Genipin ameliorates hypertension-induced renal damage via the angiotensin II-TLR/MyD88/MAPK pathway

Fitoterapia

Volumn 112, Issue , 2016, Pages 244-253

  Yu, Dawei ^a   Shi, Mengsong ^b   Bao, Jinwei ^a   Yu, Xinyan ^a   Li, Yuhui ^a   Liu, Wenbo ^a  

^a YANTAISHAN HOSPITAL   (China)

^b BINZHOU MEDICAL UNIVERSITY   (China)

Author keywords

Angiotensin II; Genipin; Human mesangial cells; Hypertension; Toll like receptors

Indexed keywords

ALBUMIN; ANGIOTENSIN II; CREATININE; GENIPIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MYELOID DIFFERENTIATION FACTOR 88; N ACETYL BETA GLUCOSAMINIDASE; NITROGEN; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; UREA; VALSARTAN; ANTIHYPERTENSIVE AGENT; CYTOKINE; IRIDOID; MYD88 PROTEIN, HUMAN; TLR2 PROTEIN, HUMAN; TLR4 PROTEIN, HUMAN;

ANIMAL MODEL; ARTICLE; CELL PROLIFERATION; CONTROLLED STUDY; CREATININE BLOOD LEVEL; CYTOKINE RELEASE; DIASTOLIC BLOOD PRESSURE; DOSE RESPONSE; DRUG MEGADOSE; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; HUMAN CELL; HYPERTENSION; KIDNEY FUNCTION; KIDNEY INJURY; LOW DRUG DOSE; MALE; MESANGIUM CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT; SIGNAL TRANSDUCTION; SYSTOLIC BLOOD PRESSURE; TREATMENT DURATION; UPREGULATION; UREA NITROGEN BLOOD LEVEL; ANIMAL; BLOOD PRESSURE; DRUG EFFECTS; KIDNEY; METABOLISM; PATHOLOGY; SPONTANEOUSLY HYPERTENSIVE RAT;

ANGIOTENSIN II; ANIMALS; ANTIHYPERTENSIVE AGENTS; BLOOD PRESSURE; CELL PROLIFERATION; CYTOKINES; HUMANS; HYPERTENSION; IRIDOIDS; KIDNEY; MALE; MAP KINASE SIGNALING SYSTEM; MESANGIAL CELLS; MYELOID DIFFERENTIATION FACTOR 88; RATS, INBRED SHR; REACTIVE OXYGEN SPECIES; TOLL-LIKE RECEPTOR 2; TOLL-LIKE RECEPTOR 4;

EID: 84976285893     PISSN: 0367326X     EISSN: 18736971     Source Type: Journal    
DOI: 10.1016/j.fitote.2016.06.010     Document Type: Article

References (48)

1. [1] Virdis, A., Dell'Agnello, U., Taddei, S., Impact of inflammation on vascular disease in hypertension. Maturitas 78 (2014), 179–183.
2. [2] McMaster, W.G., Kirabo, A., Madhur, M.S., Harrison, D.G., Inflammation, immunity, and hypertensive end-organ damage. Circ. Res. 116 (2015), 1022–1033.
3. [3] Solak, Y., Afsar, B., Vaziri, N.D., Aslan, G., CE, Y., Covic, A., et al. Hypertension as an autoimmune and inflammatory disease. Hypertens. Res., 2016.
4. [4] Young, C.N., Davisson, R.L., Angiotensin-II, the brain, and hypertension: an update. Hypertension 66 (2015), 920–926.
5. [5] Te Riet, L., van Esch, J.H., Roks, A.J., van den Meiracker, A.H., Danser, A.H., Hypertension: renin-angiotensin-aldosterone system alterations. Circ Res 116 (2015), 960–975.
6. [6] Jia, L., Li, Y., Xiao, C., Du, J., Angiotensin II induces inflammation leading to cardiac remodeling. Front. Biosci. (Landmark Ed.) 17 (2012), 221–231.
7. [7] Koller, A., Signaling pathways of mechanotransduction in arteriolar endothelium and smooth muscle cells in hypertension. Microcirculation 9 (2002), 277–294.
8. [8] Brown, J., Wang, H., Hajishengallis, G.N., Martin, M., TLR-signaling networks: an integration of adaptor molecules, kinases, and cross-talk. J. Dent. Res. 90 (2011), 417–427.
9. [9] Perret-Guillaume, C., Joly, L., Jankowski, P., Benetos, A., Benefits of the RAS blockade: clinical evidence before the ONTARGET study. J. Hypertens. Suppl. 27 (2009), S3–S7.
10. [10] Hou, F.F., Zhou, Q.G., Optimal dose of angiotensin-converting enzyme inhibitor or angiotensin II receptor blocker for renoprotection. Nephrology (Carlton) 15:Suppl. 2 (2010), 57–60.
11. [11] Taal, M.W., Brenner, B.M., Renoprotective benefits of RAS inhibition: from ACEI to angiotensin II antagonists. Kidney Int. 57 (2000), 1803–1817.
12. [12] Liu, H., Chen, Y.F., Li, F., Zhang, H.Y., Fructus Gardenia (Gardenia jasminoides J. Ellis) phytochemistry, pharmacology of cardiovascular, and safety with the perspective of new drugs development. J. Asian Nat. Prod. Res. 15 (2013), 94–110.
13. [13] Hughes, R.H., Silva, V.A., Ahmed, I., Shreiber, D.I., Morrison, B. 3rd., Neuroprotection by genipin against reactive oxygen and reactive nitrogen species-mediated injury in organotypic hippocampal slice cultures. Brain Res. 1543 (2014), 308–314.
14. [14] Guan, L., Feng, H., Gong, D., Zhao, X., Cai, L., Wu, Q., et al. Genipin ameliorates age-related insulin resistance through inhibiting hepatic oxidative stress and mitochondrial dysfunction. Exp. Gerontol. 48 (2013), 1387–1394.
15. [15] Kim, T.H., Yoon, S.J., Lee, S.M., Genipin attenuates sepsis by inhibiting Toll-like receptor signaling. Mol. Med. 18 (2012), 455–465.
16. [16] Wang, N., Zhu, M., Tsao, S.W., Man, K., Zhang, Z., Feng, Y., Up-regulation of TIMP-1 by genipin inhibits MMP-2 activities and suppresses the metastatic potential of human hepatocellular carcinoma. PLoS One, 7, 2012, e46318.
17. [17] Zhang, H.Y., Liu, H., Yang, M., Wei, S.F., Antithrombotic activities of aqueous extract from Gardenia jasminoides and its main constituent. Pharm. Biol. 51 (2013), 221–225.
18. [18] Labat, C., Lacolley, P., Lajemi, M., de Gasparo, M., Safar, M.E., Benetos, A., Effects of valsartan on mechanical properties of the carotid artery in spontaneously hypertensive rats under high-salt diet. Hypertension 38 (2001), 439–443.
19. [19] Livak, K.J., Schmittgen, T.D., Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta delta C(T)) method. Methods 25 (2001), 402–408.
20. [20] Dange, R.B., Agarwal, D., Masson, G.S., Vila, J., Wilson, B., Nair, A., et al. Central blockade of TLR4 improves cardiac function and attenuates myocardial inflammation in angiotensin II-induced hypertension. Cardiovasc Res 103 (2014), 17–27.
21. [21] Wang, Z., Zhang, L., Cui, X., Hao, T., Wang, C., Gu, X., et al. Biotransformation of geniposide by Synechocystis sp. PCC 6803 into genipin and its inhibitory effects on BEL-7402, Escherichia coli, and cyanobacteria. Ann. Microbiol. 65 (2015), 1303–1311.
22. [22] Tsm, T., Westly, J., Lee, T., Chen, C., Identification and determination of geniposide, genipin, gardenoside, and geniposidic acid from herbs by HPLC/photodiode-array detection. J. Liq. Chromatogr. 17 (1994), 2199–2205.
23. [23] Akao, T., Kobashi, K., Aburada, M., Enzymic studies on the animal and intestinal bacterial metabolism of geniposide. Biol. Pharm. Bull. 17 (1994), 1573–1576.
24. [24] Kl, U., Takeda, Y., Iwasaki, Y., Yoshizaki, F., Simultaneous estimation of geniposide and genipin in mouse plasma using high-performance liquid chromatography. Anal. Sci. 17 (2001), 1237–1239.
25. [25] Djerassi, C., Eisenbraun, E.J., Finnegan, R.A., Gilbert, B., Naturally occurring oxygen heterocyclics. IX. Isolation and characterization of genipin. J. Org. Chem. 25 (1960), 2174–2177.
26. [26] Mi, F.L., Shyu, S.S., Peng, C.K., Characterization of ring-opening polymerization of genipin and pH-dependent cross-linking reactions between chitosan and genipin. J. Polym. Sci. A 43 (2005), 1985–2000.
27. [27] Mi, F.L., Sung, H.W., Shyu, S.S., Synthesis and characterization of a novel chitosan-based network prepared using naturally occurring crosslinker. J. Polym. Sci. A 38 (2000), 2804–2814.
28. [28] Slusarewicz, P., Zhu, K., Hedman, T., Kinetic analysis of genipin degradation in aqueous solution. Nat. Prod. Commun. 5 (2010), 1853–1858.
29. [29] Suzuki, H., Yamazaki, M., Chiba, K., Uemori, Y., Sawanishi, H., Neuritogenic activities of L-alkyloxygenipins. Chem. Pharm. Bull. (Tokyo) 58 (2010), 168–171.
30. [30] Kwoh, C., Shannon, M.B., Miner, J.H., Shaw, A., Pathogenesis of nonimmune glomerulopathies. Annu. Rev. Pathol. 1 (2006), 349–374.
31. [31] Dilauro, M., Burns, K.D., Angiotensin-(1-7) and its effects in the kidney. ScientificWorldJournal 9 (2009), 522–535.
32. [32] Burns, W.C., Thomas, M.C., Angiotensin II and its role in tubular epithelial to mesenchymal transition associated with chronic kidney disease. Cells Tissues Organs 193 (2011), 74–84.
33. [33] Koo, H.J., Song, Y.S., Kim, H.J., Lee, Y.H., Hong, S.M., Kim, S.J., et al. Antiinflammatory effects of genipin, an active principle of gardenia. Eur. J. Pharmacol. 495 (2004), 201–208.
34. [34] Hughes, R.H., Silva, V.A., Ahmed, I., Shreiber, D.I., Morrison, B. 3rd., Neuroprotection by genipin against reactive oxygen and reactive nitrogen species-mediated injury in organotypic hippocampal slice cultures. Brain Res. 1543 (2014), 308–314.
35. [35] Guan, L., Feng, H., Gong, D., Zhao, X., Cai, L., Wu, Q., et al. Genipin ameliorates age-related insulin resistance through inhibiting hepatic oxidative stress and mitochondrial dysfunction. Exp. Gerontol. 48 (2013), 1387–1394.
36. [36] Hwa, J.S., Mun, L., Kim, H.J., Seo, H.G., Lee, J.H., Kwak, J.H., et al. Genipin selectively inhibits TNF-α-activated VCAM-1 but not ICAM-1 expression by upregulation of PPAR-γ in human endothelial cells. Korean J. Physiol. Pharmacol. 15 (2011), 157–162.
37. [37] Koriyama, Y., Chiba, K., Yamazaki, M., Suzuki, H., Muramoto, K., Kato, S., Long-acting genipin derivative protects retinal ganglion cells from oxidative stress models in vitro and in vivo through the Nrf2/antioxidant response element signaling pathway. J. Neurochem. 115 (2010), 79–91.
38. [38] Jeon, W.K., Hong, H.Y., Kim, B.C., Genipin up-regulates heme oxygenase-1 via PI3-kinase-JNK1/2-Nrf2 signaling pathway to enhance the anti-inflammatory capacity in RAW264.7 macrophages. Arch. Biochem. Biophys. 512 (2011), 119–125.
39. [39] Kim, E.K., Choi, E.J., Compromised MAPK signaling in human diseases: an update. Arch. Toxicol. 89 (2015), 867–882.
40. [40] Guo, Y.L., Baysal, K., Kang, B., Yang, L.J., Williamson, J.R., Correlation between sustained c-Jun N-terminal protein kinase activation and apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells. J. Biol. Chem. 273 (1998), 4027–4034.
41. [41] Wilmer, W.A., Tan, L.C., Dickerson, J.A., Danne, M., Rovin, B.H., Interleukin-1beta induction of mitogen-activated protein kinases in human mesangial cells. Role of oxidation. J. Biol. Chem. 272 (1997), 10877–10881.
42. [42] Urushihara, M., Takamatsu, M., Shimizu, M., Kondo, S., Kinoshita, Y., Suga, K., et al. ERK5 activation enhances mesangial cell viability and collagen matrix accumulation in rat progressive glomerulonephritis. Am. J. Physiol. Ren. Physiol. 298 (2010), F167–F176.
43. [43] Banerjee, A., Gerondakis, S., Coordinating TLR-activated signaling pathways in cells of the immune system. Immunol. Cell Biol. 85 (2007), 420–424.
44. [44] Robson, M.G., Toll-like receptors and renal disease. Nephron. Exp. Nephrol. 113 (2009), e1–e7.
45. [45] Leemans, J.C., Butter, L.M., Pulskens, W.P., Teske, G.J., Claessen, N., van der Poll, T., et al. The role of Toll-like receptor 2 in inflammation and fibrosis during progressive renal injury. PLoS One, 4, 2009, e5704.
46. [46] Pulskens, W.P., Rampanelli, E., Teske, G.J., Butter, L.M., Claessen, N., Luirink, I.K., et al. TLR4 promotes fibrosis but attenuates tubular damage in progressive renal injury. J. Am. Soc. Nephrol. 21 (2010), 1299–1308.
47. [47] Tang, S.C., Lai, K.N., The pathogenic role of the renal proximal tubular cell in diabetic nephropathy. Nephrol. Dial. Transplant. 27 (2012), 3049–3056.
48. [48] Liu, Y., Yin, H., Zhao, M., Lu, Q., TLR2 and TLR4 in autoimmune diseases: a comprehensive review. Clin. Rev. Allergy Immunol. 47 (2014), 136–147.