OBJECTIVEThe changes in serum adipokines and cytokines related to oxidative stress were examined during 3 months 'Off to On' and 'On to Off' periods using negatively charged particle-dominant indoor air conditions (NCPDIAC).

METHODSSeven volunteers participated in the study, which included 'OFF to 3 months ON' periods (ON trials) for a total of 16 times, and 'ON to 3 months OFF' (OFF trials) periods for a total of 13 times.

RESULTSWith the exception of one case, serum amyloid A (SAA) levels decreased significantly during the ON trials.

CONCLUSIONConsidering that SAA is an acute phase reactive protein such as C reactive protein (CRP), this observed decrease might indicate the prevention of cardiovascular and atherosclerotic changes, since an increase in high-sensitive CRP is associated with the subsequent detection of these events.

Adult ; Air ; analysis ; Air Pollution, Indoor ; Environmental Monitoring ; Female ; Housing ; Humans ; Male ; Serum Amyloid A Protein ; metabolism

PURPOSE: The measuring Epstein-Barr virus (EBV) DNA is an important predictor of nasopharyngeal carcinoma (NPC). This study evaluated the predictive value of pretreatment serum amyloid A (SAA) and C-reactive protein (CRP) comparing with EBV DNA in patients with NPC. MATERIALS AND METHODS: In an observational study of 419 non-metastatic NPC patients, we prospectively evaluated the prognostic effects of pretreatment SAA, CRP, and EBV DNA on survival. The primary end-point was progress-free survival (PFS). RESULTS: The median level of SAA and CRP was 4.28 mg/L and 1.88 mg/L, respectively. For the high-SAA group (> 4.28 mg/L) versus the low-SAA (≤ 4.28 mg/L) group and the high-CRP group (> 1.88 mg/L) versus the low-CRP (≤ 1.88 mg/L) group, the 5-year PFS was 64.5% versus 73.1% (p=0.013) and 65.2% versus 73.3% (p=0.064), respectively. EBV DNA detection showed a superior predictive result, the 5-year PFS in the EBV DNA ≥ 1,500 copies/mL group was obviously different than the EBV DNA < 1,500 copies/mL group (62.2% versus 77.8%, p < 0.001). Multifactorial Cox regression analysis confirmed that in the PFS, the independent prognostic factors were including EBV DNA (hazard ratio [HR], 1.788; p=0.009), tumour stage (HR, 1.903; p=0.021), and node stage (HR, 1.498; p=0.049), but the SAA and CRP were not included in the independent prognostic factors. CONCLUSION: The results of SAA and CRP had a certain relationship with the prognosis of NPC, and the prognosis of patients with high level of SAA and CRP were poor. However, the predictive ability of SAA and CRP was lower than that of EBV DNA.
C-Reactive Protein* ; DNA* ; Herpesvirus 4, Human* ; Humans ; Observational Study ; Prognosis ; Prospective Studies* ; Serum Amyloid A Protein* ; Survival Analysis

OBJECTIVETo screen biomarkers which can be used as an auxiliary method in the diagnosis of Henoch-Schönlein purpura (HSP) and to evaluate their diagnostic values by receiver operating characteristic (ROC) curve analysis.

METHODSA total of 127 children diagnosed with HSP between April 2012 and March 2014 were included in the HSP group and an equal number of healthy children were included in the control group. Twelve parameters, i.e., serum amyloid protein A (SAA), interleukin-6 (IL-6), immunoglobulins (IgA, IgG, IgM, and IgE), C-reactive protein (CRP), white blood cell (WBC) count, complements C3 and C4, anti-streptolysin O, and ferritin, were analyzed. The values of the screened biomarkers for diagnosis of HSP were assessed by ROC curve analysis.

RESULTSThe HSP group had significantly higher levels of SAA, IL-6, CRP, WBC, IgA, and IgM than the control group (P<0.05). The areas under the ROC curve of SAA, IL-6, WBC, IgA, and IgM for the diagnosis of HSP were higher than 0.7 (P<0.05). The optimal cut-off values of SAA, IgA, IgM, WBC, and IL-6 for the diagnosis of HSP were 3.035 μg/mL, 1579.5 mg/L, 922.5 mg/L, 8.850 × 10⁹/L, and 7.035 pg/mL, respectively; the corresponding sensitivities of the optimal cut-off values for the diagnosis of HSP were 95.1%, 75.6%, 72.3%, 78.0%, and 63.4%, respectively, and the corresponding specificities were 90.2%, 85.4%, 82.4%, 70.7%, and 80.5%, respectively.

CONCLUSIONSSAA, IgA, IgM, WBC, and IL-6 are valuable biomarkers for clinical diagnosis of HSP and among them SAA seems to be the best one.

Adolescent ; Biomarkers ; blood ; C-Reactive Protein ; analysis ; Child ; Child, Preschool ; Female ; Humans ; Male ; Purpura, Schoenlein-Henoch ; blood ; diagnosis ; ROC Curve ; Serum Amyloid A Protein ; analysis

BACKGROUNDAlteration in the protein composition of high-density lipoprotein (HDL) has been proposed as a mechanism for the development of coronary heart disease (CHD). In HDL, an increase in serum amyloid A protein (SAA) accompanying the decrease in apolipoprotein A-I (apoA-I) has been found during the acute inflammation period. However, whether this phenomenon persists in CHD patients, a disease related to inflammation, is unknown. The purpose of the present study was to explore the relationship between SAA and apoA-I in HDL isolated from CHD patients.

METHODSOverall, 98 patients with confirmed stable CHD and 90 control subjects matched for age and gender were enrolled in this case-control study. Potassium bromide (KBr) density gradient ultracentrifugation was used to isolate HDL from plasma. The levels of SAA and apoA-I in the HDL samples were detected by enzyme-linked immunosorbent assay kits. Pearson's correlation and general linear models were used in the analysis.

RESULTSCompared with controls, patients with CHD had a significant decrease in the amount of apoA-I ((14.21 ± 8.44) µg/ml vs. (10.95 ± 5.95) µg/ml, P = 0.003) in HDL and a significant increase in the amount of log SAA (1.21 ± 0.46 vs. 1.51 ± 0.55, P < 0.00001). Differences were independent of age, body mass index (BMI), HDL cholesterol (HDL-C), and other factors. An independently and statistically significant positive correlation between log SAA and apoA-I in HDL was observed only in the CHD group (β = 2.0, P = 0.026). In the general linear model, changes in log(SAA), age, age2, gender, BMI and HDL-C could explain a statistically significant 43% of the variance in apoA-I.

CONCLUSIONSThis study provides direct evidence for the first time that there was an independent positive correlation between log SAA and apoA-I in the HDL of CHD patients, indicating the alteration of protein composition in HDL. However, the question of whether this alteration in HDL is associated with impairment of HDL functions requires further research.

Adult ; Aged ; Apolipoprotein A-I ; analysis ; Coronary Disease ; blood ; etiology ; Female ; Humans ; Lipoproteins, HDL ; analysis ; blood ; Male ; Middle Aged ; Serum Amyloid A Protein ; analysis

BACKGROUNDElevated levels of serum C-reactive protein (CRP) have been reported to have prognostic significance in lung cancer patients. This study aimed to further identify CRP-bound components as prognostic markers for lung cancer and validate their prognostic value.

METHODSCRP-bound components obtained from the serum samples from lung cancer patients or healthy controls were analyzed by differential proteomics analysis. CRP-bound serum amyloid A (CRP-SAA) was evaluated by co-immunoprecipitation (IP). Serum samples from two independent cohorts with lung cancer (retrospective cohort, 242 patients; prospective cohort, 222 patients) and healthy controls (159 subjects) were used to evaluate the prognostic value of CRP-SAA by enzyme-linked immunosorbent assay.

RESULTSCRP-SAA was identified specifically in serum samples from lung cancer patients by proteomic analysis. CRP binding to SAA was confirmed by co-IP in serum samples from lung cancer patients and cell culture media. The level of CRP-SAA was significantly higher in patients than in healthy controls (0.37 ± 0.58 vs. 0.03 ± 0.04, P < 0.001). Elevated CRP-SAA levels were significantly associated with severe clinical features of lung cancer. The elevation of CRP-SAA was associated with lower survival rates for both the retrospective (hazard ration [HR] = 2.181, 95% confidence interval [CI] = 1.641-2.897, P < 0.001) and the prospective cohorts (HR = 2.744, 95% CI = 1.810-4.161, P < 0.001). Multivariate Cox analysis showed that CRP-SAA was an independent prognostic marker for lung cancer. Remarkably, in stages I-II patients, only CRP-SAA, not total SAA or CRP, showed significant association with overall survival in two cohorts. Moreover, univariate and multivariate Cox analyses also showed that only CRP-SAA could be used as an independent prognostic marker for early-stage lung cancer patients.

CONCLUSIONCRP-SAA could be a better prognostic marker for lung cancer than total SAA or CRP, especially in early-stage patients.

Biomarkers ; C-Reactive Protein ; Enzyme-Linked Immunosorbent Assay ; Humans ; Lung Neoplasms ; Multivariate Analysis ; Prognosis ; Prospective Studies ; Proteomics ; Retrospective Studies ; Serum Amyloid A Protein

BACKGROUNDHigh-density lipoprotein cholesterol (HDL-C) levels are a strong, independent inverse predictor of coronary heart disease (CHD). In this cross-sectional study we investigated the interrelationships between HDL-C and HDL related factors apolipoprotein A-I (apoA-I) and serum amyloid A (SAA) and the presence and extent of CHD in a population of Chinese patients with CHD.

METHODSTwo hundred and twenty-four consecutive patients took part in this study. Demographic data were obtained from hospital records. Serum chemical concentrations were measured by standard laboratory methods.

RESULTSThe concentrations of high-sensitive C-reactive protein (hsCRP) (median: 1.85 mg/L) and SAA (median: 9.40 mg/L) were significantly higher in the CHD group (P < 0.05), while concentrations of HDL-C ((1.03 +/- 0.25) mmol/L) and apoA-I ((604.59 +/- 105.79) mmol/L) were significantly lower than those in the non-CHD group (P < 0.05). The concentrations of apoA-I decreased with the increase in vascular damage, but the difference did not reach statistical significance. However, the concentrations of hsCRP and SAA increased with the increase in vascular damage. The unadjusted odd ratios (ORs) (CI) for apoA-I and SAA of the presence of CHD were 0.093 (0.990 - 0.997) (P = 0.00) and 2.571 (1.029 - 6.424) (P < 0.05), respectively. The association between elevated SAA and the presence of CHD was lost after adjusting for lipid status parameter concentrations. The associations between apoA-I, SAA and the extent of CHD remained strong, regardless of confounding variables.

CONCLUSIONSIncreased concentrations of SAA represent the inflammatory marker of the extent of coronary stenosis in patients with CHD. In contrast to SAA, the level of apoA-I was also associated with the presence of CHD, indicating that apoA-I was not only a marker of CHD presence but also a quantitative indicator of CHD extent. In short, determining the change apolipoprotein content within HDL particle is a more accurate and effective method to evaluate the impact of HDL on CHD.

Adult ; Aged ; Apolipoprotein A-I ; blood ; Biomarkers ; Cholesterol, HDL ; blood ; Cholesterol, LDL ; blood ; Coronary Disease ; blood ; Cross-Sectional Studies ; Female ; Humans ; Male ; Middle Aged ; Serum Amyloid A Protein ; analysis

OBJECTIVETo determine the accuracy and clinical value of combining 64 multi-slice spiral computer tomography (MSCT) and serum amyloid A protein (SAA) in the preoperative staging of rectal cancer.

METHODSProspectively enrolled patients with rectal cancer from October 2007 to October 2008. The patients were randomly assigned into two groups: MSCT and SAA combined group: both MSCT and SAA combinative assessment were performed for preoperative evaluation; MSCT group: only MSCT was performed preoperatively for tumor staging. The accuracy of the preoperative T, N, M, and TNM staging and the concordance rate of predictive operative strategy were compared between the two groups.

RESULTSTotal of 225 cases with rectal cancer were enrolled in this study. There were 110 cases in MSCT and SAA combined group and 115 cases in MSCT group. The baseline characteristics was comparable between the two groups. For MSCT and SAA combined group, the accuracies of preoperative staging of T, N, M and TNM was 87.3%, 85.2%, 100% and 86.4%, respectively; and for MSCT group, the corresponding rates was 85.2%, 67.0%, 100% and 66.1%, respectively. Statistical differences was found in the accuracy of preoperative N and TNM staging between the two groups (P = 0.009 and 0.001, respectively). In addition, there was statistical difference in the accuracy of prediction to operative procedures between the two groups (94.7% vs. 81.7%, P = 0.003).

CONCLUSIONCombinative assessment of MSCT and SAA could improve the accuracy of preoperative staging, and thus provide higher predictive coincidence rate of operative procedures.

Adult ; Aged ; Female ; Humans ; Male ; Middle Aged ; Neoplasm Staging ; Preoperative Care ; Prospective Studies ; Rectal Neoplasms ; diagnosis ; surgery ; Serum Amyloid A Protein ; analysis ; Tomography, Spiral Computed ; methods

BACKGROUNDRheumatoid arthritis (RA) is an autoimmune disease characterized by chronic inflammation at the synovial membrane. Although great progress has been made recently in exploring the etiology and pathogenesis of RA, its molecular pathological mechanism remains to be further defined and it is still a great challenge in determining the diagnosis and in choosing the appropriate therapy in early patients. This study was performed to screen candidate RA-associated serum proteins by comparative proteomics to provide research clues to early diagnosis and treatment of RA.

METHODSSera isolated from 6 RA patients and 6 healthy volunteers were pooled respectively and high-abundance proteins were depleted by Plasma 7 Multiple Affinity Removal System. The protein expression profiles between the two groups were then compared by two-dimensional gel electrophoresis (2-DE) and the proteins over/under-expressed by more than 3-fold were identified by mass spectrometry analysis. To validate the differential expression levels of the identified proteins between the two groups, ELISA was performed in two of the identified proteins in individual sera from 32 RA patients and 32 volunteers.

RESULTSEight proteins which over/under-expressed in sera of RA patients were identified. Among them, chain A of transthyretin (TTR) was under-expressed, while serum amyloid A protein, apolipoprotein A (ApoA)-IV, ApoA-IV precursor, haptoglobin 2, ceruloplasmin (Cp), immunoglobulin superfamily 22 and HT016 were over-expressed. ELISA test confirmed that Cp expressed remarkably higher while TTR obviously lower in RA group compared with volunteer group.

CONCLUSIONThere were 8 identified proteins differentially expressed between RA group and volunteer group, which might be candidate RA-associated proteins and might be promising diagnostic indicators or therapeutic targets for RA.

Adult ; Apolipoproteins A ; blood ; Arthritis, Rheumatoid ; blood ; Blood Proteins ; analysis ; Ceruloplasmin ; analysis ; Electrophoresis, Gel, Two-Dimensional ; Enzyme-Linked Immunosorbent Assay ; Female ; Humans ; Male ; Middle Aged ; Prealbumin ; analysis ; Proteomics ; Serum Amyloid A Protein ; analysis

OBJECTIVETo identify serum diagnosis or progression biomarkers in patients with lung cancer using protein chip profiling analysis.

METHODProfiling analysis was performed on 450 sera collected from 213 patients with lung cancer, 19 with pneumonia, 16 with pulmonary tuberculosis, 65 with laryngeal carcinoma, 55 with laryngopharyngeal carcinoma patients, and 82 normal individuals. A new strategy was developed to identify the biomarkers on chip by trypsin pre-digestion.

RESULTSProfiling analysis demonstrated that an 11.6 kDa protein was significantly elevated in lung cancer patients, compared with the control groups (P < 0.001). The level and percentage of 11.6 kDa protein progressively increased with the clinical stages I-IV and were also higher in patients with squamous cell carcinoma than in other subtypes. This biomarker could be decreased after operation or chemotherapy. On the other hand, 11.6 kDa protein was also increased in 50% benign diseases of lung and 13% of other cancer controls. After trypsin pre-digestion, a set of new peptide biomarkers was noticed to appear only in the samples containing a 11.6 kDa peak. Further identification showed that 2177 Da was a fragment of serum amyloid A (SAA, MW 11.6 kDa). Two of the new peaks, 1550 Da and 1611 Da, were defined from the same protein by database searching. This result was further confirmed by partial purification of 11.6 kDa protein and MS analysis.

CONCLUSIONSAA is a useful biomarker to monitor the progression of lung cancer and can directly identify some biomarkers on chip.

Adenocarcinoma ; blood ; pathology ; Adult ; Aged ; Biomarkers, Tumor ; blood ; Carcinoma, Small Cell ; blood ; pathology ; Carcinoma, Squamous Cell ; blood ; pathology ; Female ; Humans ; Lung Neoplasms ; blood ; pathology ; Male ; Middle Aged ; Neoplasm Staging ; Peptides ; blood ; Protein Array Analysis ; Serum Amyloid A Protein ; analysis

Advancements in the field of proteomics have provided great opportunities for the development of diagnostic and therapeutic tools against human diseases. In this study, we analyzed haptoglobin and amyloid A protein levels of vivax malaria patients with combinations of depletion of the abundant plasma proteins, 2-dimensional gel electrophoresis (2-DE), image analysis, and mass spectrometry in the plasma between normal healthy donors and vivax malaria patients. The results showed that the expression level of haptoglobin had become significantly lower or undetectable in the plasma of vivax malaria patients due to proteolytic cleavage when compared to healthy donors on 2-DE gels. Meanwhile, serum amyloid A protein was significantly increased in vivax malaria patient's plasma with high statistical values. These 2 proteins are common acute phase reactants and further large scale evaluation with a larger number of patient's will be necessary to establish the possible clinical meaning of the existential changes of these proteins in vivax malaria patients. However, our proteomic analysis suggests the feasible values of some plasma proteins, such as haptoglobin and serum amyloid A, as associating factor candidates for vivax malaria.
Blood Proteins/analysis/diagnostic use ; Electrophoresis, Gel, Two-Dimensional ; Haptoglobins/analysis/diagnostic use/*metabolism ; Humans ; Malaria, Vivax/diagnosis/*metabolism/parasitology ; Plasmodium vivax/physiology ; Proteomics/*methods ; Serum Amyloid A Protein/analysis/diagnostic use/*metabolism