Roe Protein Hydrolysates of Giant Grouper (Epinephelus lanceolatus) Inhibit Cell Proliferation of Oral Cancer Cells Involving Apoptosis and Oxidative Stress

J.-I. Yang; J.-Y. Tang; Y.-S. Liu; H.-R. Wang; S.-Y. Lee; C.-Y. Yen; H.-W. Chang

doi:10.1155/2016/8305073

Roe Protein Hydrolysates of Giant Grouper (Epinephelus lanceolatus) Inhibit Cell Proliferation of Oral Cancer Cells Involving Apoptosis and Oxidative Stress

J.-I. Yang, J.-Y. Tang, Y.-S. Liu, H.-R. Wang, S.-Y. Lee, C.-Y. Yen, H.-W. Chang

Research output: Contribution to journal › Article › peer-review

34 Citations (Scopus)

Abstract

Roe protein hydrolysates were reported to have antioxidant property but the anticancer effects were less addressed, especially for oral cancer. In this study, we firstly used the ultrafiltrated roe hydrolysates (URH) derived from giant grouper (Epinephelus lanceolatus) to evaluate the impact of URH on proliferation against oral cancer cells. We found that URH dose-responsively reduced cell viability of two oral cancer cells (Ca9-22 and CAL 27) in terms of ATP assay. Using flow cytometry, URH-induced apoptosis of Ca9-22 cells was validated by morphological features of apoptosis, sub-G1 accumulation, and annexin V staining in dose-responsive manners. URH also induced oxidative stress in Ca9-22 cells in terms of reactive oxygen species (ROS)/superoxide generations and mitochondrial depolarization. Taken together, these data suggest that URH is a potential natural product for antioral cancer therapy. © 2016 Jing-Iong Yang et al.

Original language	English
Journal	BioMed Research International
Volume	2016
DOIs	https://doi.org/10.1155/2016/8305073
Publication status	Published - 2016

Keywords

lipocortin 5
protein hydrolysate
reactive oxygen metabolite
superoxide
ultrafiltrated roe hydrolysate
unclassified drug
apoptosis
Article
cell proliferation
cell viability
controlled study
dose response
Epinephelus
Epinephelus lanceolatus
flow cytometry
human
human cell
mitochondrial membrane potential
mouth cancer
oral cancer cell line
oxidative stress
ultrafiltration

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1155/2016/8305073

https://www.scopus.com/inward/record.uri?eid=2-s2.0-84971536992&partnerID=40&md5=6a0528ec0ad068ab8747dd416dded337

Cite this

@article{db8ebb4367114dbc84d8f23f7102927b,

title = "Roe Protein Hydrolysates of Giant Grouper (Epinephelus lanceolatus) Inhibit Cell Proliferation of Oral Cancer Cells Involving Apoptosis and Oxidative Stress",

abstract = "Roe protein hydrolysates were reported to have antioxidant property but the anticancer effects were less addressed, especially for oral cancer. In this study, we firstly used the ultrafiltrated roe hydrolysates (URH) derived from giant grouper (Epinephelus lanceolatus) to evaluate the impact of URH on proliferation against oral cancer cells. We found that URH dose-responsively reduced cell viability of two oral cancer cells (Ca9-22 and CAL 27) in terms of ATP assay. Using flow cytometry, URH-induced apoptosis of Ca9-22 cells was validated by morphological features of apoptosis, sub-G1 accumulation, and annexin V staining in dose-responsive manners. URH also induced oxidative stress in Ca9-22 cells in terms of reactive oxygen species (ROS)/superoxide generations and mitochondrial depolarization. Taken together, these data suggest that URH is a potential natural product for antioral cancer therapy. {\textcopyright} 2016 Jing-Iong Yang et al.",

keywords = "lipocortin 5, protein hydrolysate, reactive oxygen metabolite, superoxide, ultrafiltrated roe hydrolysate, unclassified drug, apoptosis, Article, cell proliferation, cell viability, controlled study, dose response, Epinephelus, Epinephelus lanceolatus, flow cytometry, human, human cell, mitochondrial membrane potential, mouth cancer, oral cancer cell line, oxidative stress, ultrafiltration",

author = "J.-I. Yang and J.-Y. Tang and Y.-S. Liu and H.-R. Wang and S.-Y. Lee and C.-Y. Yen and H.-W. Chang",

note = "Export Date: 9 August 2016 通訊地址: Yen, C.-Y.; School of Dentistry, Taipei Medical UniversityTaiwan; 電子郵件： [email protected] 化學物質/CAS: lipocortin 5, 111237-10-6; protein hydrolysate, 76773-71-2, 9015-54-7; superoxide, 11062-77-4 出資詳情: 104-2320-B-037-013-MY3, MOST, Ministry of Science and Technology 參考文獻: Warnakulasuriya, S., Global epidemiology of oral and oropharyngeal cancer (2009) Oral Oncology, 45 (4-5), pp. 309-316; Petersen, P.E., Oral cancer prevention and control-the approach of the World Health Organization (2009) Oral Oncology, 45 (4-5), pp. 454-460; Yen, C.-Y., Huang, C.-Y., Hou, M.-F., Evaluating the performance of fibronectin 1 (FN1), integrin 41 (ITGA4), syndecan-2 (SDC2), and glycoprotein CD44 as the potential biomarkers of oral squamous cell carcinoma (OSCC) (2013) Biomarkers, 18 (1), pp. 63-72; Tanaka, T., Tanaka, M., Tanaka, T., Oral carcinogenesis and oral cancer chemoprevention: A review (2011) Pathology Research International, 2011, 10p; Yang, J.-I., Ho, H.-Y., Chu, Y.-J., Chow, C.-J., Characteristic and antioxidant activity of retorted gelatin hydrolysates from cobia (Rachycentron canadum) skin (2008) Food Chemistry, 110 (1), pp. 128-136; Yang, J.-I., Liang, W.-S., Chow, C.-J., Siebert, K.J., Process for the production of tilapia retorted skin gelatin hydrolysates with optimized antioxidative properties (2009) Process Biochemistry, 44 (10), pp. 1152-1157; Chow, C.-J., Yang, J.-I., The effect of process variables for production of cobia (Rachycentron canadum) skin gelatin hydrolysates with antioxidant properties (2008) Journal of Food Biochemistry, 35 (3), pp. 715-734; Li, X., Luo, Y., Shen, H., You, J., Antioxidant activities and functional properties of grass carp (Ctenopharyngodon idellus) protein hydrolysates (2012) Journal of the Science of Food and Agriculture, 92 (2), pp. 292-298; Elavarasan, K., Naveen Kumar, V., Shamasundar, B.A., Antioxidant and functional properties of fish protein hydrolysates from fresh water carp (Catla catla) as influenced by the nature of enzyme (2014) Journal of Food Processing and Preservation, 38 (3), pp. 1207-1214; Chalamaiah, M., Dinesh Kumar, B., Hemalatha, R., Jyothirmayi, T., Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: A review (2012) Food Chemistry, 135 (4), pp. 3020-3038; Balaswamy, K., Prabhakara Rao, P.G., Narsing Rao, G., Jyothirmayi, T., Functional properties of roe protein hydrolysates from Catla catla (2011) Electronic Journal of Environmental, Agricultural, and Food Chemistry, 10, pp. 2139-2147; Galla, N.R., Pamidighantam, P.R., Akula, S., Karakala, B., Functional properties and in vitro antioxidant activity of roe protein hydrolysates of Channa striatus and Labeo rohita (2012) Food Chemistry, 135 (3), pp. 1479-1484; Rao, G.N., Physico-chemical, functional and antioxidant properties of roe protein concentrates from Cyprinus carpio and Epinephelus tauvina (2014) Journal of Food and Pharmaceutical Sciences, 2 (1), pp. 15-22; Lee, J.-C., Hou, M.-F., Huang, H.-W., Marine algal natural products with anti-oxidative, anti-inflammatory, and anticancer properties (2013) Cancer Cell International, 13; Najafian, L., Babji, A.S., A review of fish-derived antioxidant and antimicrobial peptides: Their production, assessment, and applications (2012) Peptides, 33 (1), pp. 178-185; Yen, C.-Y., Hou, M.-F., Yang, Z.-W., Concentration effects of grape seed extracts in anti-oral cancer cells involving differential apoptosis, oxidative stress, and DNA damage (2015) BMC Complementary and Alternative Medicine, 15; Yeh, C.-C., Tseng, C.-N., Yang, J.-I., Antiproliferation and induction of apoptosis in Ca9-22 oral cancer cells by ethanolic extract of Gracilaria tenuistipitata (2012) Molecules, 17 (9), pp. 10916-10927; Yen, Y.-H., Farooqi, A.A., Li, K.-T., Methanolic extracts of Solieria robusta inhibits proliferation of oral cancer Ca9-22 cells via apoptosis and oxidative stress (2014) Molecules, 19 (11), pp. 18721-18732; Yeh, C.-C., Yang, J.-I., Lee, J.-C., Anti-proliferative effect of methanolic extract of Gracilaria tenuistipitata on oral cancer cells involves apoptosis, DNA damage, and oxidative stress (2012) BMC Complementary and Alternative Medicine, 12; Picot, L., Bordenave, S., Didelot, S., Antiproliferative activity of fish protein hydrolysates on human breast cancer cell lines (2006) Process Biochemistry, 41 (5), pp. 1217-1222; You, L., Zhao, M., Liu, R.H., Regenstein, J.M., Antioxidant and antiproliferative activities of loach (Misgurnus anguillicaudatus) peptides prepared by papain digestion (2011) Journal of Agricultural and Food Chemistry, 59 (14), pp. 7948-7953; Chi, C.-F., Hu, F.-Y., Wang, B., Li, T., Ding, G.-F., Antioxidant and anticancer peptides from the protein hydrolysate of blood clam (Tegillarca granosa) muscle (2015) Journal of Functional Foods, 15, pp. 301-313; Umayaparvathi, S., Meenakshi, S., Vimalraj, V., Arumugam, M., Sivagami, G., Balasubramanian, T., Antioxidant activity and anticancer effect of bioactive peptide from enzymatic hydrolysate of oyster (Saccostrea cucullata) (2014) Biomedicine & Preventive Nutrition, 4 (3), pp. 343-353; Xue, Z.H., Wen, H.C., Zhai, L.J.Y., Antioxidant activity and anti-proliferative effect of a bioactive peptide fromchickpea (Cicer arietinum L. ) (2015) Food Research International, 77, pp. 75-81; Hseu, J.-R., Hwang, P.-P., Ting, Y.-Y., Morphometric model and laboratory analysis of intracohort cannibalism in giant grouper Epinephelus lanceolatus fry (2004) Fisheries Science, 70 (3), pp. 482-486; Bligh, E.G., Dyer, W.J., A rapid method of total lipid extraction and purification (1959) Canadian Journal of Biochemistry and Physiology, 37 (8), pp. 911-917; Sato, K., Tsukamasa, Y., Imai, C., Ohtsuki, K., Shimizu, Y., Kawabata, M., Improved method for identification and determination of-(-glutamyl)-lysine cross-link in protein using proteolytic digestion and derivatization with phenyl isothiocyanate followed by high performance liquid chromatography separation (1992) Journal of Agricultural and FoodChemistry, 40, pp. 806-810; Jiang, L., Ji, N., Zhou, Y., CAL 27 is an oral adenosquamous carcinoma cell line (2009) Oral Oncology, 45 (11), pp. e204-e207; Wei, J., Stebbins, J.L., Kitada, S., An optically pure apogossypolone derivative as potent pan-active inhibitor of anti-apoptotic Bcl-2 family proteins (2011) Frontiers in Oncology, 1; Chen, B.-H., Chang, H.-W., Huang, H.-M., Anonaine induces DNA damage and inhibits growth and migration of human lung carcinoma H1299 cells (2011) Journal of Agricultural and Food Chemistry, 59 (6), pp. 2284-2290; Chiu, C.-C., Liu, P.-L., Huang, K.-J., Goniothalamin inhibits growth of human lung cancer cells through DNA damage, apoptosis, and reduced migration ability (2011) Journal of Agricultural and Food Chemistry, 59 (8), pp. 4288-4293; Mukhopadhyay, P., Rajesh, M., Yoshihiro, K., Hask{\'o}, G., Pacher, P., Simple quantitative detection of mitochondrial superoxide production in live cells (2007) Biochemical and Biophysical Research Communications, 358 (1), pp. 203-208; Li, R., Jen, N., Yu, F., Hsiai, T.K., Assessing mitochondrial redox status by flow cytometric methods: Vascular response to fluid shear stress (2011) Current Protocols in Cytometry, Chapter 9, , unit 9. 37; Yen, C.-Y., Chiu, C.-C., Haung, R.-W., Antiproliferative effects of goniothalamin on Ca9-22 oral cancer cells through apoptosis, DNAdamage and ROS induction (2012) Mutation Research/Genetic Toxicology and Environmental Mutagenesis, 747 (2), pp. 253-258; Yen, C.-Y., Lin, M.-H., Liu, S.-Y., Arecoline-mediated inhibition ofAMP-activated protein kinase through reactive oxygen species is required for apoptosis induction (2011) Oral Oncology, 47 (5), pp. 345-351; Han, M.H., Park, C., Jin, C.-Y., Apoptosis induction of human bladder cancer cells by sanguinarine through reactive oxygen species-mediated up-regulation of early growth response gene-1 (2013) PLoS ONE, 8 (5); Raj, L., Ide, T., Gurkar, A.U., Selective killing of cancer cells by a small molecule targeting the stress response to ROS (2011) Nature, 475 (7355), pp. 231-234; Ding, H., Han, C., Guo, D., Selective induction of apoptosis of human oral cancer cell lines by avocado extracts via a ROSmediated mechanism (2009) Nutrition and Cancer, 61 (3), pp. 348-356; Kannan, A., Hettiarachchy, N.S., Marshall, M., Raghavan, S., Kristinsson, H., Shrimp shell peptide hydrolysates inhibit human cancer cell proliferation (2011) Journal of the Science of Food and Agriculture, 91 (10), pp. 1920-1924; Bouayed, J., Bohn, T., Exogenous antioxidants-doubleedged swords in cellular redox state: Health beneficial effects at physiologic doses versus deleterious effects at high doses (2010) OxidativeMedicine and Cellular Longevity, 3 (4), pp. 228-237; Farooqi, A.A., Li, K.-T., Fayyaz, S., Anticancer drugs for the modulation of endoplasmic reticulum stress and oxidative stress (2015) Tumor Biology, 36 (8), pp. 5743-5752; Farooqi, A.A., Fayyaz, S., Hou, M.-F., Li, K.-T., Tang, J.-Y., Chang, H.-W., Reactive oxygen species and autophagymodulation in non-marine drugs and marine drugs (2014) Marine Drugs, 12 (11), pp. 5408-5424; Mat{\'e}s, J.M., Segura, J.A., Alonso, F.J., M{\'a}rquez, J., Oxidative stress in apoptosis and cancer: An update (2012) Archives of Toxicology, 86 (11), pp. 1649-1665",

year = "2016",

doi = "10.1155/2016/8305073",

language = "English",

volume = "2016",

journal = "BioMed Research International",

issn = "2314-6133",

publisher = "John Wiley and Sons Ltd",

}

TY - JOUR

T1 - Roe Protein Hydrolysates of Giant Grouper (Epinephelus lanceolatus) Inhibit Cell Proliferation of Oral Cancer Cells Involving Apoptosis and Oxidative Stress

AU - Yang, J.-I.

AU - Tang, J.-Y.

AU - Liu, Y.-S.

AU - Wang, H.-R.

AU - Lee, S.-Y.

AU - Yen, C.-Y.

AU - Chang, H.-W.

N1 - Export Date: 9 August 2016 通訊地址: Yen, C.-Y.; School of Dentistry, Taipei Medical UniversityTaiwan; 電子郵件： [email protected] 化學物質/CAS: lipocortin 5, 111237-10-6; protein hydrolysate, 76773-71-2, 9015-54-7; superoxide, 11062-77-4 出資詳情: 104-2320-B-037-013-MY3, MOST, Ministry of Science and Technology 參考文獻: Warnakulasuriya, S., Global epidemiology of oral and oropharyngeal cancer (2009) Oral Oncology, 45 (4-5), pp. 309-316; Petersen, P.E., Oral cancer prevention and control-the approach of the World Health Organization (2009) Oral Oncology, 45 (4-5), pp. 454-460; Yen, C.-Y., Huang, C.-Y., Hou, M.-F., Evaluating the performance of fibronectin 1 (FN1), integrin 41 (ITGA4), syndecan-2 (SDC2), and glycoprotein CD44 as the potential biomarkers of oral squamous cell carcinoma (OSCC) (2013) Biomarkers, 18 (1), pp. 63-72; Tanaka, T., Tanaka, M., Tanaka, T., Oral carcinogenesis and oral cancer chemoprevention: A review (2011) Pathology Research International, 2011, 10p; Yang, J.-I., Ho, H.-Y., Chu, Y.-J., Chow, C.-J., Characteristic and antioxidant activity of retorted gelatin hydrolysates from cobia (Rachycentron canadum) skin (2008) Food Chemistry, 110 (1), pp. 128-136; Yang, J.-I., Liang, W.-S., Chow, C.-J., Siebert, K.J., Process for the production of tilapia retorted skin gelatin hydrolysates with optimized antioxidative properties (2009) Process Biochemistry, 44 (10), pp. 1152-1157; Chow, C.-J., Yang, J.-I., The effect of process variables for production of cobia (Rachycentron canadum) skin gelatin hydrolysates with antioxidant properties (2008) Journal of Food Biochemistry, 35 (3), pp. 715-734; Li, X., Luo, Y., Shen, H., You, J., Antioxidant activities and functional properties of grass carp (Ctenopharyngodon idellus) protein hydrolysates (2012) Journal of the Science of Food and Agriculture, 92 (2), pp. 292-298; Elavarasan, K., Naveen Kumar, V., Shamasundar, B.A., Antioxidant and functional properties of fish protein hydrolysates from fresh water carp (Catla catla) as influenced by the nature of enzyme (2014) Journal of Food Processing and Preservation, 38 (3), pp. 1207-1214; Chalamaiah, M., Dinesh Kumar, B., Hemalatha, R., Jyothirmayi, T., Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: A review (2012) Food Chemistry, 135 (4), pp. 3020-3038; Balaswamy, K., Prabhakara Rao, P.G., Narsing Rao, G., Jyothirmayi, T., Functional properties of roe protein hydrolysates from Catla catla (2011) Electronic Journal of Environmental, Agricultural, and Food Chemistry, 10, pp. 2139-2147; Galla, N.R., Pamidighantam, P.R., Akula, S., Karakala, B., Functional properties and in vitro antioxidant activity of roe protein hydrolysates of Channa striatus and Labeo rohita (2012) Food Chemistry, 135 (3), pp. 1479-1484; Rao, G.N., Physico-chemical, functional and antioxidant properties of roe protein concentrates from Cyprinus carpio and Epinephelus tauvina (2014) Journal of Food and Pharmaceutical Sciences, 2 (1), pp. 15-22; Lee, J.-C., Hou, M.-F., Huang, H.-W., Marine algal natural products with anti-oxidative, anti-inflammatory, and anticancer properties (2013) Cancer Cell International, 13; Najafian, L., Babji, A.S., A review of fish-derived antioxidant and antimicrobial peptides: Their production, assessment, and applications (2012) Peptides, 33 (1), pp. 178-185; Yen, C.-Y., Hou, M.-F., Yang, Z.-W., Concentration effects of grape seed extracts in anti-oral cancer cells involving differential apoptosis, oxidative stress, and DNA damage (2015) BMC Complementary and Alternative Medicine, 15; Yeh, C.-C., Tseng, C.-N., Yang, J.-I., Antiproliferation and induction of apoptosis in Ca9-22 oral cancer cells by ethanolic extract of Gracilaria tenuistipitata (2012) Molecules, 17 (9), pp. 10916-10927; Yen, Y.-H., Farooqi, A.A., Li, K.-T., Methanolic extracts of Solieria robusta inhibits proliferation of oral cancer Ca9-22 cells via apoptosis and oxidative stress (2014) Molecules, 19 (11), pp. 18721-18732; Yeh, C.-C., Yang, J.-I., Lee, J.-C., Anti-proliferative effect of methanolic extract of Gracilaria tenuistipitata on oral cancer cells involves apoptosis, DNA damage, and oxidative stress (2012) BMC Complementary and Alternative Medicine, 12; Picot, L., Bordenave, S., Didelot, S., Antiproliferative activity of fish protein hydrolysates on human breast cancer cell lines (2006) Process Biochemistry, 41 (5), pp. 1217-1222; You, L., Zhao, M., Liu, R.H., Regenstein, J.M., Antioxidant and antiproliferative activities of loach (Misgurnus anguillicaudatus) peptides prepared by papain digestion (2011) Journal of Agricultural and Food Chemistry, 59 (14), pp. 7948-7953; Chi, C.-F., Hu, F.-Y., Wang, B., Li, T., Ding, G.-F., Antioxidant and anticancer peptides from the protein hydrolysate of blood clam (Tegillarca granosa) muscle (2015) Journal of Functional Foods, 15, pp. 301-313; Umayaparvathi, S., Meenakshi, S., Vimalraj, V., Arumugam, M., Sivagami, G., Balasubramanian, T., Antioxidant activity and anticancer effect of bioactive peptide from enzymatic hydrolysate of oyster (Saccostrea cucullata) (2014) Biomedicine & Preventive Nutrition, 4 (3), pp. 343-353; Xue, Z.H., Wen, H.C., Zhai, L.J.Y., Antioxidant activity and anti-proliferative effect of a bioactive peptide fromchickpea (Cicer arietinum L. ) (2015) Food Research International, 77, pp. 75-81; Hseu, J.-R., Hwang, P.-P., Ting, Y.-Y., Morphometric model and laboratory analysis of intracohort cannibalism in giant grouper Epinephelus lanceolatus fry (2004) Fisheries Science, 70 (3), pp. 482-486; Bligh, E.G., Dyer, W.J., A rapid method of total lipid extraction and purification (1959) Canadian Journal of Biochemistry and Physiology, 37 (8), pp. 911-917; Sato, K., Tsukamasa, Y., Imai, C., Ohtsuki, K., Shimizu, Y., Kawabata, M., Improved method for identification and determination of-(-glutamyl)-lysine cross-link in protein using proteolytic digestion and derivatization with phenyl isothiocyanate followed by high performance liquid chromatography separation (1992) Journal of Agricultural and FoodChemistry, 40, pp. 806-810; Jiang, L., Ji, N., Zhou, Y., CAL 27 is an oral adenosquamous carcinoma cell line (2009) Oral Oncology, 45 (11), pp. e204-e207; Wei, J., Stebbins, J.L., Kitada, S., An optically pure apogossypolone derivative as potent pan-active inhibitor of anti-apoptotic Bcl-2 family proteins (2011) Frontiers in Oncology, 1; Chen, B.-H., Chang, H.-W., Huang, H.-M., Anonaine induces DNA damage and inhibits growth and migration of human lung carcinoma H1299 cells (2011) Journal of Agricultural and Food Chemistry, 59 (6), pp. 2284-2290; Chiu, C.-C., Liu, P.-L., Huang, K.-J., Goniothalamin inhibits growth of human lung cancer cells through DNA damage, apoptosis, and reduced migration ability (2011) Journal of Agricultural and Food Chemistry, 59 (8), pp. 4288-4293; Mukhopadhyay, P., Rajesh, M., Yoshihiro, K., Haskó, G., Pacher, P., Simple quantitative detection of mitochondrial superoxide production in live cells (2007) Biochemical and Biophysical Research Communications, 358 (1), pp. 203-208; Li, R., Jen, N., Yu, F., Hsiai, T.K., Assessing mitochondrial redox status by flow cytometric methods: Vascular response to fluid shear stress (2011) Current Protocols in Cytometry, Chapter 9, , unit 9. 37; Yen, C.-Y., Chiu, C.-C., Haung, R.-W., Antiproliferative effects of goniothalamin on Ca9-22 oral cancer cells through apoptosis, DNAdamage and ROS induction (2012) Mutation Research/Genetic Toxicology and Environmental Mutagenesis, 747 (2), pp. 253-258; Yen, C.-Y., Lin, M.-H., Liu, S.-Y., Arecoline-mediated inhibition ofAMP-activated protein kinase through reactive oxygen species is required for apoptosis induction (2011) Oral Oncology, 47 (5), pp. 345-351; Han, M.H., Park, C., Jin, C.-Y., Apoptosis induction of human bladder cancer cells by sanguinarine through reactive oxygen species-mediated up-regulation of early growth response gene-1 (2013) PLoS ONE, 8 (5); Raj, L., Ide, T., Gurkar, A.U., Selective killing of cancer cells by a small molecule targeting the stress response to ROS (2011) Nature, 475 (7355), pp. 231-234; Ding, H., Han, C., Guo, D., Selective induction of apoptosis of human oral cancer cell lines by avocado extracts via a ROSmediated mechanism (2009) Nutrition and Cancer, 61 (3), pp. 348-356; Kannan, A., Hettiarachchy, N.S., Marshall, M., Raghavan, S., Kristinsson, H., Shrimp shell peptide hydrolysates inhibit human cancer cell proliferation (2011) Journal of the Science of Food and Agriculture, 91 (10), pp. 1920-1924; Bouayed, J., Bohn, T., Exogenous antioxidants-doubleedged swords in cellular redox state: Health beneficial effects at physiologic doses versus deleterious effects at high doses (2010) OxidativeMedicine and Cellular Longevity, 3 (4), pp. 228-237; Farooqi, A.A., Li, K.-T., Fayyaz, S., Anticancer drugs for the modulation of endoplasmic reticulum stress and oxidative stress (2015) Tumor Biology, 36 (8), pp. 5743-5752; Farooqi, A.A., Fayyaz, S., Hou, M.-F., Li, K.-T., Tang, J.-Y., Chang, H.-W., Reactive oxygen species and autophagymodulation in non-marine drugs and marine drugs (2014) Marine Drugs, 12 (11), pp. 5408-5424; Matés, J.M., Segura, J.A., Alonso, F.J., Márquez, J., Oxidative stress in apoptosis and cancer: An update (2012) Archives of Toxicology, 86 (11), pp. 1649-1665

PY - 2016

Y1 - 2016

N2 - Roe protein hydrolysates were reported to have antioxidant property but the anticancer effects were less addressed, especially for oral cancer. In this study, we firstly used the ultrafiltrated roe hydrolysates (URH) derived from giant grouper (Epinephelus lanceolatus) to evaluate the impact of URH on proliferation against oral cancer cells. We found that URH dose-responsively reduced cell viability of two oral cancer cells (Ca9-22 and CAL 27) in terms of ATP assay. Using flow cytometry, URH-induced apoptosis of Ca9-22 cells was validated by morphological features of apoptosis, sub-G1 accumulation, and annexin V staining in dose-responsive manners. URH also induced oxidative stress in Ca9-22 cells in terms of reactive oxygen species (ROS)/superoxide generations and mitochondrial depolarization. Taken together, these data suggest that URH is a potential natural product for antioral cancer therapy. © 2016 Jing-Iong Yang et al.

AB - Roe protein hydrolysates were reported to have antioxidant property but the anticancer effects were less addressed, especially for oral cancer. In this study, we firstly used the ultrafiltrated roe hydrolysates (URH) derived from giant grouper (Epinephelus lanceolatus) to evaluate the impact of URH on proliferation against oral cancer cells. We found that URH dose-responsively reduced cell viability of two oral cancer cells (Ca9-22 and CAL 27) in terms of ATP assay. Using flow cytometry, URH-induced apoptosis of Ca9-22 cells was validated by morphological features of apoptosis, sub-G1 accumulation, and annexin V staining in dose-responsive manners. URH also induced oxidative stress in Ca9-22 cells in terms of reactive oxygen species (ROS)/superoxide generations and mitochondrial depolarization. Taken together, these data suggest that URH is a potential natural product for antioral cancer therapy. © 2016 Jing-Iong Yang et al.

KW - lipocortin 5

KW - protein hydrolysate

KW - reactive oxygen metabolite

KW - superoxide

KW - ultrafiltrated roe hydrolysate

KW - unclassified drug

KW - apoptosis

KW - Article

KW - cell proliferation

KW - cell viability

KW - controlled study

KW - dose response

KW - Epinephelus

KW - Epinephelus lanceolatus

KW - flow cytometry

KW - human

KW - human cell

KW - mitochondrial membrane potential

KW - mouth cancer

KW - oral cancer cell line

KW - oxidative stress

KW - ultrafiltration

U2 - 10.1155/2016/8305073

DO - 10.1155/2016/8305073

M3 - Article

SN - 2314-6133

VL - 2016

JO - BioMed Research International

JF - BioMed Research International

ER -

Roe Protein Hydrolysates of Giant Grouper (Epinephelus lanceolatus) Inhibit Cell Proliferation of Oral Cancer Cells Involving Apoptosis and Oxidative Stress

Abstract

Keywords

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