune system—and serum amyloid A (SAA) as key structures of gastrointestinal and hepatobiliary inflammation, tissue remodeling, stromal crosstalk, and fibrosis. In this review, we explore immunological connections and analogies between IBD and PSC, highlighting the converging roles of canonical ASC-dependent inflammasomes, the IL-1 superfamily, SAA, and sustained gut microbiota-driven chronic inflammation in disease pathology and their surging potential as therapeutic targets across the gut–liver axis.

Background: Chimeric antigen receptor (CAR) T-cell therapy has revolutionized treatment of relapsed/refractory large B-cell lymphoma (LBCL), but its administration is often complicated by cytokine release syndrome (CRS). Interleukin-6 (IL-6) is widely used to monitor CRS, though its clinical value diminishes after tocilizumab administration. We aimed to evaluate serum amyloid A (SAA), a dynamic acute-phase reactant, as a treatment-independent biomarker of inflammation and toxicity in CAR-T recipients. Methods: This retrospective study included 43 adults with LBCL treated with axicabtagene ciloleucel. SAA and other inflammatory markers were assessed from lymphodepletion through day +11 post-infusion. CRS and ICANS were graded per ASTCT criteria. Statistical analyses included Mann–Whitney U tests, Spearman’s correlation, and ROC curve analysis to evaluate predictive performance. Results: SAA levels peaked at day +4 and normalized by day +11, displaying wave-like kinetics. Levels were significantly higher in patients with any-grade CRS at early timepoints but showed no association with ICANS. SAA correlated strongly with CRP, suPAR, sST2, fibrinogen, ferritin, procalcitonin, and IL-6. Compared to IL-6, SAA was more predictive of CRS at day +2 and +4, and unaffected by tocilizumab. Baseline SAA also correlated with the mEASIX score, suggesting linkage to endothelial stress. Non-responders at 3-month PET had higher baseline SAA than responders (196.0 vs. 17.7 mg/L, p = 0.036), with ROC analysis yielding an AUC of 0.74 and an optimal threshold of 79.8 mg/L. Conclusions: SAA is a robust and dynamic marker of systemic inflammation, with potential utility in both toxicity monitoring and response prediction in the CAR-T setting. Its independence from IL-6 modulation positions it as a promising biomarker for future integration into clinical algorithms.

Background and aimsThe relationship between serum amyloid A (SAA) and coronary heart disease (CHD) remains inconsistent, and the correlation of SAA levels and some factors have not been thoroughly evaluated in CHD. The present study assessed the associations of SAA levels and CHD, and the correlation of SAA levels and CRP, fibrinogen, interleukin-6 (IL-6), and HDL-C levels in CHD patient.MethodsWe systematically searched databases of Cochrane Library, PubMed, Embase, and ScienceDirect from their inception to 2018. Pooled standardized mean difference (SMD), correlation coefficient (r), and 95% confidence intervals (CI) were computed using random-effect model.ResultA total of 26 studies were identified for analysis, involving a total of 6466 CHD cases and 16,184 participants. Compared with the control group, the case group had markedly higher SAA levels (SMD = 0.38, 95% CI 0.21, 0.56). Subgroup analysis manifested that SAA level difference between case group and control group were associated with age, continent, and study type. Moreover, meta-regression model suggested that different continent, sex, and publication year can explain the origin of 52.05%, 50.17%, 28.07% heterogeneity, respectively. By stratified analyses, we further found that the concentration of SAA increased gradually with the aggravation of CHD. Additionally, the meta-analysis of correlation showed that SAA levels were positively related with CRP (r = 0.45, 95% CI 0.19, 0.71), fibrinogen (r = 0.41, 95% CI 0.35, 0.47), and IL-6 (r = 0.48, 95% CI 0.41, 0.54) levels, but negatively linked with HDL-C levels (r = − 0.28, 95% CI − 0.38, − 0.18) in CHD patients.ConclusionHigh levels of SAA are significantly associated with increased risk of CHD, especially for participants aged more than 55 years, subjects from Europe and Asia, or case–control study. Furthermore, we find that SAA concentrations increased with the severity of CHD. Importantly, our study suggests that high levels of SAA might play a role in CHD by increasing CRP, fibrinogen, IL-6 levels, or attenuating HDL-C levels.

Serum amyloid A (SAA) proteins belong to a family of acute-phase reactants, playing an integral role in defending the organism from pathological damage. Despite a wealth of data on the regulation of SAA transcripts in teleosts, there is only limited information on these proteins’ abundance in fish. The aim of this study is to characterise SAA protein levels in salmonids using a newly developed antibody specific to salmonid SAA. The salmonid SAA antibody detected SAA and accurately discriminated between stimulated and control specimens from rainbow trout macrophage cell line (RTS-11) in vitro, as well as rainbow trout challenged with Aeromonas salmonicida- or flagellin-stimulated Atlantic salmon in vivo. The presence of SAA protein was analysed in RTS-11 cell line supernatants, liver, and spleen samples using ELISA, immunoblotting, and immunohistochemistry. This study is the first to characterise SAA protein levels in salmonids in vivo and in vitro. The newly developed salmonid SAA antibody was able to discriminate between stimulated and unstimulated specimens, showing that it can be used to study the acute-phase response in salmonids with the potential to be further developed into assays to monitor and evaluate health in wild and farmed fish.

ABSTRACT Background Bordetella bronchiseptica is an essential bacterial pathogen characterized by chronic respiratory disease in dogs known as Kennel cough. The presence of causative antibodies in animals can also be detected by lipopolysaccharide antigen‐based enzyme linked immunosorbent assay (ELISA). In recent years, it has been determined that there is a significant relationship between acute phase proteins and diseases, and disease follow‐up can be done within the framework of this relationship. Methods In this study, blood sera from 150 dogs in an animal shelter in Van province were evaluated for B. bronchiseptica by the homemade ELISA method, and their correlations with serum amyloid A (SAA) were investigated. Blood serum samples were analysed for antibodies against B. bronchiseptica using a homemade ELISA method. Positive animals were also molecularly confirmed using nasal swabs by PCR. A commercial ELISA kit determined SAA levels in blood sera. Results Eighteen (12%) of the analysed blood serum samples were found positive by the homemade ELISA method. SAA concentrations in the positive blood sera were elevated from 12.7 to ≤38.98 mg/L. SAA concentrations in blood sera serologically positive for B. bronchiseptica were statistically significant. Conclusions In this study, in which the relationship between SAA concentration and B. bronchiseptica was investigated for the first time in Turkey, it was concluded that SAA concentration analysis may help diagnose and monitor the disease. In addition, the presence and prevalence of this critical and zoonotic agent causing chronic respiratory tract disease in dogs in Van province was revealed for the first time in this study. A study in Van, Turkey examined Bordetella bronchiseptica in shelter dogs using ELISA and PCR. Overall, 12% of blood samples tested positive. Serum amyloid A (SAA) levels were significantly elevated in positive cases, suggesting SAA could be a useful diagnostic marker for this chronic respiratory disease‐causing bacterial pathogen.

Serum amyloid A (SAA) is one of the most abundant acute-phase response proteins and has been extensively studied in vertebrates for its role in modulation of the inflammatory response and as a marker of disease diagnosis. By comparison, SAA is rarely identified in aquatic species and its physical functions are also not well studied. The present study identified the only one gene encoding SAA protein in oyster Crassostrea gigas. The open reading frame (ORF) of CgSAA was of 417 bp, encoding a putative polypeptide of 138 amino acid residues with a predicted molecular weight of 15.66 kDa. CgSAA was composed of a signal peptide (residues 1–22) and a conserved SAA domain (residues 36–138). The mRNA expression of CgSAA in normal individuals was detectable but at a low level, with the lowest expression level in the tissue of labial palp and a slightly higher expression level in hemocytes. The mRNA expression level of CgSAA was significantly up-regulated at 6 h (2.76-fold of that in control group, p < 0.01) post V. splendidus stimulation. It was also significantly induced under environmental stress at high temperature (34 °C) or low salinity (15‰ salinity). The recombinant protein rCgSAA was expressed in Escherichia coli and purified by affinity chromatography. After rCgSAA was injected into oysters or incubated with culture primary hemocytes, the mRNA expressions of the cytokines CgIL17-1, CgIL17-5, and CgTNF were all significantly up-regulated. The results collectively suggested that CgSAA, as a conserved acute-phase response protein in oyster, was quickly induced under environmental stress and promoted the expressions of cytokines, which provide fresh ideas for understanding the roles of SAA proteins in aquatic invertebrates.