Network Pharmacology Combined with Transcriptional Analysis to Unveil the Biological Basis of Astaxanthin in Reducing the Oxidative Stress Induced by Diabetes Mellitus

References

• Ambati RR, Phang SM, Ravi S, Aswathanarayana RG. Astaxanthin: sources, extraction, stability, biological activities and its commercial applications–a review. Mar Drugs. 2014;12:128–152.
   PubMed Web of Science ®Google Scholar
• Higuera-Ciapara I, Felix-Valenzuela L, Goycoolea FM. Astaxanthin: a review of its chemistry and applications. Crit Rev Food Sci Nutr. 2006;46:185–196. doi:10.1080/10408690590957188
   PubMed Web of Science ®Google Scholar
• Guerin M, Huntley ME, Olaizola M. Haematococcus astaxanthin: applications for human health and nutrition. Trends Biotechnol. 2003;21:210–216. doi:10.1016/S0167-7799(03)00078-7
   PubMed Web of Science ®Google Scholar
• Yuan JP, Peng J, Yin K, Wang JH. Potential health‐promoting effects of astaxanthin: a high‐value carotenoid mostly from microalgae. Mol Nutr Food Res. 2011;55:150–165.
   PubMed Web of Science ®Google Scholar
• Chatterjee S, Khunti K, Davies MJ. Type 2 diabetes. Lancet. 2017;389:2239–2251.
   PubMed Web of Science ®Google Scholar
• Kitade H, Chen G, Ni Y, Ota T. Nonalcoholic fatty liver disease and insulin resistance: new insights and potential new treatments. Nutrients. 2017;9:387. doi:10.3390/nu9040387
   PubMed Web of Science ®Google Scholar
• Yan T, Zhao Y, Zhang X, Lin X. Astaxanthin inhibits acetaldehyde-induced cytotoxicity in SH-SY5Y cells by modulating Akt/CREB and p38MAPK/ERK signaling pathways. Mar Drugs. 2016;14:56. doi:10.3390/md14030056
   PubMed Web of Science ®Google Scholar
• Sila A, Kamoun Z, Ghlissi Z, et al. Ability of natural astaxanthin from shrimp by-products to attenuate liver oxidative stress in diabetic rats. Pharmacol Rep. 2015;67:310–316. doi:10.1016/j.pharep.2014.09.012
   PubMedGoogle Scholar
• Dryden M. Reactive oxygen species: a novel antimicrobial. Int J Antimicrob Agents. 2018;51:299–303. doi:10.1016/j.ijantimicag.2017.08.029
   PubMed Web of Science ®Google Scholar
• Makni M, Fetoui H, Gargouri NK, Garoui EM, Zeghal N. Antidiabetic effect of flax and pumpkin seed mixture powder: effect on hyperlipidemia and antioxidant status in alloxan diabetic rats. J Diabetes Complications. 2011;25:339–345. doi:10.1016/j.jdiacomp.2010.09.001
   PubMed Web of Science ®Google Scholar
• Uchiyama K, Naito Y, Hasegawa G, Nakamura N, Takahashi J, Yoshikawa T. Astaxanthin protects β-cells against glucose toxicity in diabetic db/ db mice. Redox Rep. 2002;7:290–293. doi:10.1179/135100002125000811
   PubMed Web of Science ®Google Scholar
• Nishida Y, Nawaz A, Kado T, et al. Astaxanthin stimulates mitochondrial biogenesis in insulin resistant muscle via activation of AMPK pathway. J Cachexia Sarcopenia Muscle. 2020;11:241–258. doi:10.1002/jcsm.12530
   PubMed Web of Science ®Google Scholar
• Nakano M, Onodera A, Saito E, et al. Effect of astaxanthin in combination with α-tocopherol or ascorbic acid against oxidative damage in diabetic ODS rats. J Nutr Sci Vitaminol (Tokyo). 2008;54:329–334. doi:10.3177/jnsv.54.329
   PubMed Web of Science ®Google Scholar
• Nishigaki I, Rajendran P, Venugopal R, Ekambaram G, Sakthisekaran D, Nishigaki Y. Cytoprotective role of astaxanthin against glycated protein/iron chelate‐induced toxicity in human umbilical vein endothelial cells. Phytother Res. 2010;24:54–59. doi:10.1002/ptr.2867
   PubMed Web of Science ®Google Scholar
• Naito Y, Uchiyama K, Aoi W, et al. Prevention of diabetic nephropathy by treatment with astaxanthin in diabetic db/ db mice. Biofactors. 2004;20:49–59. doi:10.1002/biof.5520200105
   PubMed Web of Science ®Google Scholar
• Kim YJ, Kim YA, Yokozawa T. Protection against oxidative stress, inflammation, and apoptosis of high-glucose-exposed proximal tubular epithelial cells by astaxanthin. J Agric Food Chem. 2009;57:8793–8797.
   PubMed Web of Science ®Google Scholar
• Manabe E, Handa O, Naito Y, et al. Astaxanthin protects mesangial cells from hyperglycemia‐induced oxidative signaling. J Cell Biochem. 2008;103:1925–1937. doi:10.1002/jcb.21583
   PubMedGoogle Scholar
• Zheng J, Wu M, Wang H, et al. Network pharmacology to unveil the biological basis of health-strengthening herbal medicine in cancer treatment. Cancers. 2018;10(11):461. doi:10.3390/cancers10110461
   PubMed Web of Science ®Google Scholar
• Sun Y, Oberley LW, Li Y. A simple method for clinical assay of superoxide dismutase. Clin Chem. 1988;34:497–500. doi:10.1093/clinchem/34.3.497
   PubMed Web of Science ®Google Scholar
• Buege J, Aust S. Microsomal lipid peroxidation methods enzymol 52: 302–310, Find this article online. 1978.
   Google Scholar
• Ellman GL. Tissue sulfhydryl groups. Arch Biochem Biophys. 1959;82(1):70–77. doi:10.1016/0003-9861(59)90090-6
   PubMed Web of Science ®Google Scholar
• Roy A, Volgin D, Baby S, Kubin L, Lahiri S. Activation of HIF-1 alpha mRNA by hypoxia in isolated rat carotid body. FASEB J. 2002;16(5):A817–A817.
   Google Scholar
• Kuhn M, Szklarczyk D, Franceschini A, Von Mering C, Jensen LJ, Bork P. STITCH 3: zooming in on protein–chemical interactions. Nucleic Acids Res. 2012;40:D876–D880. doi:10.1093/nar/gkr1011
   PubMed Web of Science ®Google Scholar
• Grosdidier A, Zoete V, Michielin O. SwissDock, a protein-small molecule docking web service based on EADock DSS. Nucleic Acids Res. 2011;39:W270–W277. doi:10.1093/nar/gkr366
   PubMed Web of Science ®Google Scholar
• Johnson WT, Johnson LAK, Lukaski HC. Serum superoxide dismutase 3 (extracellular superoxide dismutase) activity is a sensitive indicator of Cu status in rats. J Nutr Biochem. 2005;16:682–692. doi:10.1016/j.jnutbio.2005.03.009
   PubMed Web of Science ®Google Scholar
• Shanklin J, Whittle E, Fox BG. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry. 1994;33:12787–12794. doi:10.1021/bi00209a009
   PubMed Web of Science ®Google Scholar
• Tabassum R, Rämö JT, Ripatti P, et al. Genetic architecture of human plasma lipidome and its link to cardiovascular disease. Nat Commun. 2019;10:1–14. doi:10.1038/s41467-019-11954-8
   PubMedGoogle Scholar
• Hasanvand D, Amiri I, Soleimani Asl S, Saidijam M, Shabab N, Artimani T. Effects of CeO2 nanoparticles on the HO-1, NQO1, and GCLC expression in the testes of diabetic rats. Can J Physiol Pharmacol. 2018;96:963–969. doi:10.1139/cjpp-2017-0784
   PubMedGoogle Scholar
• Henning RJ. Type-2 diabetes mellitus and cardiovascular disease. Future Cardiol. 2018;14:491–509. doi:10.2217/fca-2018-0045
   PubMed Web of Science ®Google Scholar
• Rao AR, Baskaran V, Sarada R, Ravishankar GA. In vivo bioavailability and antioxidant activity of carotenoids from microalgal biomass—A repeated dose study. Food Res Int. 2013;54:711–717.
   Google Scholar
• Ranga Rao A, Raghunath Reddy RL, Baskaran V, Sarada R, Ravishankar GA. Characterization of microalgal carotenoids by mass spectrometry and their bioavailability and antioxidant properties elucidated in rat model. J Agric Food Chem. 2010;58:8553–8559. doi:10.1021/jf101187k
   PubMed Web of Science ®Google Scholar
• Stewart JS, Lignell Å, Pettersson A, Elfving E, Soni MG. Safety assessment of astaxanthin-rich microalgae biomass: acute and subchronic toxicity studies in rats. Food Chem Toxicol. 2008;46:3030–3036. doi:10.1016/j.fct.2008.05.038
   PubMed Web of Science ®Google Scholar
• Falvella FS, Pascale RM, Gariboldi M, et al. Stearoyl-CoA desaturase 1 (Scd1) gene overexpression is associated with genetic predisposition to hepatocarcinogenesis in mice and rats. Carcinogenesis. 2002;23:1933–1936. doi:10.1093/carcin/23.11.1933
   PubMed Web of Science ®Google Scholar
• Arner P, Sahlqvist A-S, Sinha I, et al. The epigenetic signature of systemic insulin resistance in obese women. Diabetologia. 2016;59:2393–2405. doi:10.1007/s00125-016-4074-5
   PubMed Web of Science ®Google Scholar
• Nakamura BN, Lawson G, Chan JY, et al. Knockout of the transcription factor NRF2 disrupts spermatogenesis in an age-dependent manner. Free Radic Biol Med. 2010;49:1368–1379. doi:10.1016/j.freeradbiomed.2010.07.019
   PubMed Web of Science ®Google Scholar
• Wajda A, Łapczuk J, Grabowska M, et al. Nuclear factor E2-related factor-2 (Nrf2) expression and regulation in male reproductive tract. Pharmacol Rep. 2016;68:101–108. doi:10.1016/j.pharep.2015.07.005
   PubMedGoogle Scholar
• Philbrook NA, Winn LM. Sub-chronic sulforaphane exposure in CD-1 pregnant mice enhances maternal NADPH quinone oxidoreductase 1 (NQO1) activity and mRNA expression of NQO1, glutathione S-transferase, and glutamate-cysteine ligase: potential implications for fetal protection against toxicant exposure. Reprod Toxicol. 2014;43:30–37.
   PubMedGoogle Scholar
• Dinkova-Kostova AT, Talalay P. NAD(P)H: quinone acceptor oxidoreductase 1 (NQO1), a multifunctional antioxidant enzyme and exceptionally versatile cytoprotector. Arch Biochem Biophys. 2010;501:116–123. doi:10.1016/j.abb.2010.03.019
   PubMed Web of Science ®Google Scholar
• Zhao Y, Kong C, Chen X, et al. Repetitive exposure to low-dose X-irradiation attenuates testicular apoptosis in type 2 diabetic rats, likely via Akt-mediated Nrf2 activation. Mol Cell Endocrinol. 2016;422:203–210. doi:10.1016/j.mce.2015.12.012
   PubMed Web of Science ®Google Scholar
• Marino E, Batten M, Groom J, et al. Marginal-zone B-cells of nonobese diabetic mice expand with diabetes onset, invade the pancreatic lymph nodes, and present autoantigen to diabetogenic T-cells. Diabetes. 2008;57:395–404. doi:10.2337/db07-0589
   PubMed Web of Science ®Google Scholar
• Stolp J, Mariño E, Batten M, et al. Intrinsic molecular factors cause aberrant expansion of the splenic marginal zone B cell population in nonobese diabetic mice. J Immunol. 2013;191:97–109. doi:10.4049/jimmunol.1203252
   PubMed Web of Science ®Google Scholar
• Bashratyan R, Sheng H, Regn D, Rahman MJ, Dai YD. Insulinoma‐released exosomes activate autoreactive marginal zone‐like B cells that expand endogenously in prediabetic NOD mice. Eur J Immunol. 2013;43:2588–2597.
   PubMedGoogle Scholar
• Saito T, Chiba S, Ichikawa M, et al. Notch2 is preferentially expressed in mature B cells and indispensable for marginal zone B lineage development. Immunity. 2003;18:675–685. doi:10.1016/S1074-7613(03)00111-0
   PubMed Web of Science ®Google Scholar
• Tanigaki K, Han H, Yamamoto N, et al. Notch–RBP-J signaling is involved in cell fate determination of marginal zone B cells. Nat Immunol. 2002;3:443–450.
   PubMed Web of Science ®Google Scholar
• Hozumi K, Negishi N, Suzuki D, et al. Delta-like 1 is necessary for the generation of marginal zone B cells but not T cells in vivo. Nat Immunol. 2004;5:638–644. doi:10.1038/ni1075
   PubMed Web of Science ®Google Scholar
• Hampel F, Ehrenberg S, Hojer C, et al. CD19-independent instruction of murine marginal zone B-cell development by constitutive Notch2 signaling. Blood. 2011;118:6321–6331.
   PubMed Web of Science ®Google Scholar
• Witt CM, Won W-J, Hurez V, Klug CA. Notch2 haploinsufficiency results in diminished B1 B cells and a severe reduction in marginal zone B cells. J Immunol. 2003;171:2783–2788. doi:10.4049/jimmunol.171.6.2783
   PubMed Web of Science ®Google Scholar
• Tan JB, Xu K, Cretegny K, et al. Lunatic and manic fringe cooperatively enhance marginal zone B cell precursor competition for delta-like 1 in splenic endothelial niches. Immunity. 2009;30:254–263. doi:10.1016/j.immuni.2008.12.016
   PubMedGoogle Scholar