DOI QR코드

DOI QR Code

Effects of Chitosan on the Induction of Renal Dipeptidase (RDPase) from the Proximal Tubules

신장의 근위세뇨관에서 Renal Dipeptidase(RDPase)의 유도에 관한 키토산의 효과

  • Kim, Young-Ho (Dept. of Natural Science, Biology, Chosun University, College of Pharmacy, Research Institute of Drug Development, Chonnam University) ;
  • Yoon, Hyun-Joong (College of Pharmacy, Research Institute of Drug Development, Chonnam University) ;
  • Park, Haeng-Soon (College of Pharmacy, Research Institute of Drug Development, Chonnam University) ;
  • Lee, Myung-Yul (Dept. of Food and Nutrition, Chosun University) ;
  • Kim, Jong-Se (Dept. of Natural Science, Biology, Chosun University)
  • 김영호 (조선대학교 자연과학대학 생물학과, 전남대학교 약학대학 약품개발연구소) ;
  • 윤현중 (전남대학교 약학대학 약품개발연구소) ;
  • 박행순 (전남대학교 약학대학 약품개발연구소) ;
  • 이명렬 (조선대학교 자연과학대학 식품영양학과) ;
  • 김종세 (조선대학교 자연과학대학 생물학과)
  • Published : 2005.08.01

Abstract

The purpose of this study was to evaluate the effects of chitosan, which is deacetylated derivative of chitin, on the renal function. Renal dipeptidase (RDPase, membrane dipeptidase, dehydropeptidase 1, EC 3.4.13.19) is glycosyl phosphatidyl-inositol (GPI)-anchored ectoenzyme of renal proximal tubular microvilli and was related with renal disease including acute renal failure, pyelitis and nephritis. The released RDPase and Udpase activities were assayed by modified fluorometric method. In vitro experimental groups were consisted of group 1, the concentration ranges of 0, 0.01, 0.05 and $0.1\%$ chitosan only, group 2, the concentration ranges of 1, 2 and 4 mM glycerol only, and group 3, the concentration ranges of 0, 0.01, 0.05 and $0.1\%$ chitosan in the presence of glycerol (4 mM). In vivo experimental groups were consisted of group 1 in which rats were treated with glycerol for the purpose of glycerol-induced renal damage, and group 2 in which rats were treated with chitosan plus glycerol. The RDPase release of 0.01, 0.05, and $0.1\%$ chitosan groups were increased in the concentration dependent manner. The RDPase release of 1, 2, and 4mM glycerol groups were decreased in the concentration dependent manner. Chitosan in the presence of glycerol restored the released RDPase activity in the proximal tubules. In vivo, chitosan inhibited the decrease of RDPase release by glycerol in the kidney and blocked the decrease of Udpase activity by glycerol in urine. These results indicated that chitosan was possible as a functional food to control renal function and its diseases.

References

  1. Riccardo AA, Muzzarelli PI, Tomasetti M. 1993. Preparation and characteristic properties of 5-methyl pyrrolidinone chitosan. Carbohydrate Polymers 20: 99-105 https://doi.org/10.1016/0144-8617(93)90084-H
  2. Hall LD, Yalpani M. 1980. Enhancement of the metal chelating properties of chitin and chitosan. Carbohydrate Res 83: 15-17
  3. Ghani SA, Hoon LL. 2002. Comparative adsorption of lead (Il) on flake and bead-types of chitosan. J Chin Chem Soc 49: 625-628 https://doi.org/10.1002/jccs.200200096
  4. Li HY. 2002. Equilibrium and kinetic modelling of adsorption of reactive dye on crosslinked chitosan beads. J Hazard Mater B93: 233-248
  5. Ruckenstein E. 1998. Cross-linked macroporous chitosan anion-exchange membranes for protein separations. J Membr Sci 148: 195-205 https://doi.org/10.1016/S0376-7388(98)00183-5
  6. Skjak G, Anthonsen T, Sandford P. 1988. Chitin and chitosan : sources, chemistry, biochemistry, physical properties and application. Elsevier. Applied. Sci, New York
  7. Boguslawski S, Bunzeit M, Knorr D. 1990. Effects of chitosan treatment on clarity and microbial counts of apple juice. Z Lebensm Technol 41: 42-44
  8. Xie WM, Xu PX, Liu Q. 2001. Antioxidant activity of watersoluble chitosan derivates. Bioorg Med Chem Lett 11: 1699-1701 https://doi.org/10.1016/S0960-894X(01)00285-2
  9. Sapers GM. 1992. Chitosan enhances control of enzymatic browning in apple and pear juice by filtration. J Food Sci 57: 1192-1193 https://doi.org/10.1111/j.1365-2621.1992.tb11296.x
  10. El-Ghaouth A, Ponnampalam R, Castaigne F, Arul J. 1992. Chitosan coating to extend the storage life of tomatoes. Hort-science 27: 1016-1018
  11. Young DH, Kohle H, Kauss H. 1982. Effect of chitosan on membrane permeability of suspension cultured Glycine max and Phaseolus vulgaris cells. Plant Physiol 70: 1449-1454 https://doi.org/10.1104/pp.70.5.1449
  12. Choi BK, Kim KY, Yoo YJ, Oh SJ, Choi JH, Kim CY. 2001. In vitro antimicrobial activity of a chitooligosaccharide mixture against Actinobacillus actinomycetemcomitans and Streptococcus mutans. Int J Aniimicrob Agents 18: 553-557 https://doi.org/10.1016/S0924-8579(01)00434-4
  13. No HK, Park NY, Lee SH, Meyers SP. 2002. Antibacterial activity of chitosans and chitosan oligomers with different molecular weights. Int J Food Microbiol 74:65-72 https://doi.org/10.1016/S0168-1605(01)00717-6
  14. Suzuki K, Mikami T, Okawa Y, Tokoro A, Suzuki S, Suzuki M. 1986. Antitumor effect of hexa- N-acetychtohexaose and chitohexaose. Carbohydr Res 151: 403-408 https://doi.org/10.1016/S0008-6215(00)90359-8
  15. Sugano M, Yoshida K, Hashimoto M, Enomoto K, Hirano S. 1992. Hypocholesterolemic activity of partially hydrolyzed chitosan in rats. In Advances in Chitin and Chitosan. Elsevier, London. Vol 13, p 472-478
  16. Adachi H, Tawaragi Y, Inuzuka C, Kubota I, Tsujimoto M, Nishihara T, Nakazato H. 1990. Primary structure of human microsomal dipeptidase deduced from molecular cloning. J BioI Chem 265: 3992-3995
  17. Campbell BJ, Lin YC, Davis RV, Ballew E. 1966. The purification and properties of a particulate renal dipeptidase. Biochim Biophys Acta 118: 371-386 https://doi.org/10.1016/S0926-6593(66)80046-2
  18. Littlewood GM, Hooper NM, Turner AJ 1989. Ectoenzymes of the kidney microvillar membrane. Biochem J 257: 361-367 https://doi.org/10.1042/bj2570361
  19. Kahan FM, Kropp H, Sundelof JG, Birnbaum J. 1983. Thienamycin: development of imipenenecilastatin. J Antimicrob Chemother 12: 1-35 https://doi.org/10.1093/jac/12.1.1
  20. Kropp H, Sundelof JG, Hajdu R, Kahan FM. 1982. Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase. Antimierob Agents Chemother 22: 62-70 https://doi.org/10.1128/AAC.22.1.62
  21. Fukumura Y, Kera Y, Oshitani S, Ushijima Y, Kobayashi I, Liu Z, Watanabe T, Yamada R, Kikuchi H, Kawazu S, Yabuuchi M. 1999. Behaviour of urinary dipeptidase in patients with chronic renal failure. Ann Clin Biochem 36: 221-225 https://doi.org/10.1177/000456329903600215
  22. Finckh ES. 1957. Experimental acute tubular necrosis following subcutaneous injection of glycerol. J Pathol Bacteriol 73: 69-85 https://doi.org/10.1002/path.1700730110
  23. We JS, Kang BY, Lee JC, Lee HB, Park HS. 1997. Identification of urinary dipeptidase as the released form of renal dipeptidase. Kidney Blood Press Res 20: 411-415 https://doi.org/10.1159/000174264
  24. Park SW. 2001. Release mechanism of renal dipeptidase from kidney proximal tubules: a possible involvement of glycosylphosphatidylinositol (GPI)-phospholipase C. PhD Dissertation. Chonnam National University. p 76-84