Selenium deficiency induced damages and altered expressions of metalloproteinases and their inhibitors (MMP1/3, TIMP1/3) in the kidneys of growing rats

Journal of Trace Elements in Medicine and Biology

Volumn 34, Issue , 2016, Pages 1-9

  Han, Jing ^a   Liang, Hua ^a   Yi, Jianhua ^a   Tan, Wuhong ^a   He, Shulan ^b   Wu, Xiaofang ^a   Shi, Xiaowei ^a   Ma, Jing ^c   Guo, Xiong ^a  

^a XI'AN JIAOTONG UNIVERSITY   (China)

^b NINGXIA MEDICAL UNIVERSITY   (China)

^c Division for Endemic Disease Prevention and Control   (China)

Author keywords

Damage; Kidney; MMP; Selenium deficiency; TIMP

Indexed keywords

INTERSTITIAL COLLAGENASE; MESSENGER RNA; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 3; SELENIUM;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CELL HYPERPLASIA; CONTROLLED STUDY; DOWN REGULATION; EXTRACELLULAR MATRIX; FEMALE; GLOMERULUS BASEMENT MEMBRANE; IMMUNOHISTOCHEMISTRY; KIDNEY; KIDNEY COLLECTING TUBULE; KIDNEY PROXIMAL TUBULE; MALE; MESANGIUM CELL; NEWBORN; NONHUMAN; PODOCYTE; PRIORITY JOURNAL; RAT; SELENIUM DEFICIENCY; ULTRASTRUCTURE; UPREGULATION; ANIMAL; DEFICIENCY; GENETICS; METABOLISM; PATHOLOGY; PHYSIOLOGY; SPRAGUE DAWLEY RAT;

ANIMALS; FEMALE; KIDNEY; MALE; MATRIX METALLOPROTEINASE 1; MATRIX METALLOPROTEINASE 3; RATS; RATS, SPRAGUE-DAWLEY; SELENIUM; TISSUE INHIBITOR OF METALLOPROTEINASE-1; TISSUE INHIBITOR OF METALLOPROTEINASE-3;

EID: 84957540017     PISSN: 0946672X     EISSN: 18783252     Source Type: Journal    
DOI: 10.1016/j.jtemb.2015.11.003     Document Type: Article

References (34)

1. Rayman M.P. The importance of selenium to human health. Lancet 2000, 356(9225):233-241.
2. Lu J., Holmgren A. Selenoproteins. J. Biol. Chem. 2009, 284(2):723-727.
3. Zachara B.A., Gromadzińska J., Wasowicz W., et al. Red blood cell and plasma glutathione peroxidase activities and selenium concentration in patients with chronic kidney disease: a review. Acta Biochim. Pol. 2006, 53(4):663-677.
4. Li N., Gao Z.D., Luo D.G., et al. Selenium level in the environment and the population of Zhoukoudian area, Beijing, China. Sci. Total Environ. 2007, 381(1):105-111.
5. Gao J., Liu Y., Huang Y., et al. Daily selenium intake in a moderate selenium deficiency area of Suzhou, China. Food Chem. 2011, 126(3):1088-1093.
6. Mott J.D., Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol. 2004, 16(5):558-564.
7. Lenz O., Elliot S.J., Stetler-Stevenson W.G. Matrix metalloproteinases in renal development and disease. J. Am. Soc. Nephrol. 2000, 11(3):574-581.
8. Kadono Y., Shibahara K., Namiki M., et al. Membrane type 1-matrix metalloproteinase is involved in the formation of hepatocyte growth factor/scatter factor-induced branching tubules in Madin-Darby canine kidney epithelial cells. Biochem. Biophys. Res. Commun. 1998, 251(3):681-687.
9. Chang H.R., Yang S.F., Li M.L., et al. Relationships between circulating matrix metalloproteinase-2 and-9 and renal function in patients with chronic kidney disease. Clin. Chim. Acta 2006, 366(1):243-248.
10. Musiał K., Zwolińska D. Matrix metalloproteinases (MMP-2, 9) and their tissue inhibitors (TIMP-1, 2) as novel markers of stress response and atherogenesis in children with chronic kidney disease (CKD) on conservative treatment. Cell Stress Chaperon 2011, 16(1):97-103.
11. Engelmyer E., van Goor H., Edwards D.R., et al. Differential mRNA expression of renal cortical tissue inhibitor of metalloproteinase-1, -2, and -3 in experimental hydronephrosis. J. Am. Soc. Nephrol. 1995, 5(9):1675-1683.
12. Sharma A.K., Mauer S.M., Kim Y., et al. Altered expression of matrix metalloproteinase-2, TIMP, and TIMP-2 in obstructive nephropathy. J. Lab. Clin. Med. 1995, 125(6):754-761.
13. Catania J.M., Chen G., Parrish A.R. Role of matrix metalloproteinases in renal pathophysiologies. Am. J. Physiol. Renal Physiol. 2007, 292(3):F905-F911.
14. Sekiuchi M., Kudo A., Nakabayashi K., et al. Expression of matrix metalloproteinases 2 and 9 and tissue inhibitors of matrix metalloproteinases 2 and 1 in the glomeruli of human glomerular diseases: the results of studies using immunofluorescence, in situ hybridization, and immunoelectron microscopy. Clin. Exp. Nephrol. 2012, 16(6):863-874.
15. ▵▵CT method. Methods 2001, 25(4):402-408.
16. Zhang G., Chen Y., BilalWaqar A., et al. Quantitative analysis of rabbit coronary atherosclerosis: practical techniques utilizing open-source software. Anal. Quant. Cytopathol. Histpathol. 2015, 37(2):115-122.
17. Beckett G.J., Arthur J.R. Selenium and endocrine systems. J. Endocrinol. 2005, 184(3):455-465.
18. Misra S., Boylan M., Selvam A., et al. Redox-active selenium compounds from toxicity and cell death to cancer treatment. Nutrients 2015, 7(5):3536-3556.
19. He S., Guo X., Tan W., et al. Effect of selenium deficiency on phosphorylation of the AMPK pathway in rats. Biol. Trace Elem. Res. 2015, 1-7.
20. Ha E.J., Smith A.M. Plasma selenium and plasma and erythrocyte glutathione peroxidase activity increase with estrogen during the menstrual cycle. J. Am. Coll. Nutr. 2003, 22(1):43-51.
21. Zhou X., Smith A.M., Failla M.L., et al. Estrogen status alters tissue distribution and metabolism of selenium in female rats. J. Nutr. Biochem. 2012, 23(6):532-538.
22. Méplan C., Crosley L.K., Nicol F., et al. Genetic polymorphisms in the human selenoprotein P gene determine the response of selenoprotein markers to selenium supplementation in a gender-specific manner (the SELGEN study). FASEB J. 2007, 21(12):3063-3074.
23. Loeschner K., Hadrup N., Hansen M., et al. Absorption, distribution, metabolism and excretion of selenium following oral administration of elemental selenium nanoparticles or selenite in rats. Metallomics 2014, 6(2):330-337.
24. Stockler-Pinto M.B., Lobo J., Moraes C., et al. Effect of Brazil nut supplementation on plasma levels of selenium in hemodialysis patients: 12 months of follow-up. J. Renal Nutr. 2012, 22(4):434-439.
25. Salehi M., Sohrabi Z., Ekramzadeh M., et al. Selenium supplementation improves the nutritional status of hemodialysis patients: a randomized, double-blind, placebo-controlled trial. Nephrol. Dial Transpl. 2012, 0:1-6. 10.1093/ndt/gfs170.
26. Brunner H.R., Laragh J.H., Baer L., et al. Essential hypertension: renin and aldosterone, heart attack and stroke. New Engl. J. Med. 1972, 286(9):441-449.
27. Miner J.H. The glomerular basement membrane. Exp. Cell Res. 2012, 318(9):973-978.
28. Migliorini A., Ebid R., Scherbaum C.R., et al. The danger control concept in kidney disease: mesangial cells. J. Nephrol. 2013, 26(3):437-449.
29. Liu Y.P., Liang W., Yang Y.J., et al. IQGAP1 regulates actin cytoskeleton organization in podocytes through interaction with nephrin. Cell. Signal. 2015, 27(4):867-877.
30. Brosius F.C., Coward R.J. Podocytes signaling pathways, and vascular factors in diabetic kidney disease. Adv. Chronic Kidney D 2014, 21(3):304-310.
31. Daehn I., Casalena G., Zhang T., et al. Endothelial mitochondrial oxidative stress determines podocyte depletion in segmental glomerulosclerosis. J. Clin. Invest. 2014, 124(4):1608.
32. Asanuma K., Mundel P. The role of podocytes in glomerular pathobiology. J. Clin. Exp. Nephrol. 2003, 7(4):255-259.
33. Bhuvarahamurthy V., Kristiansen G.O., Johannsen M., et al. In situ gene expression and localization of metalloproteinases MMP1, MMP2, MMP3, MMP9, and their inhibitors TIMP1 and TIMP2 in human renal cell carcinoma. Oncol. Rep. 2006, 15(5):1379-1384.
34. Qian W., Miao K., Li T., et al. Effect of selenium on fluoride-induced changes in synaptic plasticity in rat hippocampus. Biol. Trace Elem. Res. 2013, 155(2):253-260.