Stimulatory effect of components of rose flowers on catalytic activity and mRNA expression of superoxide dismutase and catalase in erythrocytes

Environmental Toxicology and Pharmacology

Volumn 27, Issue 3, 2009, Pages 396-401

  Jiang, Y ^a   Wong, J H ^b   Pi, Z F ^c   Ng, T B ^b   Wang, C R ^a   Hou, J ^d   Chen, R R ^a   Niu, H J ^a   Liu, F ^a  

^a BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

^b Prince of Wales Hospital   (Hong Kong)

^c CHANGCHUN INSTITUTE OF APPLIED CHEMISTRY   (China)

^d HENAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

CAT; mRNA expression; Rosa rugosa; SOD

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; MESSENGER RNA; PEPTIDE DERIVATIVE; POLYSACCHARIDE; TANNIN;

ANIMAL CELL; ANTIOXIDANT ACTIVITY; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ERYTHROCYTE; FLOWER; GENE EXPRESSION; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; ROSE;

ROSA RUGOSA;

EID: 62949226730     PISSN: 13826689     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.etap.2009.01.004     Document Type: Article

References (45)

1. Aeschlach R., Loliger J., Scott B.C., Murcia A., Butler J., and Halliwell B. Antioxidant actions of thymol, carvacrol, 6-gingerol, zinglrone and hydroxytyrosol. Food Chem. Toxicol. 32 (1994) 31-36
2. Agrawal D., and Sultana P. Biochemical and structural alterations in rat erythrocytes due to hexachlorocyclohexane exposure. Food and Chemical Toxicology 31 (1993) 443-448
3. Aslan M., Cort A., and Yucel L. Oxidative and nitrative stress markers in glaucoma. Free Radical Biology and Medicine 4 (2008) 367-376
4. Blum J., and Fridovich I. Inactivation of glutathione peroxidase by superoxide radical. Archives of Biochemistry and Biophysics 240 (1985) 500-508
5. Borgstahl G.E., Parge H.E., Hickey M.J., Beyer Jr. W.F., Hallewell R.A., and Tainer J.A. The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 71 (1992) 107-118
6. Cai Y., Luo Q., Sun M., and Corke H. Antioxidant activity and phenolic compounds of 112 traditional Chinese medicinal plants associated with anticancer. Life Sciences 74 (2004) 2157-2184
7. Chiu D., Kuypers F., and Lubin B. Lipid peroxidation in human red cells. Seminars in Hematology 26 (1989) 257-276
8. Clemens M.R., and Waller H.D. Lipid peroxidation in erythrocytes. Chemistry and Physics of Lipids 45 (1987) 251-268
9. Fridovich I. Superoxide radical and superoxide dismutases. Annual Review of Biochemistry 64 (1995) 97-112
10. Fukuhara R., and Tezuka T. Structure, molecular evolution, and gene expression of primate superoxide dismutases. Gene 296 (2002) 99-109
11. Giannopolitis C.N., and Ries S.K. Superoxide dismutases. Plant Physiology 59 (1997) 309-314
12. Gilgun-Sherki Y., Rosenbaum Z., Melamed E., and Offen D. Antioxidant therapy in acute central nervous system injury: current state. Pharmacological Reviews 54 (2002) 271-284
13. Ji L.L., Stratman F.W., and Lardy H.A. Antioxidant enzyme systems in rat liver and skeletal muscle. Archives of Biochemistry and Biophysics 263 (1988) 150-160
14. Jiang S., Lee J., Zhang Z., Inserra P., Solkoff D., and Watson R.R. Dehydroepiandrosterone synergizes with antioxidant supplement. Journal of Nutritional Biochemistry 9 (1998) 362-369
15. Kiningham K., and Kasarkis E. Antioxidant function of metallothioneins. The Journal of Trace Elements in Experimental Medicine 11 (1998) 219-226
16. Kleszczynska H., Oswiecmska H., Sarapuk J., Witek S., and Przestalska S. Protective effect of quaternary piperidinium salts on lipid oxidation in the erythrocyte membrane. Verlag der Zeitschrift für Naturforschung 54 (1999) 424-428
17. Ko H., Kim M., Kim C., and Ryu W. Binding of annexin V to oxidized lipid on oxidatively damaged erythrocyte. Atherosclerosis Supplements 9 (2008) 56
18. Kono Y., and Fridovich I. Superoxide radical inhibits catalase. Journal of Biological Chemistry 257 (1982) 5751-5754
19. Li L., Ng T.B., Gao W., Li W., Fu M., Niu S.M., Zhao L., Chen R.R., and Liu F. Antioxidant activity of gallic acid from rose flowers in senescence accelerated mice. Life Sciences 77 (2005) 230-240
20. Madesh M., Anup R., Benard O., and Balasubramanian K.A. Apoptosis in the monkey small intestinal epithelium: structural and functional alterations in the mitochondria. Free Radical Biology and Medicine 26 (1999) 836-843
21. 2 or ultraviolet B light. Archives of Dermatological Research 290 (1998) 113-118
22. Matés J.M., Pérez-Gómez C., and Núñ ez de Castro I. Antioxidant enzymes and human diseases. Clinical Biochemistry 32 (1999) 595-603
23. Miki M., Tnmai H., Mino M., Yamamoto Y., and Niki E. Free-radical chain oxidation of rat red blood cells by molecular oxygen and its inhibition by aloha-tocopherol. Archives of Biochemistry and Biophysics 58 (1987) 373-380
24. Naik G.H., Pyiyadarsini K.I., Satav J.G., Banavalikar M.M., Sohoni D.P., Biyani M.k., and Mohan H. Comparative antioxidant activity of individual herbal components used in Ayurvedic medicine. Phytochemistry 63 (2003) 97-104
25. Ng T.B., Gao W., and Li L. Rose (Rosa rugosa) flower extract increases the activities of antioxidant enzymes and their gene expression and reduces lipid peroxidation. Biochemistry and Cell Biology 83 8 (2005) 78-85
26. Ng T.B., He J.S., Niu S.M., Zhao L., Pi Z.F., Shao W., and Liu F. A gallic acid derivative and polysaccharides with antioxidative activity from rose (Rosa rugosa) flowers. Journal of Pharmacy and Pharmacology 56 (2004) 537-545
27. Ng T.B., Pi Z.F., Yue H., Zhao L., Fu M., Li L., Hou J., Shi L.S., Chen R.R., Jiang Y., and Liu F. A polysaccharopeptide complex and a condensed tannin with antioxidant activity from dried rose (Rose rugosa) flowers. Journal of Pharmacy and Pharmacology 58 (2006) 529-534
28. Oliver C.N., Starke-Reed P.E., Stadtman E.R., Liu G.J., Carney J.M., and Floyed R.A. Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain. Proceedings of the National Academy of Sciences of the United States of America 87 (1990) 5144-5157
29. Pablos M.I., Agapito M.T., Gutierrez R., Recio J.M., Reiter R.J., Barlow-Walden L., Acuna-Castroviejo D., and Menendez-Pelaez A. Melatonin stimulates the activity of the detoxifying enzyme glutathione peroxidase in several tissues of chicks. Journal of Pineal Research 19 (1995) 111-115
30. Prasanthi K., Muralidhara, et al. Morphological and biochemical perturbations in rat erythrocytes following in vitro exposure to Fenvalerate and its metabolite. Toxicology in Vitro 19 (2005) 449-456
31. Radi R., Beckman J.S., Bush K.M., and Freeman B.A. Peroxynitrite induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Archives of Biochemistry and Biophysics 288 (1991) 481
32. Reiter R.J., Melchiorri D., Sewerynek E., Poeggeler B., Barlow-Walden L., Chuang J., Ortiz G.G., and Acuna-Castroviejo D. A review of the evidence supporting melatonin's role as an antioxidant. Journal of Pineal Research 18 (1995) 1-11
33. Rodriguez A.B., Nogales G., Ortega E., and Barriga C. Melatonin controls superoxide anion level: Modulation of superoxide dismutase activity in ring dove heterophils. Journal of Pineal Research 24 (1998) 9-14
34. Rong Z.X., Liu H.Z., Bao .Q., Cheng H.Z., Sun Y.Y., and Sun T. Measurement of glutathione peroxidase activity in the whole blood of mice. Progress of Biochemistry and Biophysics 21 (1994) 362-366
35. Shashoua V.E., and Adams D.S. New synthetic peptides can enhance gene expression of key antioxidant defense enzymes in vitro and in vivo. Brain Research 1024 (2004) 34-43
36. Shankar J.C., and Julie K.A. Redox imbalance in Parkinson's disease. Biochimica et Biophysica Acta (BBA)-General Subjects 1780 (2008) 1362-1367
37. 3-induced epilopogenic foci in the brain. Epilepsia 31 (1990) 15-36
38. Smith M.W., and Doolittle R.F. A comparison of evolutionary rates of the two major kinds of superoxide dismutase. Journal of Molecular Evolution 34 (1992) 175-184
39. Stern A. Red cell oxidative damage. In: Sies H. (Ed). Oxidative Stress (1985), Academic Press, New York 331-349
40. Suwalsky M., Benites M., Villena F., Aguilar F., and Sotomayor C.P. The organochlorine pesticide heptachlor disrupts the structure of model and cell membranes. Biochimica et Biophysica Acta 1326 (1997) 115-123
41. Tolmasoff J.M., Ono T., and Cutler R.G. Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species. Proceedings of the National Academy of Sciences of the United States of America 77 (1980) 2777-2781
42. Wade M.A., and Tucker H.N. Antioxidant characteristics of l-histidine. Journal of Nutritional Biochemistry 9 (1998) 308-315
43. Wang Y.M.D. Antioxidant Activities and mRNA Expression of superoxide dismutase, catalase, and glutathione peroxidase in normal and preeclamptic placentas. Journal of the Society for Gynecological Investigation 3 (1996) 179-184
44. Yasuyuki H. The phytochemistry of Rosa rugosa. Phytochemistry 43 (1996) 535-549
45. Youdim K.A., Shukitt-Hale B., Mackinnon S., Kalt W., and Joseph J.A. Polyphenolics enhance red blood cell resistance to oxidative stress in vitro and in vivo. Biochimica et Biophysica Acta 1519 (2000) 117-122