Malondialdehyde Causes Glutathione/Glutathione Transferase Pathway Oxidative Stress in Intestine and Hepatopancreas of Grass Carp (Ctenopharyngodon idellus)

LIN Xiuxiu; YE Yuantu; CAI Chunfang; WU Ping; HUANG Yuwei; CHEN Kequan; XU Denghui; PENG Kan; LUO Qigang

doi:10.3969/j.issn.1006-267x.2015.11.034

2015 , Vol. 27 >Issue 11: 3604 - 3612

DOI: https://doi.org/10.3969/j.issn.1006-267x.2015.11.034

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Malondialdehyde Causes Glutathione/Glutathione Transferase Pathway Oxidative Stress in Intestine and Hepatopancreas of Grass Carp (Ctenopharyngodon idellus)

LIN Xiuxiu ,
YE Yuantu ,
CAI Chunfang ,
WU Ping ,
HUANG Yuwei ,
CHEN Kequan ,
XU Denghui ,
PENG Kan ,
LUO Qigang

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Preclinical Medicine and Biological Science College of Soochow University, Key Laboratory of Aquatic Animal Nutrition in Jiangsu Province, Suzhou 215123, China

Received date: 2015-02-09

Online published: 2015-11-21

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Abstract

In order to study the effects of malondialdehyde (MDA) on anti-oxidation capability in intestine and hepatopancreas of grass carp (Ctenopharyngodon idellus), the glutathione (GSH)/glutathione transferase (GSTs) pathway was studied. The grass carp, with an initial body weight of (74.8±1.0) g, were randomly divided into 4 groups with 3 replicates in each group and each replicate contained 20 fish. Fish in those 4 groups were fed with a basal diet (control group) and four experimeantal diets added with 61 (B1 group), 124 (B2 group) and 185 mg/kg (B3 group) MDA, respectively. After feeding 72 days, the contents of MDA and GSH in intestine, hepatopancreas and serum were measured, and the expression levels of catalytic subunit of glutamate-cysteine ligase (GCLC), glutathione reductase (GSR), glutathione-S-transferase-pi (GSTpi), microsomal glutathione-S-transferase 1 (MGST1) genes in GSH/GSTs pathway were determined by RT-qPCR method.The results showed as follows:1) in addition to MDA content in hepatopancreas of B3 group was significantly increased (P<0.05), while the other experimental groups was not significantly different compared with control group (P>0.05); serum MDA content of all experimental groups were significantly higher than that in control group (P<0.05). 2) In addition to GSH content in intestine of B1 and B3 groups was significantly increased (P<0.05), while the other experimental groups was not significantly different compared with control group (P>0.05); compared with control group, serum GSH content of B1 and B2 groups was significantly increased (P<0.05). 3) Compared with control group, the expression level of GCLC was significantly up-regulated in intestine of B2 and B3 groups and in hepatopancreas of B1 group (P<0.05); in addition to the expression level of GSR was significantly up-regulated in intestine of B2 group (P<0.05), while the other experimental groups was not significantly different (P>0.05); the expression level of GSTpi was significantly up-regulated in intestine of B2 and B3 groups and in hepatopancreas of B3 group(P<0.05); the expression level of MGST1 was significantly up-regulated in intestine of B3 group (P<0.05); the expression level of MGST1 was significantly down-regulated in hepatopancreas of all experimental groups (P<0.05). The results show that MDA causes GSH/GSTs pathway oxidative stress in intestine and hepatopancreas of grass carp and impacts of MDA have some differences in intestine and hepatopancreas.

Key words： grass carp (Ctenopharyngodon idellus); MDA; intestine; hepatopancreas; GSH; GSTs; gene

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LIN Xiuxiu , YE Yuantu , CAI Chunfang , WU Ping , HUANG Yuwei , CHEN Kequan , XU Denghui , PENG Kan , LUO Qigang . Malondialdehyde Causes Glutathione/Glutathione Transferase Pathway Oxidative Stress in Intestine and Hepatopancreas of Grass Carp (Ctenopharyngodon idellus)[J]. Chinese Journal of Animal Nutrition, 2015 , 27(11) : 3604 -3612 . DOI: 10.3969/j.issn.1006-267x.2015.11.034

References

[1] 李勇, 王雷, 蒋克勇, 等.水产动物营养的生态适宜与环保饲料[J].海洋科学, 2004, 28(3):76-78.
[2] 汪开毓, 叶仕根, 耿毅.氧化脂肪对鱼类危害的病理及防治[J].淡水渔业, 2002, 32(4):60-63.
[3] 韩雨哲, 姜志强, 任同军, 等.氧化鱼油与棕榈油对花鲈肝脏抗氧化酶及组织结构的影响[J].中国水产科学, 2010, 17(4):798-806.
[4] 任泽林, 曾虹, 霍启光, 等.氧化鱼油对鲤肝胰脏抗氧化机能及其组织结构的影响[J].大连水产学院学报, 2000, 15(4):235-243.
[5] KROHNE T U, KAEMMERER E, HOLZ F G, et al.Lipid peroxidation products reduce lysosomal protease activities in human retinal pigment epithelial cells via two different mechanisms of action[J].Experimental Eye Research, 2010, 90(2):261-266.

[6] ISHⅡ T, KUMAZAWA S, SAKURAI T, et al.Mass spectroscopic characterization of protein modification by malondialdehyde[J].Chemical Research in Toxicology, 2006, 19(1):122-129.

[7] 龙建纲, 王学敏, 高宏翔, 等.丙二醛对大鼠肝线粒体呼吸功能及相关脱氢酶活性影响[J].第二军医大学学报, 2006, 26(10):1131-1135.
[8] 童海达, 王佳茗, 宋英.Keap1-Nrf2-ARE在机体氧化应激损伤中的防御作用[J].癌变·畸变·突变, 2013, 25(1):71-75.
[9] BANKI K, HUTTER E, COLOMBO E, et al.Glutathione levels and sensitivity to apoptosis are regulated by changes in transaldolase expression[J].Journal of Biological Chemistry, 1996, 271(51):32994-33001.

[10] 聂芳红, 孔庆波, 刘连平, 等.两种二英类化合物对斑马鱼肝脏MDA、SOD和GST的影响[J].食品与生物技术学报, 2009, 28(2):210-213.
[11] 郑英, 楼宜嘉.对乙酰氨基酚致小鼠肝微粒体谷胱甘肽S-转移酶的激活机制[J].中国药理学与毒理学杂志, 2003, 17(3):211-215.
[12] 姚芹.亚砷酸钠对小鼠体内谷胱甘肽S-转移酶活力及其基因表达的影响[D].硕士学位论文.乌鲁木齐:新疆医科大学, 2009.
[13] 陈科全, 叶元土, 蔡春芳, 等.饲料中氧化鱼油对草鱼(Ctenopharyngodon idellus)生长及肌肉脂肪酸组成的影响[J].动物营养学报, 2015, 27(6):1698-1708.
[14] 叶元土, 蔡春芳, 吴萍.氧化油脂对草鱼生长和健康的损伤作用[M].北京:中国农业科技出版社, 2015.
[15] 姚仕彬, 叶元土, 蔡春芳, 等.丙二醛对离体草鱼肠道黏膜细胞的损伤作用[J].水生生物学报, 2015, 39(1):137-146.
[16] 陈蛟, 张映林, 刘作金.肝肠轴相关机制研究进展[J].现代医药卫生, 2014, 30(22):3405-3408.
[17] ESTERBAUER H, SCHAUR R J, ZOLLNER H.Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes[J].Free Radical Biology and Medicine, 1991, 11(1):81-128.

[18] 李莉, 陈菁菁, 李方序, 等.氧应激毒性产物丙二醛(MDA)对小鼠体能的影响及其体内代谢[J].湖南师范大学自然科学学报, 2006, 29(2):97-101.
[19] SLATTER D A, BOLTON C H, BAILEY A J.The importance of lipid-derived malondialdehyde in diabetes mellitus[J].Diabetologia, 2000, 43(5):550-557.

[20] UCHIDA K, SAKAI K, ITAKURA K, et al.Protein modification by lipid peroxidation products:formation of malondialdehyde-derived N^e-(2-propenal) lysine in proteins[J].Archives of Biochemistry and Biophysics, 1997, 346(1):45-52.

[21] TRAVERSO N, MENINI S, MAINERI E P, et al.Malondialdehyde, a lipoperoxidation-derived aldehyde, can bring about secondary oxidative damage to proteins[J].The Journals of Gerontology Series A:Biological Sciences and Medical Sciences, 2004, 59(9):B890-B895.
[22] CHEN J J, YU B P.Alterations in mitochondrial membrane fluidity by lipid peroxidation products[J].Free Radical Biology and Medicine, 1994, 17(5):411-418.

[23] EDWARDS R, DIXON D P, WALBOT V.Plant glutathione S-transferases:enzymes with multiple functions in sickness and in health[J].Trends in Plant Science, 2000, 5(5):193-198.

[24] 裴冬丽.谷胱甘肽还原酶在植物防御中的研究进展[J].中国农学通报, 2012, 28(18):185-188.
[25] 张媛.产黄青霉谷胱甘肽转移酶基因的克隆、表达与功能研究[D].硕士学位论文.石家庄:河北师范大学, 2007.
[26] TEW K D.Glutathione-associated enzymes in anticancer drug resistance[J].Cancer Research, 1994, 54(16):4313-4320.
[27] CHO S G, LEE Y H, PARK H S, et al.Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1[J].Journal of Biological Chemistry, 2001, 276(16):12749-12755.

[28] RUSCOE J E, ROSARIO L A, WANG T L, et al.Pharmacologic or genetic manipulation of glutathione S-transferase P1-1(GSTπ) influences cell proliferation pathways[J].Journal of Pharmacology and Experimental Therapeutics, 2001, 298(1):339-345.
[29] WU Y, FAN Y, XUE B, et al.Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals[J].Oncogene, 2006, 25(42):5787-5800.

[30] AYALA A, MUÑOZ M F, ARGVELLES S.Lipid peroxidation:production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal[J].Oxidative Medicine and Cellular Longevity, 2014, 2014(2014):1-31.
[31] LENGQVIST J, SVENSSON R, EVERGREN E, et al.Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry[J].Journal of Biological Chemistry, 2004, 279(14):13311-13316.

[32] SHINNO E, SHIMOJI M, IMAIZUMI N, et al.Activation of rat liver microsomal glutathione S-transferase by gallic acid[J].Life Sciences, 2005, 78(1):99-106.

[33] IMAIZUMI N, MIYAGI S, ANIYA Y.Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase[J].Life Sciences, 2006, 78(26):2998-3006.

[34] MORGENSTERN R, LUNDQVIST G, ANDERSSON G, et al.The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms[J].Biochemical Pharmacology, 1984, 33(22):3609-3614.

[35] SCHAFFERT C S.Role of MGST1 in reactive intermediate-induced injury[J].World Journal of Gastroenterology, 2011, 17(20):2552-2557.

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