Discrimination of delays of reinforcement in aversive conditioning.

<p>(a) The protein level changes of CA125 and LRG1 were confirmed in the larger sample set 2. (b) Marker distributions for the EOC patients with different histological subtypes.</p

Autoantibodies to TP53 discriminate breast cancer sera from control sera.

<p>ROC curves showing the 43 HRN cases (black) and the 28 TN subset (blue) vs. 87 matched healthy controls.</p

Selection of 15 analytes and their sensitivity/specificity as serum markers.

<p>Data from 43 cases and 87 controls. Marker selection criteria: (1) serum marker potential in high-grade serous ovarian cancer and involvement in breast cancer; (2) transcript involved in breast cancer; (3) association with poor breast cancer outcome; (4) protein decreased in breast cancer tissue compared to normal breast.</p><p>Selection of 15 analytes and their sensitivity/specificity as serum markers.</p

Validation of LRG1 as a Potential Biomarker for Detection of Epithelial Ovarian Cancer by a Blinded Study

<div><p>Background</p><p>Leucine-rich alpha-2-glycoprotein (LRG1) was found to be differentially expressed in sera from patients with Epithelial Ovarian Cancer (EOC). The aim of this study is to investigate the performance of LRG1 for detection of EOC, including early stage EOC, and to evaluate if LRG1 can complement CA125 in order to improve EOC detection using two independent blinded sample sets.</p><p>Methods and Results</p><p>Serum LRG1 and CA125 were measured by immunoassays. All assays were performed blinded to clinical data. Using the two independent sample sets (156 participants for sample set 1, and 233 for sample set 2), LRG1 was differentially expressed in EOC cases as compared to healthy, surgical, and benign controls, and its performance was not affected by the conditions of blood collection. The areas under the ROC curve (AUC) for LRG1 in differentiating EOC cases from non-cases were 0.797 and 0.786 for sample set 1 and 2. For differentiating EOC cases from healthy controls, the AUC values for LRG1 were 0.792 and 0.794. At a fixed specificity of 95%, LRG1 detects 52%, and 53.5% of EOC cases from healthy controls for sample set 1 and 2. When combining LRG1 and CA125, the AUC value increased to 0.927, which was improved compared to CA125 (AUC=0.916) (<i>p</i>=0.008) alone in distinguishing EOC cases from non-cases. More importantly, LRG1 also showed potential performance in differentiating early stage EOC from non-cases with an AUC of 0.715 for sample set 1, and 0.690 for sample set 2. The combination of LRG1 and CA125 resulted in an AUC of 0.838, which outperforms CA125 (AUC=0.785) (<i>p</i>=0.018) in detecting early stage EOC cases from non-cases using the larger sample set.</p><p>Conclusions</p><p>LRG1 could be a useful biomarker alone or in combination with CA125 for the diagnosis of ovarian cancer.</p></div

ROC curves comparing marker concentrations in cases to non-cases for sample set 1.

<p>(a) ROC analyses for CA125 and LRG1 to differentiate EOC from non-cases. (b) ROC analyses for CA125 and LRG1 to differentiate early stage EOC from non-cases.</p

ROC curves comparing marker concentrations in cases to healthy controls for sample set 1.

<p>(a) ROC analyses for CA125 and LRG1 to differentiate EOC from healthy controls. (b) ROC analyses for CA125 and LRG1 to differentiate early stage EOC from healthy controls.</p

Multimarker panel analysis.

<p>The performance of multimarker panels in distinguishing EOC/ early stage EOC from non-cases using sample set 1and sample set 2.</p

Use of cancer-specific yeast-secreted biotinylated recombinant antibodies for serum biomarker discovery-4

bound to case-pool serum. The enriched yeast-display scFv were labeled with anti-c-myc mAb and 25 μg/ml (A,B,E,F) or 100 μg/ml (C,D,G,H) of biotinylated case (A,C,E,G) or control (B,D,F,H) serum pools, before (A-D) or after depletion by magnetic sorting (E-H). Binding signals were detected as shown with the secondary antibody 488-alexa anti-mouse Ig (488 anti-mIg) and PE-labeled streptavidin (SA-PE).<p><b>Copyright information:</b></p><p>Taken from "Use of cancer-specific yeast-secreted biotinylated recombinant antibodies for serum biomarker discovery"</p><p>http://www.translational-medicine.com/content/6/1/41</p><p>Journal of Translational Medicine 2008;6():41-41.</p><p>Published online 24 Jul 2008</p><p>PMCID:PMC2503970.</p><p></p

Use of cancer-specific yeast-secreted biotinylated recombinant antibodies for serum biomarker discovery-1

Trophoresis before (lanes 1,3) or after (lanes 2,4) depletion for abundant proteins by cibacron blue and detected by coomassie blue straining. B-C: Control- and ovarian cancer-pool serum depleted for abundant sequences were immunoprecipitated with biobodies selected for specific binding to case-pool serum. The products of elution from control sera (B lane 2, and C) and ovarian cancer (B lane 1, and D) were separated by 1-D (B) or 2-D (C,D) protein electrophoresis and detected by silver staining. In the 2-D gels, the immunoprecipitates were focused over a pH3 to pH10 range and run on a 10% acrylamide gel. The circle indicates the region where PEBP1 was found in patient serum (D) but not in control serum (C).<p><b>Copyright information:</b></p><p>Taken from "Use of cancer-specific yeast-secreted biotinylated recombinant antibodies for serum biomarker discovery"</p><p>http://www.translational-medicine.com/content/6/1/41</p><p>Journal of Translational Medicine 2008;6():41-41.</p><p>Published online 24 Jul 2008</p><p>PMCID:PMC2503970.</p><p></p

Use of cancer-specific yeast-secreted biotinylated recombinant antibodies for serum biomarker discovery-2

endometrioid origin (as shown) were diluted in binding buffer, coated on plastic wells, and detected with polyclonal antibodies made to the center (pAb, white bars) or N-terminal (pAb, gray bars) region of PEBP1 or with a pAb made to the whole recombinant protein (black bars). Samples were tested in triplicates. Averages are shown. Wells coated with binding buffer were used as negative controls.<p><b>Copyright information:</b></p><p>Taken from "Use of cancer-specific yeast-secreted biotinylated recombinant antibodies for serum biomarker discovery"</p><p>http://www.translational-medicine.com/content/6/1/41</p><p>Journal of Translational Medicine 2008;6():41-41.</p><p>Published online 24 Jul 2008</p><p>PMCID:PMC2503970.</p><p></p