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Journal of Environmental Science and Health, Part B
Pesticides, Food Contaminants, and Agricultural Wastes
Volume 56, 2021 - Issue 2
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Research Article

Cyanogenic glycoside amygdalin influences functions of human osteoblasts in vitro

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References

  • Qian, L.; Xie, B.; Wang, Y.; Qian, J. Amygdalin-Mediated Inhibition of Non-Small Cell Lung Cancer Cell Invasion In Vitro. Int. J. Clin. Exp. Pathol. 2015, 8, 5363–5370.
  • Kopcekova, J.; Kolesarova, A.; Kovacik, A.; Kovacikova, E.; Gazarova, M.; Chlebo, P.; Valuch, J.; Kolesarova, A. Influence of Long-Term Consumption of Bitter Apricot Seeds on Risk Factors for Cardiovascular Diseases. J. Environ. Sci. Health B 2018, 53, 298–303. doi:10.1080/03601234.2017.1421841.
  • Halenar, M.; Medvedova, M.; Maruniakova, N.; Kolesarova, A. Ovarian Hormone Production Affected by Amygdalin Addition In Vitro. J. Microbiol. Biotech. Food Sci. 2015, 4, 19–22. doi:10.15414/jmbfs.2015.4.special2.19-22.
  • Lee, H. M.; Moon, A. Amygdalin Regulates Apoptosis and Adhesion in hs578t Triple-Negative Breast Cancer Cells. Biomol. Ther. (Seoul) 2016, 24, 62–66. doi:10.4062/biomolther.2015.172.
  • Juengel, E.; Afschar, M.; Makarevic, J.; Rutz, J.; Tsaur, I.; Mani, J.; Nelson, K.; Haferkamp, A.; Blaheta, R. A. Amygdalin Blocks the In Vitro Adhesion and Invasion of Renal Cell Carcinoma Cells by an Integrin-Dependent Mechanism. Int. J. Mol. Med. 2016, 37, 843–850. doi:10.3892/ijmm.2016.2454.
  • Kovacikova, E.; Kovacik, A.; Halenar, M.; Tokarova, K.; Chrastinova, L.; Ondruska, L.; Jurcik, R.; Kolesar, E.; Valuch, J.; Kolesarova, A. Potential Toxicity of Cyanogenic Glycoside Amygdalin and Bitter Apricot Seed in Rabbits-Health Status Evaluation. J. Anim. Physiol. Anim. Nutr. (Berl) 2019, 103, 695–703. doi:10.1111/jpn.13055.
  • Nour, A.; Azar, B.; Rabata, A.; Manadili, A. The Effect of Amygdalin in the Treatment of Squamous Cell Carcinoma Induced in the Buccal Pouch of Golden Syrian Hamster. Iosr-Jdms. 2016, 15, 75–79. doi:10.9790/0853-15297579.
  • Juengel, E.; Thomas, A.; Rutz, J.; Makarevic, J.; Tsaur, I.; Nelson, K.; Haferkamp, A.; Blaheta, R. A. Amygdalin Inhibits the Growth of Renal Cell Carcinoma Cells In Vitro. Int. J. Mol. Med. 2016, 37, 526–532. doi:10.3892/ijmm.2015.2439.
  • Song, Z.; Xu, X. Advanced Research on Anti-Tumor Effects of Amygdalin. J. Cancer Res. Ther. 2014, 10, 3–7. doi:10.4103/0973-1482.139743.
  • Chang, H. K.; Shin, M. S.; Yang, H. Y.; Lee, J. W.; Kim, Y. S.; Lee, M. H.; Kim, J.; Kim, K. H.; Kim, C. J. Amygdalin Induces Apoptosis through Regulation of Bax and Bcl-2 Expressions in Human DU145 and LNCaP Prostate Cancer Cells. Biol. Pharm. Bull. 2006, 29, 1597–1602. doi:10.1248/bpb.29.1597.
  • Sireesha, D.; Reddy, B. S.; Reginald, B. A.; Samatha, M.; Kamal, F. Effect of Amygdalin on Oral Cancer Cell Line: An In Vitro Study. J. Oral Maxillofac Pathol. 2019, 23, 104–107. doi:10.4103/jomfp.JOMFP_281_18.
  • Liczbiński, P.; Bukowska, B. Molecular Mechanism of Amygdalin Action In Vitro: Review of the Latest Research. Immunopharmacol. Immunotoxicol. 2018, 40, 212–218. doi:10.1080/08923973.2018.1441301.
  • Kim, J.-Y.; Song, Y.-K.; Lim, H.-H. Amygdalin Extract from Armeniaceae Semen Induces Apoptosis in Human COLO 201 Colon Cancer Cells. Korean J. Intern. Med. 2005, 26, 108–121. doi:10.3904/kjim.2011.26.1.108.
  • Jiagang, D.; Li, C.; Wang, H.; Hao, E.; Du, Z.; Bao, C.; Lv, J.; Wang, Y. Amygdalin Mediates Relieved Atherosclerosis in Apolipoprotein E Deficient Mice through the Induction of Regulatory T Cells. Biochem. Biophys. Res. Commun. 2011, 411, 523–529. doi:10.1016/j.bbrc.2011.06.162.
  • Wei, Y.; Xie, Q.; Ito, Y. Preparative Separation of Axifolin-3-Glucoside, Hyperoside and Amygdalin from Plant Extracts by High-Speed Countercurrent Chromatography. J. Liq. Chromatogr. Relat. Technol. 2009, 32, 1010–1022. doi:10.1080/10826070902790983.
  • Moon, J. Y.; Kim, S. W.; Yun, G. M.; Lee, H. S.; Kim, Y. D.; Jeong, G. J.; Ullah, I.; Rho, G. J.; Jeon, B. G. Inhibition of Cell Growth and Down-Regulation of Telomerase Activity by Amygdalin in Human Cancer Cell Lines. Anim. Cells Syst. 2015, 19, 295–304. doi:10.1080/19768354.2015.1060261.
  • Park, H. J.; Yoon, S. H.; Han, L. S.; Zheng, L. T.; Jung, K. H.; Uhm, Y. K.; Lee, J. H.; Jeong, J. S.; Joo, W. S.; Yim, S. V.; et al. Amygdalin Inhibits Genes Related to Cell Cycle in SNU-C4 Human Colon Cancer Cells. World J. Gastroenterol. 2005, 11, 5156–5161. doi:10.3748/wjg.v11.i33.5156.
  • Chen, Y.; Ma, J.; Wang, F.; Hu, J.; Cui, A.; Wei, C.; Yang, Q.; Li, F. Amygdalin Induces Apoptosis in Human Cervical Cancer Cell Line HeLa Cells. Immunopharmacol. Immunotoxicol. 2013, 35, 43–51. doi:10.3109/08923973.2012.738688.
  • Makarevic, J.; Rutz, J.; Juengel, E.; Kaulfuss, S.; Reiter, M.; Tsaur, I.; Bartsch, G.; Haferkamp, A.; Blaheta, R. A. Amygdalin Blocks Bladder Cancer Cell Growth in Vitro by Diminishing Cyclin a and cdk2. PLoS One. 2014, 9, e105590. doi:10.1371/journal.pone.0105590.
  • Yang, C.; Li, X.; Rong, J. Amygdalin Isolated from Semen Persicae (Tao Ren) Extracts Induces the Expression of Follistatin in HepG2 and C2C12 Cell lines. Chin. Med. 2014, 9, 23. doi:10.1186/1749-8546-9-23.
  • Kovacova, V.; Sarocka, A.; Omelka, R.; Bauerova, M.; Grosskopf, B.; Formicki, G.; Kolesarova, A.; Martiniakova, M. Subacute Exposure to Amygdalin Influences Compact Bone Remodelling of Rabbits. J. Physiol. Pharmacol. 2019, 70, 641–648. doi:10.26402/jpp.2019.4.15.
  • Kovacova, V.; Sarocka, A.; Blahova, J.; Sranko, P.; Omelka, R.; Galbavy, D.; Kolesarova, A.; Martiniakova, M. Long-Term Peroral Administration of Bitter Apricot Seeds influences Cortical Bone Microstructure of Rabbits. J. Anim. Physiol. Anim. Nutr. (Berl) 2020, 104, 362–370. doi:10.1111/jpn.13229.
  • Halenar, M.; Tusimova, E.; Nynca, A.; Sadowska, A.; Ciereszko, R.; Kolesarova, A. Stimulatory Effect of Amygdalin on the Viability and Steroid Hormone Secretion by Porcine Ovarian Granulosa Cells In Vitro. J. Microbiol. Biotech. Food Sci. 2016, 5, 44–46. doi:10.15414/jmbfs.2016.5.special1.44-46.
  • Halenar, M.; Medvedova, M.; Baldovska, S.; Michalcova, K.; Kolesarova, A. Co-Administration of Amygdalin and Deoxynivalenol Disrupted Regulatory Proteins Linked to Proliferation of Porcine Ovarian Cells in Vitro. Potravinarstvo Slovak J. Food Sci. 2017, 11, 503–509. doi:10.5219/791.
  • Syrigos, K. N.; Rowlinson-Busza, G.; Epenetos, A. A. In Vitro Cytotoxicity following Specific Activation of Amygdalin by β-Glucosidase Conjugated to a Bladder Cancer-Associated Monoclonal Antibody. Int. J. Cancer 1998, 78, 712–719. doi:10.1002/(sici)1097-0215(19981209(78:6 < 712::aid-ijc8 > 3.0.co;2-d.
  • Guo, J.; Wu, W.; Sheng, M.; Yang, S.; Tan, J. Amygdalin Inhibits Renal Fibrosis in Chronic Kidney Disease. Mol. Med. Rep. 2013, 7, 1453–1457. doi:10.3892/mmr.2013.1391.
  • Roeder, E.; Matthews, B. G.; Kalajzic, I. Visual Reporters for Study of the Osteoblast Lineage. Bone 2016, 92, 189–195. doi:10.1016/j.bone.2016.09.004.
  • Rutkovskiy, A.; Stensløkken, K. O.; Vaage, I. J. Osteoblast Differentiation at a Glance. Med. Sci. Monit. Basic Res. 2016, 22, 95–106. doi:10.12659/msmbr.901142.
  • Shi, S.; Kirk, M.; Kahn, A. J. The Role of Type I Collagen in the Regulation of the Osteoblast Phenotype. J. Bone Miner. Res. 1996, 11, 1139–1145. doi:10.1002/jbmr.5650110813.
  • Komori, T. Regulation of Proliferation, Differentiation and Functions of Osteoblasts by Runx2. IJMS. 2019, 20, 1694. doi:10.3390/ijms20071694.
  • Gelse, K.; Pöschl, E.; Aigner, T. Collagens-Structure, Function, and Biosynthesis. Adv. Drug Deliv. Rev. 2003, 55, 1531–1546. doi:10.1016/j.addr.2003.08.002.
  • Millan, J. L. Alkaline Phosphatases: Structure, Substrate Specificity and Functional Relatedness to Other Members of a Large Superfamily of Enzymes. Puronergic Signal 2006, 2, 335–341. doi:10.1007/s11302-005-5435-6.
  • Golub, E. E.; Boesze-Battaglia, K. The Role of Alkaline Phosphatase in Mineralization. Curr. Opin. Orthop. 2007, 18, 444–448. doi:10.1097/BCO.0b013e3282630851.
  • Xu, Z.; Dai, F.; Chen, J.; Lv, M.; Cheng, J.; Zhang, X.; Lin, B. Experimental Research into the Potential Therapeutic Effect of GYY4137 on Ovariectomy-Induced Osteoporosis. Cell Mol. Biol. Lett. 2018, 23, 47. doi:10.1186/s11658-018-0114-0.
  • Zhang, A.; Pan, W.; Lv, J.; Wu, H. Protective Effect of Amygdalin on LPS-Induced Acute Lung Injury by Inhibiting NF-κB and NLRP3 Signaling Pathways. Inflammation 2017, 40, 745–751. doi:10.1007/s10753-017-0518-4.
  • Zhang, J.; Cai, H.; Guo, X.; Yin, J.; Yang, B.; Feng, Y.; Jin, H. Effects of Amygdalin on Alcohol-Induced Adipogenic Differentiation of Rabbit Bone Marrow Mesenchymal Stem Cells. Int. J. Clin. Exp. Pathol. 2016, 9, 12439–12445.
  • Aitken, D.; West, D.; Smith, F.; Poznanski, W.; Cowan, J.; Hurtig, J.; Peterson, E.; Benoit, B. Cyanide Toxicity following Nitroprusside Induced Hypotension. Can. Anaesth. Soc. J. 1977, 24, 651–660. doi:10.1007/bf03006709.
  • Yen, D.; Tsai, J.; Wang, L. M.; Kao, W. F.; Hu, S. C.; Lee, C. H.; Deng, J. F. The Clinical Experience of Acute Cyanide Poisoning. Am. J. Emerg. Med. 1995, 13, 524–528. doi:10.1016/0735-6757(95)90162-0.
  • Park, J.; Lee, S.; Choi, H.; Choi, Y. H.; Lee, Y. Management of Cyanide Intoxication with Extracorporeal Membrane Oxygenation and Continuous Renal Replacement Therapy. Korean J. Crit. Care Med. 2015, 30, 218–221. doi:10.4266/kjccm.2015.30.3.218.
  • Krieger, N. S.; Sessler, N. E.; Bushinsky, D. A. Acidosis Inhibits Osteoblastic and Stimulates Osteoclastic Activity In Vitro. Am. J. Physiol. 1992, 262, F442–F448. doi:10.1152/ajprenal.1992.262.3.F442.
  • Frick, K. K.; Jiang, L.; Bushinsky, D. A. Acute Metabolic Acidosis Inhibits the Induction of Osteoblastic Egr-1 and Type 1 Collagen. Am. J. Physiol. 1997, 272, C1450–1456. doi:10.1152/ajpcell.1997.272.5.C1450.
  • Zoch, M. L.; Clemens, T. L.; Riddle, R. C. New Insights into the Biology of Osteocalcin. Bone 2016, 82, 42–49. doi:10.1016/j.bone.2015.05.046.
  • Blair, H. C.; Larrouture, Q. C.; Li, Y.; Lin, H.; Beer-Stoltz, D.; Liu, L.; Tuan, R. S.; Robinson, L. J.; Schlesinger, P. H.; Nelson, D. J. Osteoblast Differentiation and Bone Matrix Formation In Vivo and In Vitro. Tissue Eng. Part B Rev. 2017, 23, 268–280. doi:10.1089/ten.TEB.2016.0454.
  • Han, Y.; You, X.; Xing, W.; Zhang, Z.; Zou, W. Paracrine and Endocrine Actions of Bone-the Functions of Secretory Proteins from Osteoblasts, Osteocytes, and Osteoclasts. Bone Res. 2018, 6, 1–11. doi:10.1038/s41413-018-0019-6.
  • Takahashi, N.; Maeda, K.; Ishihara, A.; Uehara, S.; Kobayashi, Y. Regulatory Mechanism of Osteoclastogenesis by RANKL and Wnt Signals. Front Biosci. (Landmark Ed) 2011, 16, 21–30. doi:10.2741/3673.
  • Maeda, K.; Kobayashi, Y.; Udagawa, N.; Uehara, S.; Ishihara, A.; Mizoguchi, T.; Kikuchi, Y.; Takada, I.; Kato, S.; Kani, S.; et al. Wnt5a-Ror2 Signaling between Osteoblast-Lineage Cells and Osteoclast Precursors Enhances Osteoclastogenesis. Nat. Med. 2012, 18, 405–412. doi:10.1038/nm.2653.
  • Frick, K. K.; Bushinsky, D. A. Metabolic Acidosis Stimulates RANKL RNA Expression in Bone through a Cyclo-Oxygenase-Dependent Mechanism. J. Bone Miner. Res. 2003, 18, 1317–1325. doi:10.1359/jbmr.2003.18.7.1317.
  • Krieger, N. S.; Bushinsky, D. A.; Frick, K. K. Cellular Mechanisms of Bone Resorption Induced by Metabolic Acidosis. Semin. Dial. 2003, 16, 463–466. doi:10.1046/j.1525-139x.2003.16100.x.
  • Valencia, J.; Martinez, V. G.; Hidalgo, L.; Hernandez-Lopez, C.; Canseco, N. M.; Vicente, A.; Varas, A.; Sacedon, R. Wnt5a Signaling increases IL-12 Secretion by Human Dendritic Cells and enhances IFN-γ Production by CD4+ T cells. Immunol. Lett. 2014, 162, 188–199. doi:10.1016/j.imlet.2014.08.015.
  • Riemann, A.; Wußling, H.; Loppnow, H.; Fu, H.; Reime, S.; Thews, O. Acidosis Differently Modulates the Inflammatory Program in Monocytes and Macrophages. Biochim. Biophys. Acta. 2016, 1862, 72–81. doi:10.1016/j.bbadis.2015.10.017.
  • Chang, J.; Jackson, S. G.; Wardale, J.; Jones, S. W. Hypoxia Modulates the Phenotype of Osteoblasts Isolated from Knee Osteoarthritis Patients, Leading to Undermineralized Bone Nodule Formation. Arthritis Rheumatol. 2014, 66, 1789–1799. doi:10.1002/art.38403.
  • Kawane, T.; Qin, X.; Jiang, Q.; Miyazaki, T.; Komori, H.; Yoshida, C. A.; Matsuura-Kawata, V. K. D. S.; Sakane, C.; Matsuo, Y.; Nagai, K.; et al. Runx2 is Required for the Proliferation of Osteoblast Progenitors and Induces Proliferation by Regulating Fgfr2 and Fgfr3. Sci. Rep. 2018, 8, 13551. doi:10.1038/s41598-018-31853-0.
  • Bruderer, M.; Richards, R. G.; Alini, M.; Stoddart, M. J. Role and Regulation of RUNX2 in osteogenesis. Eur. Cell. Mater. 2014, 28, 269–286. doi:10.22203/ecm.v028a19.
  • Komori, T. Runx2, an Inducer of Osteoblast and chondrocyte differentiation. Histochem. Cell Biol. 2018, 149, 313–323. doi:10.1007/s00418-018-1640-6.
  • Miao, E. A.; Rajan, J. V.; Aderem, A. Caspase-1-Induced Pyroptotic Cell Death. Immunol. Rev. 2011, 243, 206–214. doi:10.1111/j.1600-065X.2011.01044.x.
  • Gokalp-Ozkorkmaz, E.; Asir, F.; Basaran, S. O.; Agacayak, E.; Sahin, F.; Kaya, S.; Erdogan, G.; Deveci, E. Examination of Bcl-2 and Bax Protein Levels for Determining the Apoptotic Changes in Placentas with Gestational Diabetes and Preeclampsia. Proceedings 2018, 2, 1548. doi:10.3390/proceedings2251548.
  • Cassiem, W.; de Kock, M. The anti-Proliferative Effect of Apricot and Peach Kernel Extracts on Human Colon Cancer Cells In Vitro. BMC Complement Altern. Med. 2019, 19, 32. doi:10.1186/s12906-019-2437-4.
  • Kikuchi, A.; Yamamoto, H.; Sato, A.; Matsumoto, S. Wnt5a: its Signalling, Functions and Implication in Diseases. Acta Physiol. (Oxf.) 2012, 204, 17–33. doi:10.1111/j.1748-1716.2011.02294.x.
  • She, Y.; Shao, L.; Zhang, Y.; Hao, Y.; Cai, Y.; Cheng, Z.; Deng, C.; Liu, X. Neuroprotective Effect of Glycosides in Buyang Huanwu Decoction on Pyroptosis following Cerebral Ischemia-Reperfusion Injury in Rats. J. Ethnopharmacol. 2019, 242, 112051. doi:10.1016/j.jep.2019.112051.
  • Domazetovic, V.; Marcucci, G.; Iantomasi, T.; Brandi, M. L.; Vincenzini, M. T. Oxidative Stress in Bone Remodeling: Role of Antioxidants. Clin. Cases Miner. Bone Metab. 2017, 14, 209–216. doi:10.11138/ccmbm/2017.14.1.209.
  • Perillo, B.; Di Donato, M.; Pezone, A.; Di Zazzo, E.; Giovannelli, P.; Galasso, G.; Castoria, G.; Migliaccio, A. ROS in Cancer Therapy: The Bright Side of the Moon. Exp. Mol. Med. 2020, 52, 192–203. doi:10.1038/s12276-020-0384-2.
  • Abboud, M. M.; Al Awaida, W.; Alkhateeb, H. H.; Abu-Ayyad, A. N. Antitumor Action of Amygdalin on Human Breast Cancer Cells by Selective Sensitization to Oxidative Stress. Nutr. Cancer 2019, 71, 483–490. doi:10.1080/01635581.2018.1508731.
  • Ighodaro, O. M.; Akinloye, O. A. First Line Defence Antioxidants-Superoxide Dismutase (SOD), Catalase (CAT) and Glutathione Peroxidase (GPX): Their Fundamental Role in the Entire Antioxidant Defence Grid. Alexandria J. Med. 2018, 54, 287–293. doi:10.1016/j.ajme.2017.09.001.

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