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- Bulten, W, et al.
(author)
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Artificial intelligence for diagnosis and Gleason grading of prostate cancer: the PANDA challenge
- 2022
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In: Nature medicine. - : Springer Science and Business Media LLC. - 1546-170X .- 1078-8956. ; 28:1, s. 154-
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Journal article (peer-reviewed)abstract
- Artificial intelligence (AI) has shown promise for diagnosing prostate cancer in biopsies. However, results have been limited to individual studies, lacking validation in multinational settings. Competitions have been shown to be accelerators for medical imaging innovations, but their impact is hindered by lack of reproducibility and independent validation. With this in mind, we organized the PANDA challenge—the largest histopathology competition to date, joined by 1,290 developers—to catalyze development of reproducible AI algorithms for Gleason grading using 10,616 digitized prostate biopsies. We validated that a diverse set of submitted algorithms reached pathologist-level performance on independent cross-continental cohorts, fully blinded to the algorithm developers. On United States and European external validation sets, the algorithms achieved agreements of 0.862 (quadratically weighted κ, 95% confidence interval (CI), 0.840–0.884) and 0.868 (95% CI, 0.835–0.900) with expert uropathologists. Successful generalization across different patient populations, laboratories and reference standards, achieved by a variety of algorithmic approaches, warrants evaluating AI-based Gleason grading in prospective clinical trials.
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- Suutari, T. J., et al.
(author)
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IgE cross reactivity between reindeer and bovine milk beta-lactoglobulins in cow's milk allergic patients
- 2006
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In: J Investig Allergol Clin Immunol. - 1018-9068. ; 16:5, s. 296-302
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Journal article (peer-reviewed)abstract
- BACKGROUND: Allergic reactions to cow's milk are common in small children. One of the main protein allergens found in cow's milk is beta-lactoglobulin (beta-Lg). Reindeer and bovine milk both contain related beta-Lg proteins, but the allergenicity of reindeer beta-Lg has not previously been studied. The purpose of this study was to analyze the immunological cross-reactivity of IgE antibodies from children with cow's milk allergy to reindeer and bovine beta-Lg. METHODS: Sera from 17 children and a serum pool of 4 patients with elevated cow's milk-specific IgE were investigated. Beta-Lg from bovine and reindeer milk was isolated in native form and an enzyme-linked immunosorbent inhibition assay was developed. Bovine beta-Lg was used as a capturing antigen and the inhibiting effects of reindeer and bovine beta-Lg on the IgE binding were measured. RESULTS: Cross-reactivity patterns of bovine milk beta-Lg specific IgE to reindeer beta-Lg varied among patients. In general, reindeer beta-Lg showed significantly lower inhibition (mean 43%) of IgE binding to the capturing antigen than did bovine beta-Lg (mean 89%). In some patients, even high concentrations of reindeer beta-Lg only partly eliminated the IgE binding to bovine beta-Lg. CONCLUSIONS: The partial cross-reactivity of human anti-bovine IgE with reindeer beta-Lg suggests that it lacks important bovine epitopes and those that are recognized are only weakly bound.
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| 8. |
- Suutari, T.J., et al.
(author)
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IgE cross reactivity between reindeer and bovine milk ?-lactoglobulins in cow's milk allergic patients
- 2006
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In: Journal of investigational allergology & clinical immunology. - 1018-9068 .- 1698-0808. ; 16:5, s. 296-302
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Journal article (peer-reviewed)abstract
- Background: Allergic reactions to cow's milk are common in small children. One of the main protein allergens found in cow's milk is ?-lactoglobulin (?-Lg). Reindeer and bovine milk both contain related ?-Lg proteins, but the allergenicity of reindeer ?-Lg has not previously been studied. The purpose of this study was to analyze the immunological cross-reactivity of IgE antibodies from children with cow's milk allergy to reindeer and bovine ?-Lg. Methods: Sera from 17 children and a serum pool of 4 patients with elevated cow's milk-specific IgE were investigated. ?-Lg from bovine and reindeer milk was isolated in native form and an enzyme-linked immunosorbent inhibition assay was developed. Bovine ?-Lg was used as a capturing antigen and the inhibiting effects of reindeer and bovine ?-Lg on the IgE binding were measured. Results: Cross-reactivity patterns of bovine milk ?-Lg specific IgE to reindeer ?-Lg varied among patients. In general, reindeer ?-Lg showed significantly lower inhibition (mean 43%) of IgE binding to the capturing antigen than did bovine ?-Lg (mean 89%). In some patients, even high concentrations of reindeer ?-Lg only partly eliminated the IgE binding to bovine ?-Lg. Conclusions: The partial cross-reactivity of human anti-bovine IgE with reindeer ?-Lg suggests that it lacks important bovine epitopes and those that are recognized are only weakly bound. © 2006 Esmon Publicidad.
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