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불레기말(Colpomenia sinuosa)의 최종당화산물 저해 효능 및 신장 보호 효과

Anti-glycation effect and renal protective activity of Colpomenia sinuosa extracts against advanced glycation end-products (AGEs)

  • 김민경 (과학기술연합대학원대학교 식품생명공학전공) ;
  • 조치흥 (한국식품연구원 식품기능연구본부) ;
  • 김세라 (한국식품연구원 식품기능연구본부) ;
  • 최인욱 (한국식품연구원 식품기능연구본부) ;
  • 이상훈 (한국식품연구원 식품기능연구본부)
  • Kim, Mingyeong (Department of Food Biotechnology, University of Science and Technology) ;
  • Cho, Chi Heung (Division of Food Functionality Research, Korea Food Research Institute) ;
  • Kim, Sera (Division of Food Functionality Research, Korea Food Research Institute) ;
  • Choi, In-Wook (Division of Food Functionality Research, Korea Food Research Institute) ;
  • Lee, Sang-Hoon (Division of Food Functionality Research, Korea Food Research Institute)
  • 투고 : 2021.11.22
  • 심사 : 2021.12.24
  • 발행 : 2021.12.31

초록

Here, we evaluated the anti-glycation effects and renal protective properties of 70% (v/v) ethanolic extract of Colpomenia sinuosa (CSE) against AGEs -induced oxidative stress and apoptosis at different concentrations (1, 5, and 20 ㎍/mL). At 20 ㎍/mL, CSE showed that anti-glycation activities via the inhibition of AGE formation (51.1%), inhibition of AGEs-protein cross-linking (61.7%), and breaking of AGEs-protein cross-links (33.3%), were significantly (###p < 0.001 vs. non-treated group) lower than the nontreated group. Methylglyoxal (MGO) significantly (***p < 0.001) reduced cell viability (24.4%) and increased reactive oxygen species (ROS) level (642.3%), MGO accumulation (119.4 ㎍/mL), and apoptosis (55.0%) in mesangial cells compared to the nontreated group. Pretreatment with CSE significantly (###p < 0.001) increased cell viability (57.8%) and decreased intracellular ROS (96.5%), MGO accumulation (80.0 ㎍/mL), and apoptosis (22.6%) at 20 ㎍/mL. Additionally, we confirmed intracellular AGEs reduction by CSE pretreatment. Consequently, our results suggest that CSE is a good source of natural therapeutics for managing diabetic complications by the antiglycation effect and renal protective activity against MGO-induced oxidative stress.

키워드

과제정보

본 연구성과는 정부(과학기술정보통신부)의 재원으로 한국연구재단(NRF-2020R1A2C201260811)의 지원을 받아 수행된 연구임

참고문헌

  1. Rabbani, N. and P.J. Thornalley, 2018. Advanced glycation end products in the pathogenesis of chronic kidney disease. Kidney international, 93. 803-813.
  2. Rowan, S., E. Bejarano and A. Taylor, 2018. Mechanistic targeting of advanced glycation end-products in age-related diseases. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1864. 3631-3643. https://doi.org/10.1016/j.bbadis.2018.08.036
  3. Vistoli, G., D. De Maddis, A. Cipak, N. Zarkovic, M. Carini and G. Aldini, 2013. Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation. Free radical research, 47. 3-27. https://doi.org/10.3109/10715762.2013.815348
  4. Huebschmann, A.G., J.G. Regensteiner, H. Vlassara and J.E. Reusch, 2006. Diabetes and advanced glycoxidation end products. Diabetes care, 29. 1420-1432. https://doi.org/10.2337/dc05-2096
  5. Khalifah, R.G., J.W. Baynes and B.G. Hudson, 1999. Amadorins: novel post-Amadori inhibitors of advanced glycation reactions. Biochemical and biophysical research communications, 257. 251-258. https://doi.org/10.1006/bbrc.1999.0371
  6. Edelstein, D. and M. Brownlee, 1992. Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine. Diabetes, 41. 26-29. https://doi.org/10.2337/diab.41.1.26
  7. Thornalley, P.J., 2003. Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts. Archives of biochemistry and biophysics, 419. 31-40. https://doi.org/10.1016/j.abb.2003.08.013
  8. El Gamal, A.A., 2010. Biological importance of marine algae. Saudi pharmaceutical journal, 18. 1-25. https://doi.org/10.1016/j.jsps.2009.12.001
  9. Lee, C.-H., Y.N. Park and S.G. Lee, 2020. Analysis and comparison of bioactive compounds and total antioxidant capabilities of Korean brown algae. Korean Journal of Food Science and Technology, 52. 54-59. https://doi.org/10.9721/KJFST.2020.52.1.54
  10. Pangestuti, R. and S.-K. Kim, 2011. Biological activities and health benefit effects of natural pigments derived from marine algae. Journal of functional foods, 3. 255-266. https://doi.org/10.1016/j.jff.2011.07.001
  11. Ponnudurai, G. and J.J.P. Paul, 2020. GC-MS Analysis of Methanolic Extract of Colpomenia Sinuosa (Mertens Ex Roth) Derb. Et Sol. From Manapad in the South East Coast of Tamil Nadu, India. Asian Journal of Pharmaceutical Research and Development, 8. 41-43.
  12. Lekameera, R., P. Vijayabaskar and S. Somasundaram, 2013. Evaluating antioxidant property of brown alga Colpomenia sinuosa (DERB. ET SOL). African Journal of Food Science, 2. 126-130.
  13. Ramarajan, L., S.T. Somasundaram, S. Subramanian and V. Pandian, 2012. Nephroprotective effects of Colpomenia sinuosa (Derbes & Solier) against carbon tetrachloride induced kidney injury in Wistar rats. Asian Pacific Journal of Tropical Disease, 2. S435-S441. https://doi.org/10.1016/S2222-1808(12)60199-6
  14. Lee, J., B. Kim, M.-H. Park, K.-H. Choi, C. Kong, S.-H. Lee, Y.Y. Kim, K.H. Yu and M. Kim, 2016. Effects of Colpomenia sinuosa extract on serum lipid level and bone formation in ovariectomized rats. Journal of the Korean Society of Food Science and Nutrition, 45. 492-500. https://doi.org/10.3746/JKFN.2016.45.4.492
  15. S.-C. Ko, S.-H. Lee, S.-M. Kang, G. Ahn, S.-H. Cha and Y.-J. Jeon, 2011. Evaluation of α-glucosidase Inhibitory Activity of Jeju Seaweeds Using High Throughput Screening (HTS) Technique, 5. 33-39. https://doi.org/10.15433/KSMB.2011.5.4.033
  16. Do, M.H., J. Hur, J. Choi, M. Kim, M.J. Kim, Y. Kim and S.K. Ha, 2018. Eucommia ulmoides ameliorates glucotoxicity by suppressing advanced glycation end-products in diabetic mice kidney. Nutrients, 10. 265. https://doi.org/10.3390/nu10030265
  17. Lee, J.-y., J.-G. Oh, J.S. Kim and K.-W. Lee, 2014. Effects of chebulic acid on advanced glycation end-products-induced collagen cross-links. Biological and Pharmaceutical Bulletin, b14-00034.
  18. Liu, Y.-W., X.-L. Liu, L. Kong, M.-Y. Zhang, Y.-J. Chen, X. Zhu and Y.-C. Hao, 2019. Neuroprotection of quercetin on central neurons against chronic high glucose through enhancement of Nrf2/ARE/glyoxalase-1 pathway mediated by phosphorylation regulation. Biomedicine & Pharmacotherapy, 109. 2145-2154. https://doi.org/10.1016/j.biopha.2018.11.066
  19. Kim, M., C.H. Cho, G.H. Youm, Y. Park and S.-H. Lee, 2020. Glycation inhibitory effect and renal protective ability of Hizikia Fusiformis extracts against advanced glycation end-products (AGEs). Journal of Chitin and Chitosan 25. 175-183.
  20. Kim, M., C. Cho, C. Lee, B. Ryu, S. Kim, J. Hur and S.-H. Lee, 2021. Ishige okamurae Ameliorates Methylglyoxal-Induced Nephrotoxicity via Reducing Oxidative Stress, RAGE Protein Expression, and Modulating MAPK, Nrf2/ARE Signaling Pathway in Mouse Glomerular Mesangial Cells. Foods, 10. 2000. https://doi.org/10.3390/foods10092000
  21. Cho, C.H., M. Kim, G.H. Youm, S. Kim, Y. Park and S.-h. Lee, 2020. Advanced glycation end-products inhibitory activities and renoprotective effects of Ishige foliacea ethanolic extract. Journal of Chitin and Chitosan, 25. 134-142. https://doi.org/10.17642/jcc.25.3.4
  22. Cove-Smith, A. and B.M. Hendry, 2008. The regulation of mesangial cell proliferation. Nephron Experimental Nephrology, 108. e74-e79. https://doi.org/10.1159/000127359
  23. Olivetti, G., P. Anversa, W. Rigamonti, L. Vitali-Mazza and A.V. Loud, 1977. Morphometry of the renal corpuscle during normal postnatal growth and compensatory hypertrophy. A light microscope study. Journal of Cell Biology, 75. 573-585. https://doi.org/10.1083/jcb.75.2.573
  24. Stockand, J.D. and S.C. Sansom, 1998. Glomerular mesangial cells: electrophysiology and regulation of contraction. Physiological reviews, 78. 723-744. https://doi.org/10.1152/physrev.1998.78.3.723
  25. Redza-Dutordoir, M. and D.A. Averill-Bates,2016. Activation of apoptosis signalling pathways by reactive oxygen species. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1863. 2977-2992. https://doi.org/10.1016/j.bbamcr.2016.09.012
  26. van Engeland, M., F.C. Ramaekers, B. Schutte and C.P. Reutelingsperger, 1996. A novel assay to measure loss of plasma membrane asymmetry during apoptosis of adherent cells in culture. Cytometry: The Journal of the International Society for Analytical Cytology, 24. 131-139. https://doi.org/10.1002/(SICI)1097-0320(19960601)24:2<131::AID-CYTO5>3.0.CO;2-M
  27. Riccardi, C. and I. Nicoletti, 2006. Analysis of apoptosis by propidium iodide staining and flow cytometry. Nature protocols, 1. 1458-1461. https://doi.org/10.1038/nprot.2006.238
  28. Sena, C.M., P. Matafome, J. Crisostomo, L. Rodrigues, R. Fernandes, P. Pereira and R.M. Seica, 2012. Methylglyoxal promotes oxidative stress and endothelial dysfunction. Pharmacological Research, 65. 497-506. https://doi.org/10.1016/j.phrs.2012.03.004
  29. Yang, M., J. Fan, J. Zhang, J. Du and X. Peng, 2018. Visualization of methylglyoxal in living cells and diabetic mice model with a 1, 8-naphthalimide-based two-photon fluorescent probe. Chemical science, 9. 6758-6764. https://doi.org/10.1039/c8sc02578a
  30. Liu, B.-F., S. Miyata, Y. Hirota, S. Higo, H. Miyazaki, M. Fukunaga, Y. Hamada, S. Ueyama, O. Muramoto and A. Uriuhara, 2003. Methylglyoxal induces apoptosis through activation of p38 mitogen-activated protein kinase in rat mesangial cells. Kidney international, 63. 947-957. https://doi.org/10.1046/j.1523-1755.2003.00829.x
  31. Doonan, F. and T.G. Cotter, 2008. Morphological assessment of apoptosis. Methods, 44. 200-204. https://doi.org/10.1016/j.ymeth.2007.11.006