60 research outputs found

    ROC plot displaying the AUC of conventional CA15-3 (green), CA15-3<sup>MGL</sup> (purple) and CA15-3<sup>WGA</sup> (red) from metastatic breast cancer patients (n = 53) and healthy control (n = 20).

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    The 95% confidence intervals of the ROCs are depicted as shaded areas and displayed numerically in brackets. The color of shadings corresponds to the plotted lines and the overlap of conventional CA15-3 and CA15-3MGL is dark green, the overlap of all assays is brown and the overlap of CA15-3MGL and CA15-3WGA is dark red.</p

    CA15-3 levels of 19 patients who had a disease progression at the time of final plasma sampling and a previous reference plasma available while on study treatment (Reference).

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    A. Conventional CA15-3. Two patients with very high CA15-3 levels were excluded (Reference CA15-3 110.6 U/mL, Final 986.4 U/mL and Reference 1825.5 U/mL, Final 3909.7 U/mL) B. CA15-3MGL. C. CA15-3WGA. One patient with very high CA15-3WGA level was excluded (Reference CA15-3WGA 393.1 U/mL, Final CA15-3WGA 430.9 U/mL).</p

    Correlation of the conventional CA15-3 and CA15-3<sup>Lectin</sup> assays.

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    A: Scatterplot of baseline conventional CA15-3 levels and baseline CA15-3MGL levels in metastatic breast cancer patients. r = 0.68, pB: Enlargement of the scatterplot for the patients with the lowest CA15-3 levels for both conventional CA15-3 and CA15-3MGL. Very low baseline CA15-3MGL levels C: Scatterplot of baseline conventional CA15-3 levels and baseline CA15-3WGA levels in metastatic breast cancer patients. r = 0.90, pD: Enlargement of the scatterplot for the patients with conventional CA15-3 < 250 U/mL and CA15-3WGA < 130 U/mL, 85% of the study patients.</p

    Adjuvant radiotherapy-induced cardiac changes among patients with early breast cancer: a three-year follow-up study<sup>*</sup>

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    Background: In this study, we evaluate the evolution of cardiac changes during a three-year follow-up after adjuvant breast radiotherapy (RT). Methods: Sixty patients with left-sided and 20 patients with right-sided early stage breast cancer without chemotherapy were included in this prospective study. Echocardiography and cardiac biomarkers were evaluated before, immediately after and 3 years after RT. Radiation doses to cardiac structures were calculated. Results: In echocardiography, left ventricle (LV) systolic measurements had impaired at 3 years compared to baseline: the mean global longitudinal strain (GLS) worsened from –18 ± 3 to –17 ± 3 (p = .015), LV ejection fraction from 62 ± 5% to 60 ± 4% (p = .003) and the stroke volume from 73 ± 16 mL to 69 ± 15 mL (p = .015). LV diastolic function was also negatively affected: the isovolumetric relaxation time was prolonged (p = .006) and the first peak of diastole decreased (p = .022). Likewise, left atrial (LA) measurements impaired. These changes in echocardiography were more prominent in left-sided than in right-sided patients. The concurrent aromatase inhibitor (AI) use was associated with GLS impairment. In all patients, the N-terminal pro-brain natriuretic peptide (proBNP) values were median (interquartile range) 74 (41–125) ng/L at baseline, 75 (41–125) ng/L at the end of RT and 96 (56–162) ng/L at 3 years (p  Conclusion: During the 3-year follow-up after RT, negative subclinical changes in cardiac biomarkers and in LV systolic and diastolic function were observed. The measured changes were more pronounced in left-sided patients. In addition, AI use was associated with impaired cardiac systolic function.</p

    Lectin NPs binding to BC-associated CA15-3 from cell line ZR-75-1 (ATCC CRL-1500) using the lectin assay principle depicted in Fig 1.

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    The different lectin Eu+3-NPs used are shown on the x-axis and the y-axis displays the signal to background ratios using either biotinylated Ma695 (bioMa695) or biotinylated Ma552 (bioMa552) as the capture mAb.</p

    The principle of the conventional and in-house Eu<sup>+3</sup>-NP-based CA15-3 lectin assays.

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    In the conventional CA15-3 immunoassay, the capture and tracer mAbs bind to the protein and glycan epitopes of CA15-3. Alternatively, in the lectin assay, the CA15-3 is captured with mAbs and detected with lectins, which have been coated on the surface of Eu3+-NPs. This method allows multivalent binding of the tracer to the glycan moieties of BC-CA15-3.</p
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