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In vitro and ex vivo evaluation of a multi-epitope heparinase vaccine for various malignancies.

Tang XD, Guo SL, Wang GZ, Li N, Wu YY, Fang DC, Fan YH, Yang SM - Cancer Sci. (2013)

Bottom Line: The results showed that multi-epitope vaccines Hpa525 + 277 + 405 + 16 and Hpa8 + 310 + 315 + 363 induced higher Hpa-specific lysis of various cancer cells from different tissues in a HLA-A2-restricted and heparanase-specific manner compared with the single epitope vaccines Hpa525, Hpa277, Hpa405, Hpa16, Hpa8, Hpa310, Hpa315 and Hpa363, both in vitro and ex vivo.However, these heparanase-specific CTL did not lyse heparanase-expressing autologous lymphocytes and dendritic cells, which confirms the safety of these multi-epitope vaccines.Therefore, the present study provides theoretical evidence for the use of heparanase multi-epitope vaccines for clinical application.

View Article: PubMed Central - PubMed

Affiliation: Department of Gastroenterology, Xinqiao Hospital, Third Military Medical University, Chongqing, China; Department of Respiratory and Critical Care Medicine, The First Affiliated Hospital, Chongqing Medical University, Chongqing, China.

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Analysis of the HLA-A2-binding affinity of epitopes derived from human heparanase. (a, b) Fluorescence index (FI) of human heparanase-derived peptides binding to HLA-A2. NP, negative peptide control; PP, positive peptide control.
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fig01: Analysis of the HLA-A2-binding affinity of epitopes derived from human heparanase. (a, b) Fluorescence index (FI) of human heparanase-derived peptides binding to HLA-A2. NP, negative peptide control; PP, positive peptide control.

Mentions: As shown in Figure1, we found that all epitopes from human heparanase upregulated the expression of HLA-A2 on T2 cells except Hpa(184-192)(LIFGLNALL). Expression of the peptides increased the expression of HLA-A2 molecules on T2 cells in a dose-dependent manner. When the concentration of peptides reached 40 μmol/L, the relative binding affinity exceeded 1.5 (Fig.1). These results indicate that the human heparanase epitopes could bind to HLA-A2 molecules on T2 cells.


In vitro and ex vivo evaluation of a multi-epitope heparinase vaccine for various malignancies.

Tang XD, Guo SL, Wang GZ, Li N, Wu YY, Fang DC, Fan YH, Yang SM - Cancer Sci. (2013)

Analysis of the HLA-A2-binding affinity of epitopes derived from human heparanase. (a, b) Fluorescence index (FI) of human heparanase-derived peptides binding to HLA-A2. NP, negative peptide control; PP, positive peptide control.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4317872&req=5

fig01: Analysis of the HLA-A2-binding affinity of epitopes derived from human heparanase. (a, b) Fluorescence index (FI) of human heparanase-derived peptides binding to HLA-A2. NP, negative peptide control; PP, positive peptide control.
Mentions: As shown in Figure1, we found that all epitopes from human heparanase upregulated the expression of HLA-A2 on T2 cells except Hpa(184-192)(LIFGLNALL). Expression of the peptides increased the expression of HLA-A2 molecules on T2 cells in a dose-dependent manner. When the concentration of peptides reached 40 μmol/L, the relative binding affinity exceeded 1.5 (Fig.1). These results indicate that the human heparanase epitopes could bind to HLA-A2 molecules on T2 cells.

Bottom Line: The results showed that multi-epitope vaccines Hpa525 + 277 + 405 + 16 and Hpa8 + 310 + 315 + 363 induced higher Hpa-specific lysis of various cancer cells from different tissues in a HLA-A2-restricted and heparanase-specific manner compared with the single epitope vaccines Hpa525, Hpa277, Hpa405, Hpa16, Hpa8, Hpa310, Hpa315 and Hpa363, both in vitro and ex vivo.However, these heparanase-specific CTL did not lyse heparanase-expressing autologous lymphocytes and dendritic cells, which confirms the safety of these multi-epitope vaccines.Therefore, the present study provides theoretical evidence for the use of heparanase multi-epitope vaccines for clinical application.

View Article: PubMed Central - PubMed

Affiliation: Department of Gastroenterology, Xinqiao Hospital, Third Military Medical University, Chongqing, China; Department of Respiratory and Critical Care Medicine, The First Affiliated Hospital, Chongqing Medical University, Chongqing, China.

Show MeSH
Related in: MedlinePlus