Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy

Yun-long Li; Qiao-xing Li; Rui-jiang Liu; Xiang-qian Shen

doi:10.1007/s11655-015-2154-x

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Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy

Updated：2021-08-27

- Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy
- Chinese Journal of Integrative Medicine Vol. 24, Issue 3, Pages: 237-240(2018)
- Affiliations：
  
  1. Department of Urology, Kunshan Hospital Affiliated to Jiangsu University, Kunshan,Zhejiang Province,China
  2. School of Material Science and Engineering, Jiangsu University,Zhejiang Province,Zhenjiang,China
- Author bio：
- Funds：
- DOI：10.1007/s11655-015-2154-x
  CLC：
- Published：2018，
  
  Published Online：14 August 2015，
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Li, Yl., Li, Qx., Liu, Rj. et al. Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy., Chin. J. Integr. Med. 24, 237–240 (2018). https://doi.org/10.1007/s11655-015-2154-x

Yun-long Li, Qiao-xing Li, Rui-jiang Liu, et al. Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy. [J]. Chinese Journal of Integrative Medicine 24(3):237-240(2018)
Li, Yl., Li, Qx., Liu, Rj. et al. Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy., Chin. J. Integr. Med. 24, 237–240 (2018). https://doi.org/10.1007/s11655-015-2154-x DOI：

Yun-long Li, Qiao-xing Li, Rui-jiang Liu, et al. Chinese Medicine Amygdalin and β-Glucosidase Combined with Antibody Enzymatic Prodrug System As A Feasible Antitumor Therapy. [J]. Chinese Journal of Integrative Medicine 24(3):237-240(2018) DOI： 10.1007/s11655-015-2154-x.

摘要

Amarogentin is an efficacious Chinese herbal medicine and a component of the bitter apricot kernel. It is commonly used as an expectorant and supplementary anti-cancer drug. β-Glucosidase is an enzyme that hydrolyzes the glycosidic bond between aryl and saccharide groups to release glucose. Upon their interaction

β-glucosidase catalyzes amarogentin to produce considerable amounts of hydrocyanic acid

which inhibits cytochrome C oxidase

the terminal enzyme in the mitochondrial respiration chain

and suspends adenosine triphosphate synthesis

resulting in cell death. Hydrocyanic acid is a cell-cycle-stage-nonspecific agent that kills cancer cells. Thus

β-glucosidase can be coupled with a tumor-specific monoclonal antibody. β-Glucosidase can combine with cancer-cell-surface antigens and specifically convert amarogentin to an active drug that acts on cancer cells and the surrounding antibodies to achieve a killing effect. β-Glucosidase is injected intravenously and recognizes cancer-cell-surface antigens with the help of an antibody. The prodrug amarogentin is infused after β-glucosidase has reached the target position. Coupling of cell membrane peptides with β-glucosidase allows the enzyme to penetrate capillary endothelial cells and clear extracellular deep solid tumors to kill the cells therein. The Chinese medicine amarogentin and β-glucosidase will become an important treatment for various tumors when an appropriate monoclonal antibody is developed.

Abstract

β-glucosidase catalyzes amarogentin to produce considerable amounts of hydrocyanic acid

which inhibits cytochrome C oxidase

the terminal enzyme in the mitochondrial respiration chain

and suspends adenosine triphosphate synthesis

resulting in cell death. Hydrocyanic acid is a cell-cycle-stage-nonspecific agent that kills cancer cells. Thus

关键词

amarogentinβ-glucosidaseantibody enzymatic prodrugtargeting therapyChinese Medicine

Keywords

amarogentinβ-glucosidaseantibody enzymatic prodrugtargeting therapyChinese Medicine

references

Schellmann N, Deckert P M, Bachran D, Fuchs H, Bachran C. Targeted enzyme prodrug therapies. Mini Rev Med Chem 2010;10:887–904.

Shen YY, ed. Pharmacology of traditional Chinese medicine. Beijing: People’s Medical Publishing House; 2011:684–687.

Milazzo S, Ernst E, Lejeune S, Schmidt K. Laetrile treatment for cancer. Cochrane Database Syst Rev 2006:2:CD005476.

Cao ML. Research progress of cyanogentic glycosides in plant. Plant Physiol Commun 1992;29:68–72.

Wu XR, Liu JW. Cyanogenic compounds structure and distribution in plants. Plant Physiol Commun 1985;1:8–14.

Swain E, Poulton JE. Utilization of amygdalin during seedling development of prunus serotina. Plant Physiol 1994;106:437–445.

Chang HK, Shin MS, Yang HY, Lee JW, Kim YS, Lee MH, et al. 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.

Shukla S, Bafna K, Sundar D, Thorat SS. The bitter barricading of prostaglandin biosynthesis pathway: understanding the molecular mechanism of selective cyclooxygenase-2 inhibition by amarogentin, a secoiridoid glycoside from Swertia chirayita. PLoS One 2014;9:90637.

Xie Y, Shang XX, Cao LH. Studies on the liquid-state culture medium of ß-glucosidase from Aspergillus niger. J Nanchang Hangkong Univ (Social Sci, Chin) 2007;21:49–52.

Yang JH, Ren DM. Selection of high-yield ß-glucosidase strain and the optimized of solid state fermentation. J Anhui Agricult Sci (Chin) 2005;33:1566–1568.

Lian YJ, Chen DD, Huang T, Ke ML, Xu TW, Zheng YB, et al. In vitro cytotoxity on colorectal carcinoma LoVo cells of amygdalin following specific activation by ß-glucosidase and influence on expression of bcl-2, bax gene and caspase-3 activity. Chin J Cancer prev Treat 2005;12:413.

Xu NX. The research progress of amygdalin. Inner Mongolia Chin Med (Chin) 2012;31:66–67.

Xing GX, Li N, Yang JY, Cui LJ, Wang T. Research progress of natural amygdalin. Chin Tradit Patent Med (Chin) 2003;25:1007–1009.

Lian YJ, Chen DD, Huang T. Research progress of tumor antibody oriented enzyme prodrug. Med J Chin People Health (Chin) 2006;18:888.

Nie Z, Zhou J, Wang QH, Wang GW. Bladder cancer cells apoptosis induced by amygdalin following specific activation by ß-gIucosidase. J Mod Urol 2013;18:113–116.

Chen SM. New use of bitter almond. Chin J Modern Appl Pharm (Chin) 1991;8:44–45.

Mu J. Research development of Apricot seed sapomin. Inform Tradit Chin Med (Chin) 2002;19:19–21.

Wei JT, Liu WQ. Research on and application of amygdalin in prescription. J Hainan Med Coll (Chin) 2007;13:589–590.

Lian YJ, Xu TW, Zheng YB, Ke ML, Li Z, Huang T, et al. Therapeutic effect of anti-CEAMcAb-ß-glucosidase conjugate/amygdalin system on colorectal cancer xenografts in nude mice. Orthopaedics 2005;29:50.

Fonseca SB, Pemim MP, Kelley SD. Recent advances in the use of cell-penetrating pepties for medical and biological applications. Adv Drug Deliy Rev 2009;61:953–964.

Zhang XJ, Liu YW, Wang J, Deng P, Jiang Y. Construction and inhibitory effect of TAT-p38(AF) on UV-induced activation of p38 MAPK pathway. Shangdong Med J (Chin) 2010;50:19–21.

Wang GW, Zhou J, Wang QH, Liu YL. Preparation and identification of CPPs-ß-glucosidase conjugates. Shandong Med J (Chin) 2013;53:1–4.

Syrigos KN, Rowlinson Busza G, Epenetos AA. In vitro cytotoxicity following specific activation of amygadalin by beta-glicosidase conjugated to a bladder cancer-associated monoclonalantibody. Int J Cancer 1998;78:721–719.

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