Cortex Mori Radicis extract attenuates myocardial damages in diabetic rats by regulating ERS

Biomedicine and Pharmacotherapy

Volumn 90, Issue , 2017, Pages 777-785

  Lian, Jiangfang ^a   Chen, Jiayuan ^a   Yuan, Yanyan ^a   Chen, Jiayi ^a   Daud M Sayed, M ^a   Luo, Lin ^a   Zhu, Yabing ^a   Li, Song ^b   Bu, Shizhong ^a  

^a NINGBO UNIVERSITY   (China)

^b UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

Diabetes; Myocardial damage; The cortex mori radicis

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; COLLAGEN TYPE 1; CONNECTIVE TISSUE GROWTH FACTOR; GLUCOSE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; INITIATION FACTOR 2ALPHA; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MULBERRY EXTRACT; PROTEIN KINASE; PROTEIN KINASE RNA LIKE ENDOPLASMIC RETICULUM KINASE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; PLANT EXTRACT; STREPTOZOCIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CARDIAC MUSCLE; CONTROLLED STUDY; DIABETIC CARDIOMYOPATHY; DOWN REGULATION; ENDOPLASMIC RETICULUM STRESS; EXTRACELLULAR MATRIX; GLUCOSE BLOOD LEVEL; GLUCOSE METABOLISM; HEART MUSCLE FIBROSIS; HEART MUSCLE INJURY; HEART PROTECTION; INSULIN BLOOD LEVEL; METABOLIC PARAMETERS; MORUS ALBA; NONHUMAN; ORAL GLUCOSE TOLERANCE TEST; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; RAT; ROOT CORTEX; STREPTOZOTOCIN-INDUCED DIABETES MELLITUS; WESTERN BLOTTING; ANIMAL; BARK; CARDIAC MUSCLE CELL; CHEMISTRY; COMPLICATION; DRUG EFFECTS; EXPERIMENTAL DIABETES MELLITUS; MALE; METABOLISM; ORIENTAL MEDICINE; PATHOLOGY; PLANT ROOT; PROCEDURES; SPRAGUE DAWLEY RAT;

ANIMALS; DIABETES MELLITUS, EXPERIMENTAL; DIABETIC CARDIOMYOPATHIES; ENDOPLASMIC RETICULUM STRESS; EXTRACELLULAR MATRIX; MALE; MEDICINE, EAST ASIAN TRADITIONAL; MITOGEN-ACTIVATED PROTEIN KINASES; MYOCARDIUM; MYOCYTES, CARDIAC; PLANT BARK; PLANT EXTRACTS; PLANT ROOTS; RATS; RATS, SPRAGUE-DAWLEY; STREPTOZOCIN;

EID: 85017538337     PISSN: 07533322     EISSN: 19506007     Source Type: Journal    
DOI: 10.1016/j.biopha.2017.03.097     Document Type: Article

References (47)

1. [1] WH. Organization, Global Report on Diabetes., 2016.
2. [2] Perez-Diaz, I., Diabetes mellitus. Gaceta medica de Mexico 152:Suppl. 1 (2016), 50–55.
3. [3] Alberti, K.G., Zimmet, P.Z., Definition, diagnosis and classification of diabetes mellitus and its complications: Part 1: diagnosis and classification of diabetes mellitus provisional report of a WHO consultation. Diabet. Med. 15:7 (1998), 539–553.
4. [4] da Rocha Fernandes, J., Ogurtsova, K., Linnenkamp, U., Guariguata, L., Seuring, T., Zhang, P., Cavan, D., Makaroff, L.E., IDF Diabetes Atlas estimates of 2014 global health expenditures on diabetes. Diabetes Res. Clin. Pract. 117 (2016), 48–54.
5. [5] From, A.M., Leibson, C.L., Bursi, F., Redfield, M.M., Weston, S.A., Jacobsen, S.J., Rodeheffer, R.J., Roger, V.L., Diabetes in heart failure: prevalence and impact on outcome in the population. Am. J. Med. 119:7 (2006), 591–599.
6. [6] Groenendyk, J., Sreenivasaiah, P.K., Kim, D.H., Agellon, L.B., Michalak, M., Biology of endoplasmic reticulum stress in the heart. Circ. Res. 107:10 (2010), 1185–1197.
7. [7] Xu, J., Zhou, Q., Xu, W., Cai, L., Endoplasmic reticulum stress and diabetic cardiomyopathy. Exp. Diabetes Res., 2012, 2012, 827971.
8. [8] Yang, L., Zhao, D., Ren, J., Yang, J., Endoplasmic reticulum stress and protein quality control in diabetic cardiomyopathy. Biochim. Biophys. Acta 1852:2 (2015), 209–218.
9. [9] Ma, Y., Hendershot, L.M., The unfolding tale of the unfolded protein response. Cell 107:7 (2001), 827–830.
10. [10] Walter, P., Ron, D., The unfolded protein response: from stress pathway to homeostatic regulation. Science (New York, NY) 334:6059 (2011), 1081–1086.
11. [11] Beer, S., Golay, S., Bardy, D., Feihl, F., Gaillard, R.C., Bachmann, C., Waeber, B., Ruiz, J., Increased plasma levels of N-terminal brain natriuretic peptide (NT-proBNP) in type 2 diabetic patients with vascular complications. Diabetes Metab. 31:6 (2005), 567–573.
12. [12] Ganguly, P.K., Role of atrial natriuretic peptide in congestive heart failure due to chronic diabetes. Can. J. Cardiol. 7:6 (1991), 275–280.
13. [13] Li, Z., Zhang, T., Dai, H., Liu, G., Wang, H., Sun, Y., Zhang, Y., Ge, Z., Involvement of endoplasmic reticulum stress in myocardial apoptosis of streptozocin-induced diabetic rats. J. Clin. Biochem. Nutr. 41:1 (2007), 58–67.
14. [14] Yang, X., Yang, L., Zheng, H., Hypolipidemic and antioxidant effects of mulberry (Morus alba L.) fruit in hyperlipidaemia rats. Food Chem. Toxicol. 48:8-9 (2010), 2374–2379.
15. [15] Choi, E.M., Hwang, J.K., Effects of Morus alba leaf extract on the production of nitric oxide, prostaglandin E2 and cytokines in RAW264.7 macrophages. Fitoterapia 76:7-8 (2005), 608–613.
16. [16] Shibata, Y., Kume, N., Arai, H., Hayashida, K., Inui-Hayashida, A., Minami, M., Mukai, E., Toyohara, M., Harauma, A., Murayama, T., Mulberry leaf aqueous fractions inhibit TNF-alpha-induced nuclear factor kappaB (NF-kappaB) activation and lectin-like oxidized LDL receptor-1 (LOX-1) expression in vascular endothelial cells. Atherosclerosis 193:1 (2007), 20–27.
17. [17] Lee, Y.J., Choi, D.H., Kim, E.J., Kim, H.Y., Kwon, T.O., Kang, D.G., Lee, H.S., Hypotensive, hypolipidemic, and vascular protective effects of Morus alba L: in rats fed an atherogenic diet. Am. J. Chin. Med. 39:1 (2011), 39–52.
18. [18] Mahmoud, A.M., Abd El-Twab, S.M., Abdel-Reheim, E.S., Consumption of polyphenol-rich Morus alba leaves extract attenuates early diabetic retinopathy: the underlying mechanism. Eur. J. Nutr., 2016, 10.1007/s00394-016-1214-0.
19. [19] Ma, S.T., Zhang, X.K., Wang, Q.L., Experimental study on the preventive and treatment function of cortex mori for peripheral nervous lesion at the early stage of diabetes rats. Zhongguo ying yong sheng li xue za zhi 24:2 (2008), 201–204.
20. [20] Sugano, M., Yamato, H., Hayashi, T., Ochiai, H., Kakuchi, J., Goto, S., Nishijima, F., Iino, N., Kazama, J.J., Takeuchi, T., et al. High-fat diet in low-dose-streptozotocin-treated heminephrectomized rats induces all features of human type 2 diabetic nephropathy: a new rat model of diabetic nephropathy. Nutr. Metab. Cardiovasc. Dis. 16:7 (2006), 477–484.
21. [21] Mihm, M.J., Seifert, J.L., Coyle, C.M., Bauer, J.A., Diabetes related cardiomyopathy time dependent echocardiographic evaluation in an experimental rat model. Life Sci. 69:5 (2001), 527–542.
22. [22] Chen, H.S., Shan, Y.X., Yang, T.L., Lin, H.D., Chen, J.W., Lin, S.J., Wang, P.H., Insulin deficiency downregulated heat shock protein 60 and IGF-1 receptor signaling in diabetic myocardium. Diabetes 54:1 (2005), 175–181.
23. [23] Liang, D., Zhong, P., Hu, J., Lin, F., Qian, Y., Xu, Z., Wang, J., Zeng, C., Li, X., Liang, G., EGFR inhibition protects cardiac damage and remodeling through attenuating oxidative stress in STZ-induced diabetic mouse model. J. Mol. Cell. Cardiol. 82 (2015), 63–74.
24. [24] Montanari, D., Yin, H., Dobrzynski, E., Agata, J., Yoshida, H., Chao, J., Chao, L., Kallikrein gene delivery improves serum glucose and lipid profiles and cardiac function in streptozotocin-induced diabetic rats. Diabetes 54:5 (2005), 1573–1580.
25. [25] Zhang, H., Zhao, T., Gong, Y., Dong, X., Zhang, W., Sun, S., Wang, H., Gu, Y., Lu, X., Yan, M., Attenuation of diabetic nephropathy by Chaihuang-Yishen granule through anti-inflammatory mechanism in streptozotocin-induced rat model of diabetics. J. Ethnopharmacol. 151:1 (2014), 556–564.
26. [26] Klimas, J., Kmecova, J., Jankyova, S., Yaghi, D., Priesolova, E., Kyselova, Z., Musil, P., Ochodnicky, P., Krenek, P., Kyselovic, J., Pycnogenol improves left ventricular function in streptozotocin-induced diabetic cardiomyopathy in rats. Phytother. Res. 24:7 (2010), 969–974.
27. [27] Xu, Z., Ju, J., Wang, K., Gu, C., Feng, Y., Evaluation of hypoglycemic activity of total lignans from Fructus Arctii in the spontaneously diabetic Goto-Kakizaki rats. J. Ethnopharmacol. 151:1 (2014), 548–555.
28. [28] Li, X., Du, N., Zhang, Q., Li, J., Chen, X., Liu, X., Hu, Y., Qin, W., Shen, N., Xu, C., MicroRNA-30d regulates cardiomyocyte pyroptosis by directly targeting foxo3a in diabetic cardiomyopathy. Cell. Death. Dis., 5, 2014, e1479.
29. [29] Toth, A., Nickson, P., Mandl, A., Bannister, M.L., Toth, K., Erhardt, P., Endoplasmic reticulum stress as a novel therapeutic target in heart diseases. Cardiovasc. Hematol. Disorders Drug Targets 7:3 (2007), 205–218.
30. [30] Ti, Y., Xie, G.L., Wang, Z.H., Bi, X.L., Ding, W.Y., Wang, J., Jiang, G.H., Bu, P.L., Zhang, Y., Zhong, M., TRB3 gene silencing alleviates diabetic cardiomyopathy in a type 2 diabetic rat model. Diabetes 60:11 (2011), 2963–2974.
31. [31] Satomi-Kobayashi, S., Ueyama, T., Mueller, S., Toh, R., Masano, T., Sakoda, T., Rikitake, Y., Miyoshi, J., Matsubara, H., Oh, H., et al. Deficiency of nectin-2 leads to cardiac fibrosis and dysfunction under chronic pressure overload. Hypertension (Dallas, Tex: 1979) 54:4 (2009), 825–831.
32. [32] Zhang, M., Chen, M., Zhang, H.Q., Sun, S., Xia, B., Wu, F.H., In vivo hypoglycemic effects of phenolics from the root bark of Morus alba. Fitoterapia 80:8 (2009), 475–477.
33. [33] Zhang, Z., Shi, L., Anti-inflammatory and analgesic properties of cis-mulberroside A from Ramulus mori. Fitoterapia 81:3 (2010), 214–218.
34. [34] Aragno, M., Mastrocola, R., Catalano, M.G., Brignardello, E., Danni, O., Boccuzzi, G., Oxidative stress impairs skeletal muscle repair in diabetic rats. Diabetes 53:4 (2004), 1082–1088.
35. [35] Fang, Z.Y., Prins, J.B., Marwick, T.H., Diabetic cardiomyopathy: evidence, mechanisms, and therapeutic implications. Endocr. Rev. 25:4 (2004), 543–567.
36. [36] Martinez, D.A., Guhl, D.J., Stanley, W.C., Vailas, A.C., Extracellular matrix maturation in the left ventricle of normal and diabetic swine. Diabetes Res. Clin. Pract. 59:1 (2003), 1–9.
37. [37] Surveyor, G.A., Brigstock, D.R., Immunohistochemical localization of connective tissue growth factor (CTGF) in the mouse embryo between days 7.5 and 14.5 of gestation. Growth Factors (Chur, Switzerland) 17:2 (1999), 115–124.
38. [38] Rajesh, M., Mukhopadhyay, P., Batkai, S., Mukhopadhyay, B., Patel, V., Hasko, G., Szabo, C., Mabley, J.G., Liaudet, L., Pacher, P., Xanthine oxidase inhibitor allopurinol attenuates the development of diabetic cardiomyopathy. J. Cell. Mol. Med. 13:8b (2009), 2330–2341.
39. [39] Rao, R.V., Niazi, K., Mollahan, P., Mao, X., Crippen, D., Poksay, K.S., Chen, S., Bredesen, D.E., Coupling endoplasmic reticulum stress to the cell-death program: a novel HSP90-independent role for the small chaperone protein p23. Cell Death Differ. 13:3 (2006), 415–425.
40. [40] Mulhern, M.L., Madson, C.J., Danford, A., Ikesugi, K., Kador, P.F., Shinohara, T., The unfolded protein response in lens epithelial cells from galactosemic rat lenses. Invest. Ophthalmol. Vis. Sci. 47:9 (2006), 3951–3959.
41. [41] Ma, K., Vattem, K.M., Wek, R.C., Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress. J. Biol. Chem. 277:21 (2002), 18728–18735.
42. [42] Bertolotti, A., Zhang, Y., Hendershot, L.M., Harding, H.P., Ron, D., Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2:6 (2000), 326–332.
43. [43] Shi, Y., Vattem, K.M., Sood, R., An, J., Liang, J., Stramm, L., Wek, R.C., Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18:12 (1998), 7499–7509.
44. [44] Harding, H.P., Zhang, Y., Zeng, H., Novoa, I., Lu, P.D., Calfon, M., Sadri, N., Yun, C., Popko, B., Paules, R., An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11:3 (2003), 619–633.
45. [45] Hansen, H.G., Schmidt, J.D., Soltoft, C.L., Ramming, T., Geertz-Hansen, H.M., Christensen, B., Sorensen, E.S., Juncker, A.S., Appenzeller-Herzog, C., Ellgaard, L., Hyperactivity of the Ero1alpha oxidase elicits endoplasmic reticulum stress but no broad antioxidant response. J. Biol. Chem. 287:47 (2012), 39513–39523.
46. [46] Papakrivopoulou, J., Lindahl, G.E., Bishop, J.E., Laurent, G.J., Differential roles of extracellular signal-regulated kinase 1/2 and p38MAPK in mechanical load-induced procollagen alpha1(I) gene expression in cardiac fibroblasts. Cardiovasc. Res. 61:4 (2004), 736–744.
47. [47] Pattingre, S., Bauvy, C., Carpentier, S., Levade, T., Levine, B., Codogno, P., Role of JNK1-dependent Bcl-2 phosphorylation in ceramide-induced macroautophagy. J. Biol. Chem. 284:5 (2009), 2719–2728.