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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: Previous studies have indicated that heparanase (Hpa) might represent a candidate universal tumor-associated antigen.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.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: Previous studies have indicated that heparanase (Hpa) might represent a candidate universal tumor-associated antigen.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.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