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4. Additional file 4: of (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling

Author

An-Dong Liu, Xu, Hui, Gao, Ya-Nan, Luo, Dan-Ni, Li, Zhao-Feng, Voss, Courtney, Li, Shawn, and Cao, Xuan

Abstract

Figure S2. (Arg)9-GST SH2 TrM could effectively capture diverse pY proteins in A375 and A375/DDP cells. Levels of pY proteins from A375(a) and A375/DDP(b) cells stimulated with or without EGF (100 ng/ml) were assessed with Anti-pY antibody. The whole cell lysates were incubated with (Arg)9-GST, (Arg)9-GST SH2 Wt or (Arg)9-GST SH2 TrM for 12 h at 4 °C and purified by an appropriate amount of glutathione agarose. Data shown are representative of three independent experiments. (PPTX 107 kb)

Published
2018
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5. Additional file 9: of (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling

Author

An-Dong Liu, Xu, Hui, Gao, Ya-Nan, Luo, Dan-Ni, Li, Zhao-Feng, Voss, Courtney, Li, Shawn, and Cao, Xuan

Abstract

Figure S7. The toxicity effect of (Arg)9-GST SH2 TrM on PBMCs. (Arg)9-GST-SH2 TrM protein resulted in some toxicity effect on PBMCs according to the CCK-8 data, but the effect was moderate as (Arg)9-GST-SH2 TrM protein only specifically recognizing and binding to pY residue, which is low abundance in PBMCs. Cells were treated with different GST-fused proteins at different concentrations (a) (0.5, 1, 2, 4 and 8 μM) for various time (b) (1,2,4 and 8 h) and cell viability was measured by CCK-8 assay (n = 3, *P

Published
2018
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6. Additional file 3: of (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling

Author

An-Dong Liu, Xu, Hui, Gao, Ya-Nan, Luo, Dan-Ni, Li, Zhao-Feng, Voss, Courtney, Li, Shawn, and Cao, Xuan

Abstract

Figure S1. Construction, expression and purification of GST fusion proteins. (a) DNA gel electrophoresis image showing the molecular weights of the DNA fragment of SH2 TrM and pGEX-4Â T3-(Arg)9-SH2 TrM plasmid. (b) SDS-PAGE Coomassie blue-staining image displaying the expression and purification of (Arg)9-GST, (Arg)9-GST SH2 Wt and (Arg)9-GST SH2 TrM in E.coli. Data shown are representative of three independent experiments. (PPTX 163 kb)

Published
2018
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8. Additional file 8: of (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling

Author

An-Dong Liu, Xu, Hui, Gao, Ya-Nan, Luo, Dan-Ni, Li, Zhao-Feng, Voss, Courtney, Li, Shawn, and Cao, Xuan

Abstract

Figure S6. The penetration and toxicity effects of (Arg)9-GST SH2 TrM on PBMCs. (a) The level of pY proteins was very low in PBMCs compared with B16F10 cells. (b) (Arg)9-GST-SH2 TrM protein could enter into PBMCs, but could not efficiently be enriched by pY proteins in these non-cancerous cells, thus the green signal was observed to be weak. All images shown are representative of at least three independent experiments. (PPTX 329 kb)

Published
2018
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9. Additional file 6: of (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling

Author

An-Dong Liu, Xu, Hui, Gao, Ya-Nan, Luo, Dan-Ni, Li, Zhao-Feng, Voss, Courtney, Li, Shawn, and Cao, Xuan

Subjects
animal structures
Abstract

Figure S4. (Arg)9-GST SH2 TrM inhibited the proliferation of A375/DDP cells. Effects of GST, GST SH2 Wt, GST SH2 TrM, (Arg)9-GST, (Arg)9-GST SH2 Wt and (Arg)9-GST SH2 TrM on the proliferation of A375/DDP cells. Cells were treated with different GST-fused proteins at different concentrations (a) (0.5, 1, 2, 4 and 8 μM) for various time (b) (1,2,4 and 8 h) and cell viability was measured by MTT assay (n = 3, *P

Published
2018
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11. Additional file 5: of (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling

Author

An-Dong Liu, Xu, Hui, Gao, Ya-Nan, Luo, Dan-Ni, Li, Zhao-Feng, Voss, Courtney, Li, Shawn, and Cao, Xuan

Subjects
animal structures
Abstract

Figure S3. (Arg)9-GST SH2 TrM inhibited the proliferation of A375 cells. Effects of GST, GST SH2 Wt, GST SH2 TrM, (Arg)9-GST, (Arg)9-GST SH2 Wt and (Arg)9-GST SH2 TrM on the proliferation of A375 cells. Cells were treated with different GST-fused proteins at different concentrations (a) (0.5,1, 2, 4 and 8 μM) for various time (b) (1,2,4 and 8 h) and cell viability was measured by MTT assay (n = 3, *P

Published
2018
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16. (Arg)9-SH2 superbinder: a novel promising anticancer therapy to melanoma by blocking phosphotyrosine signaling.

Author

Liu, An-dong, Xu, Hui, Gao, Ya-nan, Luo, Dan-ni, Li, Zhao-feng, Voss, Courtney, Li, Shawn S. C., and Cao, Xuan

Subjects
MELANOMA, PHOSPHOTYROSINE, CANCER prognosis, ANTINEOPLASTIC agents, CELL proliferation
Abstract

Background: Melanoma is a malignant tumor with high misdiagnosis rate and poor prognosis. The bio-targeted therapy is a prevailing method in the treatment of melanoma; however, the accompanying drug resistance is inevitable. SH2 superbinder, a triple-mutant of the Src Homology 2 (SH2) domain, shows potent antitumor ability by replacing natural SH2-containing proteins and blocking multiple pY-based signaling pathways. Polyarginine (Arg)9, a powerful vector for intracellular delivery of large molecules, could transport therapeutic agents across cell membrane. The purpose of this study is to construct (Arg)9-SH2 superbinder and investigate its effects on melanoma cells, expecting to provide potential new approaches for anti-cancer therapy and overcoming the unavoidable drug resistance of single-targeted antitumor agents. Methods: (Arg)9 and SH2 superbinder were fused to form (Arg)9-SH2 superbinder via genetic engineering. Pull down assay was performed to identify that (Arg)9-SH2 superbinder could capture a wide variety of pY proteins. Immunofluorescence was used to detect the efficiency of (Arg)9-SH2 superbinder entering cells. The proliferation ability was assessed by MTT and colony formation assay. In addition, wound healing and transwell assay were performed to evaluate migration of B16F10, A375 and A375/DDP cells. Moreover, apoptosis caused by (Arg)9-SH2 superbinder was analyzed by flow cytometry-based Annexin V/PI. Furthermore, western blot revealed that (Arg)9-SH2 superbinder influenced some pY-related signaling pathways. Finally, B16F10 xenograft model was established to confirm whether (Arg)9-SH2 superbinder could restrain the growth of tumor. Results: Our data showed that (Arg)9-SH2 superbinder had the ability to enter melanoma cells effectively and displayed strong affinities for various pY proteins. Furthermore, (Arg)9-SH2 superbinder could repress proliferation, migration and induce apoptosis of melanoma cells by regulating PI3K/AKT, MAPK/ERK and JAK/STAT signaling pathways. Importantly, (Arg)9-SH2 superbinder could significantly inhibit the growth of tumor in mice. Conclusions: (Arg)9-SH2 superbinder exhibited high affinities for pY proteins, which showed effective anticancer ability by replacing SH2-containing proteins and blocking diverse pY-based pathways. The remarkable ability of (Arg)9-SH2 superbinder to inhibit cancer cell proliferation and tumor growth might open the door to explore the SH2 superbinder as a therapeutic agent for cancer treatment. [ABSTRACT FROM AUTHOR]

Published
2018
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