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The anti-cancer effect of amygdalin on human cancer cell lines

  • Asghar Arshi
  • Sayed Mostafa HosseiniEmail author
  • Fataneh Saleh Khaje Hosseini
  • Zahra Yousefnejad Amiri
  • Fatemeh Sadat Hosseini
  • Mahsa Sheikholia Lavasani
  • Hossein Kerdarian
  • Maryam Safarpour Dehkordi
Original Article
  • 12 Downloads

Abstract

Derived from rosaceous plant seed, amygdalin belongs to aromatic cyanogenic glycoside group, and its anticancer effects have been supported by mounting evidence. In this study, we objected to investigate amygdalin effect on two antiapoptotic genes (Survivin, XIAP) and two lncRNAs (GAS5, MALAT1) in human cancer cells (A549, MCF7, AGS). Employing RT-qPCR analysis, we compared the mRNA levels of the genes related to apoptosis in A549, MCF7, and AGS cancer cells between amygdalin-treated (24, 48 and 72 h) and un-treated groups. RNA was extracted from both cell groups and then cDNAs were synthesized. The changes in the gene expression levels were specified using ΔΔCt method. RT-qPCR analysis has revealed that the expression of Survivin, XIAP, GAS5 and MALAT1 in amygdala-treated cancer cells were significantly different, compared to the un-treated cells. However, these expressions were different depending on the treatment time. According to the results, amygdalin significantly inhibited the expression level of Survivin, and XIAP genes in treated via untreated group. Our findings suggest that amygdalin might have an anticancer effect due to the various gene expressions in A549, MCF7, and AGS human cancer cells, showing it’s potential as a natural therapeutic anticancer drug.

Keywords

Amygdalin Antiapoptotic genes LncRNAs Cancer cell line 

Notes

Acknowledgements

Iran’s National Elites Foundation give this opportunity to graduate students to work on a scientific project instead of going to the military garrison. This manuscript is an outcome of military service project of first author (Mr. Asghar Arshi). Also, the authors would like to thank all the staff members of the Cellular and Molecular Research Center, Shahrekord University of Medical Sciences in Iran for their sincere support.

Author contributions

AA and SMH: Conceptualization; FH: Software; ZYA: Validation; FSH and ML: Formal analysis; SMH: Investigation; HK and MSD: Resources; AA and SMH: Writing-original draft preparation, Writing-review & editing; SMH: Supervision.

Compliance with ethical standards

Conflict of interest

All authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human participants performed by any of the authors.

References

  1. 1.
    Milazzo S, Ernst E, Lejeune S et al (2011) Laetrile treatment for cancer. In: Milazzo S (ed) Cochrane database of systematic reviews. Wiley, Chichester, p CD005476Google Scholar
  2. 2.
    Santos Pimenta LP, Schilthuizen M, Verpoorte R, Choi YH (2014) Quantitative analysis of amygdalin and prunasin in Prunus serotina Ehrh. Using H-NMR spectroscopy. Phytochem Anal 25:122–126.  https://doi.org/10.1002/pca.2476 CrossRefGoogle Scholar
  3. 3.
    Isoza T, Matano Y, Yamamoto K et al (2001) Quantitative determination of amygdalin epimers by cyclodextrin-modified micellar electrokinetic chromatography. J Chromatogr A 923:249–254CrossRefGoogle Scholar
  4. 4.
    Owa C, Messina ME, Halaby R, Halaby R (2013) Triptolide induces lysosomal-mediated programmed cell death in MCF-7 breast cancer cells. Int J Womens Health 5:557–569.  https://doi.org/10.2147/IJWH.S44074 Google Scholar
  5. 5.
    Xu X, Song Z (2014) Advanced research on anti-tumor effects of amygdalin. J Cancer Res Ther 10:3.  https://doi.org/10.4103/0973-1482.139743 CrossRefGoogle Scholar
  6. 6.
    Zhou C, Qian L, Ma H et al (2012) Enhancement of amygdalin activated with β-d-glucosidase on HepG2 cells proliferation and apoptosis. Carbohydr Polym 90:516–523.  https://doi.org/10.1016/j.carbpol.2012.05.073 CrossRefGoogle Scholar
  7. 7.
    Jaswal V, Palanivelu J, C R (2018) Effects of the Gut microbiota on amygdalin and its use as an anti-cancer therapy: substantial review on the key components involved in altering dose efficacy and toxicity. Biochem Biophys Rep 14:125–132.  https://doi.org/10.1016/j.bbrep.2018.04.008 Google Scholar
  8. 8.
    Lee HM, Moon A (2016) Amygdalin regulates apoptosis and adhesion in Hs578T triple-negative breast cancer cells. Biomol Ther 24:62–66.  https://doi.org/10.4062/biomolther.2015.172 CrossRefGoogle Scholar
  9. 9.
    Chang H-K, Shin M-S, Yang H-Y et al (2006) Amygdalin induces apoptosis through regulation of Bax and Bcl-2 expressions in human DU145 and LNCaP prostate cancer cells. Biol Pharm Bull 29:1597–1602CrossRefGoogle Scholar
  10. 10.
    Chen Y, Ma J, Wang F et al (2013) Amygdalin induces apoptosis in human cervical cancer cell line HeLa cells. Immunopharmacol Immunotoxicol 35:43–51.  https://doi.org/10.3109/08923973.2012.738688 CrossRefGoogle Scholar
  11. 11.
    Makarević J, Rutz J, Juengel E et al (2014) Amygdalin influences bladder cancer cell adhesion and invasion in vitro. PLoS ONE 9:e110244.  https://doi.org/10.1371/journal.pone.0110244 CrossRefGoogle Scholar
  12. 12.
    Sarela AI, Scott N, Ramsdale J et al (2001) Immunohistochemical detection of the anti-apoptosis protein, survivin, predicts survival after curative resection of stage II colorectal carcinomas. Ann Surg Oncol 8:305–310CrossRefGoogle Scholar
  13. 13.
    Galbán S, Hwang C, Rumble JM et al (2009) Cytoprotective effects of IAPs revealed by a small molecule antagonist. Biochem J 417:765–771.  https://doi.org/10.1042/BJ20081677 CrossRefGoogle Scholar
  14. 14.
    Prager GW, Mihaly J, Brunner PM et al (2009) Urokinase mediates endothelial cell survival via induction of the X-linked inhibitor of apoptosis protein. Blood 113:1383–1390.  https://doi.org/10.1182/blood-2008-06-164210 CrossRefGoogle Scholar
  15. 15.
    Karnoub AE, Weinberg RA (2006) Chemokine networks and breast cancer metastasis. Breast Dis 26:75–85CrossRefGoogle Scholar
  16. 16.
    Smith CM, Steitz JA (1998) Classification of gas5 as a multi-small-nucleolar-RNA (snoRNA) host gene and a member of the 5′-terminal oligopyrimidine gene family reveals common features of snoRNA host genes. Mol Cell Biol 18:6897–6909CrossRefGoogle Scholar
  17. 17.
    Kino T, Hurt DE, Ichijo T et al (2010) Noncoding RNA Gas5 Is a growth arrest- and starvation-associated repressor of the glucocorticoid receptor. Sci Signal 3:ra8–ra8.  https://doi.org/10.1126/scisignal.2000568 Google Scholar
  18. 18.
    Ji P, Diederichs S, Wang W et al (2003) MALAT-1, a novel noncoding RNA, and thymosin β4 predict metastasis and survival in early-stage non-small cell lung cancer. Oncogene 22:8031–8041.  https://doi.org/10.1038/sj.onc.1206928 CrossRefGoogle Scholar
  19. 19.
    Bernard D, Prasanth KV, Tripathi V et al (2010) A long nuclear-retained non-coding RNA regulates synaptogenesis by modulating gene expression. EMBO J 29:3082–3093.  https://doi.org/10.1038/emboj.2010.199 CrossRefGoogle Scholar
  20. 20.
    Tripathi V, Ellis JD, Shen Z et al (2010) The nuclear-retained noncoding RNA MALAT1 regulates alternative splicing by modulating SR splicing factor phosphorylation. Mol Cell 39:925–938.  https://doi.org/10.1016/j.molcel.2010.08.011 CrossRefGoogle Scholar
  21. 21.
    Yang L, Lin C, Liu W et al (2011) ncRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs. Cell 147:773–788.  https://doi.org/10.1016/j.cell.2011.08.054 CrossRefGoogle Scholar
  22. 22.
    Arshi A, Sharifi FS, Khorramian Ghahfarokhi M et al (2018) Expression analysis of MALAT1, GAS5, SRA and NEAT1 long non-coding RNAs in breast cancer tissues from young women and women over 45 years of age. Mol Ther-Nucleic Acids 12:751–757.  https://doi.org/10.1016/J.OMTN.2018.07.014 CrossRefGoogle Scholar
  23. 23.
    Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2-∆∆CT Method. Methods 25:402–408.  https://doi.org/10.1006/meth.2001.1262 CrossRefGoogle Scholar
  24. 24.
    Wang H, Khor TO, Shu L et al (2012) Plants vs. cancer: a review on natural phytochemicals in preventing and treating cancers and their druggability. Anticancer Agents Med Chem 12:1281–1305CrossRefGoogle Scholar
  25. 25.
    Liczbiński P, Bukowska B (2018) Molecular mechanism of amygdalin action in vitro: review of the latest research. Immunopharmacol Immunotoxicol 40:212–218.  https://doi.org/10.1080/08923973.2018.1441301 CrossRefGoogle Scholar
  26. 26.
    Moss RW (2005) Patient perspectives. Integr Cancer Ther 4:65–86.  https://doi.org/10.1177/1534735404273918 CrossRefGoogle Scholar
  27. 27.
    Qian L, Xie B, Wang Y, Qian J (2015) Amygdalin-mediated inhibition of non-small cell lung cancer cell invasion in vitro. Int J Clin Exp Pathol 8:5363–5370Google Scholar
  28. 28.
    Fukuda T, Ito H, Mukainaka T et al (2003) Anti-tumor promoting effect of glycosides from prunus persica seeds. Biol Pharm Bull 26:271–273CrossRefGoogle Scholar
  29. 29.
    Kwon H-Y, Hong S-P, Hahn D-H, Kim JH (2003) Apoptosis induction of persicae semen extract in human promyelocytic leukemia (HL-60) cells. Arch Pharm Res 26:157–161CrossRefGoogle Scholar

Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Human Genetic Research CenterBaqiyatallah University of Medical ScienceTehranIran
  2. 2.Department of Biology, Science and Research BranchIslamic Azad UniversityTehranIran
  3. 3.Students Research CommitteeBabol University of Medical ScienceBabolIran
  4. 4.Young Researchers and Elite Club, Shahrekord BranchIslamic Azad UniversityShahrekordIran

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