Journal Home > Volume 11 , Issue 5
Objective

To investigate the effects of silkworm pupa (Bombyx mori) protein (SPP) on cell proliferation, apoptosis and energy metabolism in human colon cancer cells DLD-1.

Methods

CCK-8 was used to detect cell proliferation rate after 72 h of cell culture for the control group (normal cultured DLD-1 cells) and SPP dose groups; Annexin-V/PI was applied to observe cell apoptosis; XFe24 Extracellular Flux Analyzer was used to detect cell mitochondrial respiratory function and glycolytic function.

Results

Comparing with the control, SPP significantly inhibited the proliferation of DLD-1 cells with all the dosage tested (P < 0.01); flow cytometry showed that SPP significantly promoted apoptosis (P < 0.05). Additionally, SPP could significantly inhibited mitochondrial metabolism and glycolysis of DLD-1 cells and decreased cell energy metabolism in all groups treated with different doses.

Conclusion

SPP can cause oxidative damage, promote apoptosis, and reduce mitochondrial respiratory and glycolysis rate in colon cancer DLD-1 cells, which reveals that SPP has the potential to serve as the anti-cancer drugs in the future, but further experimental evidence is needed.


menu
Abstract
Full text
Outline
About this article

Effects of silkworm pupa protein on apoptosis and energy metabolism in human colon cancer DLD-1 cells

Show Author's information Xiaojiao JiaJing WangbAijin MacDuo FengaYue HeaWenjie Yana( )
College of Biochemical Engineering, Beijing Union University, Beijing 100101, China
Institute of Food and Nutrition Development, Ministry of Agriculture and Rural Affairs, Beijing 100125, China
College of Food and Health, Beijing Technology and Business University, Beijing 100048, China

Peer review under responsibility of KeAi Communications Co., Ltd.

Abstract

Objective

To investigate the effects of silkworm pupa (Bombyx mori) protein (SPP) on cell proliferation, apoptosis and energy metabolism in human colon cancer cells DLD-1.

Methods

CCK-8 was used to detect cell proliferation rate after 72 h of cell culture for the control group (normal cultured DLD-1 cells) and SPP dose groups; Annexin-V/PI was applied to observe cell apoptosis; XFe24 Extracellular Flux Analyzer was used to detect cell mitochondrial respiratory function and glycolytic function.

Results

Comparing with the control, SPP significantly inhibited the proliferation of DLD-1 cells with all the dosage tested (P < 0.01); flow cytometry showed that SPP significantly promoted apoptosis (P < 0.05). Additionally, SPP could significantly inhibited mitochondrial metabolism and glycolysis of DLD-1 cells and decreased cell energy metabolism in all groups treated with different doses.

Conclusion

SPP can cause oxidative damage, promote apoptosis, and reduce mitochondrial respiratory and glycolysis rate in colon cancer DLD-1 cells, which reveals that SPP has the potential to serve as the anti-cancer drugs in the future, but further experimental evidence is needed.

Keywords: Mitochondria, Apoptosis, Glycolysis, Colon cancer DLD-1 cells, Silkworm pupa protein

References(31)

[1]
World Health Organization: Cancer Factsheet N°297, (2011). http://www.who.int/mediacentre/factsheets/fs297/en/.
[2]

R.L. Siegel, K.D. Miller, A. Jemal, Cancer statistics, 2018, CA Cancer J. Clin. 68(1) (2018) 7-30. https://doi.org/10.3322/caac.21442.

[3]

R.S. Zheng, K.X. Sun, S.W. Zhang, et al., Report of cancer incidence and mortality in China, Chin. J. Cancer Res. 41(1) (2019) 19-28.

[4]
F. Sheets, All cancers (excluding non-melanoma skin cancer) estimated incidence, Mortality and Prevalence Worldwide in 2012, 2014.
[5]

P. Yang, S. Abe, Y.P. Zhao, et al., Growth suppression of rat hepatoma cells by a pentapeptide from Antheraea yamamai, Insect Biotechnol. Sericol. 73 (2004) 7-13.

[6]

C. Wang, T. Chen, N. Zhang, et al., Melittin, a major component of bee venom, sensitizes human hepatocellular carcinoma cells to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis by activating CaMKII-TAK1-JNK/p38 and inhibiting IκBα kinase-NFκB, Biol. Chem. 284 (2009) 3804-3813. https://doi.org/10.1074/jbc.M807191200.

[7]

C. Bincoletto, S. Eberlin, C.A.V. Figueiredo, et al., Effects produced by Royal Jelly on haematopoiesis: relation with host resistance against Ehrlich ascites tumour challenge, Int. Immunopharmacol. 5(4) (2005) 679-688. https://doi.org/10.1016/j.intimp.2004.11.015.

[8]

W. Wang, G.Q. He, Y.Z. Jin, et al., Comprehensive utilization of silkworm pupa proteins and prospects for development, Food Fermn. Ind. 32(9) (2006) 112-115.

[9]

Q. Wu, J. Jia, H. Yan, et al., A novel angiotensin-I converting enzyme (ACE) inhibitory peptide from gastrointestinal protease hydrolysate of silkworm pupa (Bombyx mori) protein: biochemical characterization and molecular docking study, Peptides 68 (2015) 17-24. https://doi.org/10.1016/j.peptides.2014.07.026.

[10]

W. Wang, N. Wang, Y. Zhou, et al., Isolation of a novel peptide from silkworm pupae protein components and interaction characteristics to angiotensin I-converting enzyme, Eur. Food Res. Technol. 232 (2010) 29-38. https://doi.org/10.1007/s00217-010-1358-8.

[11]

W. Wang, N. Wang, Y. Zhang, Antihypertensive properties on spontaneously hypertensive rats of peptide hydrolysates from silkworm pupae protein, Food Nutr. Sci. 5 (2014) 1202-1211. https://doi.org/10.4236/fns.2014.513131.

[12]

S.P. Ryu, Silkworm pupae powder ingestion increases fat metabolism in swim-trained rats, J. Exerc. Nutr. Biochem. 18(2) (2014) 141-149. https://doi.org/10.5717/jenb.2014.18.2.141.

[13]

J. Wattanathorn, S. Muchimapura, A. Boosel, et al., Silkworm pupae protect against Alzheimer's disease, Am. J. Agric. Biol. Sci. 7(3) (2012) 330-336. https://doi.org/10.3844/ajabssp.2012.330.336.

[14]

R.K. Maiti, A.P. Ocejio, P. Mastreta, Note on edible insects as protein source in underdeveloped countries, Proc. Zool. Soc. 54(2) (2001) 43-46.

[15]

H. Tomotake, M. Katagiri, M. Yamato, Silkworm pupae (Bombyx mori) are new sources of high quality protein and lipid, J. Nutr. Sci. Vitaminol. (Tokyo) 56(6) (2010) 446-448. https://doi.org/10.3177/jnsv.56.446.

[16]

Y. Yang, L. Tang, L. Tong, et al., Silkworms culture as a source of protein for humans in space, Adv. Space Res. 43 (2009) 1236-1242. https://doi.org/10.1016/j.asr.2008.12.009.

[17]

S.H. Lee, D. Park, G. Yang, et al., Silk and silkworm pupa peptides suppress adipogenesis in preadipocytes and fat accumulation in rats fed a high-fat diet, Eur. J. Nutr. 51(8) (2012) 1011-1019. https://doi.org/10.1007/s00394-011-0280-6.

[18]

J. Zhou, D. Han, Safety evaluation of protein of silkworm (Antheraea pernyi) pupae, Food Chem. Toxicol. 44(7) (2006) 1123-1130. https://doi.org/10.1016/j.fct.2006.01.009.

[19]

X.T. Li, H.Q. Xie, Y.J. Chen, et al., Silkworm pupa protein hydrolysate induces mitochondria-dependent apoptosis and S phase cell cycle arrest in human gastric cancer SGC-7901 cells, Int. J. Mol. Sci. 19(4) (2018) 1013. https://doi.org/10.3390/ijms19041013.

[20]

S.R. Mitchell, K. Larkin, N.R. Grieselhuber, et al., Selective targeting of NAMPT by KPT-9274 in acute myeloid leukemia, Blood Adv. 3(3) (2019) 242-255. https://doi.org/10.1182/bloodadvances.2018024182.

[21]

C. Yang, S. Wang, H. Ruan, et al., Downregulation of PDK4 increases lipogenesis and associates with poor prognosis in hepatocellular carcinoma, Cancer 10(4) (2019) 918-926. https://doi.org/10.7150/jca.27226.

[22]

C.L. Wang, Application of extracellular flux analyzer in the studies of cancer cell metabolism, Chin. J. Cell Biol. (38) (2016) 1066-1076.

[23]

L. Zhen, S.C. Zang, J.F. Wang, et al., Effects of miR-383-5p-down-regulation in hepatocyte on energy metabolism based on cold stress, Chin. J. Vet. Sci. 39(6) (2019) 1163-1169.

[24]

B.D. Pence, J.R. Yarbro, Classical monocytes maintain ex vivo glycolytic metabolism and early but not later inflammatory responses in older adults, Immun. Ageing 16(1) (2019) 3. https://doi.org/10.1186/s12979-019-0143-1.

[25]

O. Warburg, On the origin of cancer cells, Science 123(3191) (1956) 309-314. https://doi.org/10.1126/science.123.3191.309.

[26]

F. Bray, J. Ferlay, I. Soerjomataram, et al., Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries, CA Cancer J. Clin. 68(6) (2018) 394-424. https://doi.org/10.3322/caac.21492.

[27]

C. Fitzmaurice, D. Abate, N. Abbasi, et al. Global, regional, and national cancer incidence, mortality, years of life lost, years lived with disability, and disability-adjusted life-years for 29 cancer groups, 1990 to 2016: a systematic analysis for the global burden of disease study, JAMA Oncol. 4(11) (2018) 1553-1568. https://doi.org/10.1001/jamaoncol.2019.2996.

[28]

M.A. Blanco, J.A. Gutierrez, P.M. Perez, et al., From amino acid sequence to bioactivity: scientific evidence on antitumor peptides, Protein Sci. 25 (2016) 1084-1095.

[29]

T.G. Cotter, Apoptosis and cancer: the genesis of a research field, Nature Reviews Cancer 9(7) (2009) 501-507. https://doi.org/10.1002/pro.2927.

[30]

H. Nishijima, A. Kosaihira, J. Shibata, et al., Development of signaling echomethod for cell-based quantitative efficacy evaluation of anti-cancer drugs in apoptosis without drug presence using high-precision surface plasmon resonance sensing, Anal. Sci. 26(5) (2010) 529-534. https://doi.org/10.2116/analsci.26.529.

[31]

S.H. Cho, K.S. Chung, J.H. Choi, et al., Compound K, a metabolite of ginseng saponin, induces apoptosis via caspase-8-dependent pathway in HL-60 human leukemia cells, BMC Cancel 9 (2009) 449. https://doi.org/10.1186/1471-2407-9-449.

Publication history
Copyright
Rights and permissions

Publication history

Received: 11 December 2020
Revised: 21 December 2020
Accepted: 30 December 2020
Published: 02 June 2022
Issue date: September 2022

Copyright

© 2022 Beijing Academy of Food Sciences.

Rights and permissions

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Return