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Mitochondria: the birth place, battle ground and the site of melatonin metabolism in cells
Open accessAbstract
It was a surprising discovery when mitochondria, as the power houses of cells, were also found to synthesize the potent mitochondrial targeted antioxidant, melatonin. The melatonin synthetic enzyme serotonin N-acetyltransferase (SNAT) was found in matrix and also in the intermembrane space of mitochondria. We hypothesize that the melatonin synthesis occurs in the matrix due to substrate (N-acetyl co-enzyme A) availability while the intermembrane space may serve as the recycling pool of SNAT to regulate the melatonin circadian rhythm. Another surprise was that the melatonin membrane receptors, including MT1 and MT2, were also present in mitochondria. The protective effects of melatonin against neuronal injury induced by brain ischemia/reperfusion were proven to be mainly mediated by mitochondrial melatonin receptors rather than the cell surface membrane receptors which is contrary to the classical principle. In addition, melatonin metabolic enzyme has also been identified in the mitochondria. This enzyme can convert melatonin to N-acetylserotonin to strengthen the antitumor effects of melatonin. Thus, mitochondria are the generator, battle ground and metabolic sites of melatonin. The biological significance of the strong association between mitochondria and melatonin should be intensively investigated.
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“Recently obtained results indicate that mitochondria play an important role in the production, metabolism, and activity of melatonin (Tan et al. 2016; Tan and Reiter 2019).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Tan and Reiter 2019
In the citing paper
“Newer data indicate that the mitochondria are pivotal for several aspects of melatonin: its production, metabolism, and activity through receptors [35].”
From Is Melatonin the “Next Vitamin D”?: A Review of Emerging Science, Clinical Uses, Safety, and Dietary Supplements (2022) · cites this paper as [35]
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“The high mΔψ decreases the electron flow in the ETC and mitochondria enter the stagnation status, which results in electron leakage from the ETC and forms ROS.”
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“For post-miotic cells including neurons, myocardial cells and muscle most of the time melatonin inhibits mitochondrial fission and promotes fusion (151-153).”
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Melatonin Mitigates Mitochondrial Meltdown: Interactions with SIRT3
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“Thus, melatonin is referred as the mitochondrial targeted antioxidant (5, 89-91).”
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“In contrast, in plants many SNAT homologs have been identified in different species (7-9).”
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“Melatonin is a suitable selection for this purpose due to its antioxidative potency and its availability (25).”
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“The most likely precursors (proteobacteria) of mitochondria have the capacity to produce melatonin (35, 36).”
BackgroundLei, Q., Wang, L., Tan, D. X., Zhao, Y. Q., Zheng, X., Chen, H., Li, Q., Zuo, B., & Kong, J. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12096 · Cited by 108 · cited 1×
“In contrast, in plants many SNAT homologs have been identified in different species (7-9).”
BackgroundSelf-citationLu, J.-J., Fu, L., Tang, Z., Zhang, C., Qin, L., Wang, J., Yu, Z., Shi, D., Xiao, X., Xie, F., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6407 · Cited by 107
Mendivil‐Perez, M., Soto‐Mercado, V., Guerra‐Librero, A., Fernández-Gil, B. I., Florido, J., Shen, Y., Tejada, M. A., Capilla‐González, V., Rusanova, I., García‐Verdugo, J. M., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12415 · Cited by 106 · cited 2×
“For example, melatonin improves aging-related ATP deficiency in cybrids (96), restores the normal ATP production in a parkinsonian phenotype zebra fish which express high oxidative stress (88) and increases ATP levels in neural stem cells (NSCs) which require high energy to differentiate into oligodendrocytes and neur…”
BackgroundGalley, H. F., McCormick, B., Wilson, K. L., Lowes, D. A., Colvin, L., & Torsney, C. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12444 · Cited by 103
A Novel Metabolic Pathway of Melatonin: Oxidation by Cytochromec
Semak, I. V., Naumova, M., Корик, Е. О., Terekhovich, V., Wortsman, J., & Slominski, A. T. (2005) · Biochemistry · doi:10.1021/bi050202d · Cited by 103 · cited 1×
“Semak et al (60, 61) initially observed that melatonin was metabolized to form AFMK in mitochondria.”
BackgroundChang, C.-C., Huang, T.-Y., Chen, Y.-H., Huang, T., Lin, L.-C., Chang, Y.-J., & Hsia, S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9015765 · Cited by 103
Zhang, W., Chen, X., Su, S., Jia, Q., Ding, T., Zhu, Z., & Zhang, T. (2015) · Neurological Sciences · doi:10.1007/s10072-015-2357-0 · Cited by 102
Targeting Mitochondria and Reactive Oxygen Species-Driven Pathogenesis in Diabetic Nephropathy
Lindblom, R. S. J., Higgins, G. C., Coughlan, M. T., & de Haan, J. B. (2015) · The Review of Diabetic Studies · doi:10.1900/rds.2015.12.134 · Cited by 99
Yu, L., Liang, H., Lu, Z., Zhao, G., Zhai, M., Yang, Y., Yang, J. Z., Yi, D., Chen, W., Wang, X., et al. (2015) · Journal of Pineal Research · doi:10.1111/jpi.12272 · Cited by 97 · cited 1×
“AAC tightly binds to cardiolipin in the closed status (163).”
BackgroundMelatonin reduces oxidative neurotoxicity due to quinolinic acid:
Cabrera, J., Reiter, R. J., Tan, D. X., Qi, W., Sainz, R. M., Mayo, J. C., García, J. J., Kim, S. J., & El‐Sokkary, G. H. (2000) · Neuropharmacology · doi:10.1016/s0028-3908(99)00128-8 · Cited by 94
Self-citationMelatonin and cancer: From the promotion of genomic stability to use in cancer treatment
Farhood, B., Goradel, N. H., Mortezaee, K., Khanlarkhani, N., Najafi, M., & Sahebkar, A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27391 · Cited by 94
Byeon, Y., Lee, K., Park, Y., Park, S., & Back, K. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12080 · Cited by 91
Jang, H. S., Na, Y., Hong, K., Lee, S. H., Moon, S., Cho, M., Park, M., Lee, O., Chang, E. M., Lee, D. R., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12432 · Cited by 91
Evolution of arylalkylamine N-acetyltransferase: Emergence and divergence
Coon, S. L., & Klein, D. C. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.03.039 · Cited by 89 · cited 1×
“In most vertebrates, only one homolog of SNAT gene is detected and it is probably transferred from the proteobacteria (6).”
BackgroundYe, T., Yin, X., Yu, L., Zheng, S.-J., Cai, W., Wu, Y., & Feng, Y. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12531 · Cited by 89 · cited 1×
“In that study, the results indicated that during normal condition, a majority of melatonin was the product of ASMT as the last enzyme; however, under stressful conditions, the major part of melatonin was generated by catalytic activity of SNAT as the final enzyme (49).”
BackgroundChoi, G., Lee, H. Y., & Back, K. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12412 · Cited by 86 · cited 1×
“This alternative pathway for melatonin synthesis has been confirmed in plants (48).”
BackgroundMelatonin Balance the Autophagy and Apoptosis by Regulating UCP2 in the LPS-Induced Cardiomyopathy
Pan, P., Zhang, H., Su, L., Wang, X., & Liu, D. (2018) · Molecules · doi:10.3390/molecules23030675 · Cited by 84 · cited 1×
“Several reports have attributed melatonin’s protective effects on oxidative stress in different tissues to its ability to upregulate gene expression as well as the activation of UCP2 (136, 137).”
BackgroundChen, H., Chen, Y., Yang, C., Chen, K., Sung, P., Chiang, H., Chen, C., Chua, S. O., Chung, S., Chen, Y., et al. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12326 · Cited by 83
Melatonin prevents adverse myocardial infarction remodeling via Notch1/Mfn2 pathway
Pei, H., Du, J., Song, X., He, L., Zhang, Y., Li, X., Qiu, C., Zhang, Y., Hou, J., Feng, J., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.015 · Cited by 82 · cited 1×
“For post-miotic cells including neurons, myocardial cells and muscle most of the time melatonin inhibits mitochondrial fission and promotes fusion (151-153).”
BackgroundMetabolism of melatonin by cytochrome P450s in rat liver mitochondria and microsomes
Semak, I. V., Корик, Е. О., Antonova, M., Wortsman, J., & Slominski, A. T. (2008) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2008.00630.x · Cited by 80 · cited 2×
“was discussed in detail by two groups (60, 63).”
BackgroundMelatonin attenuates postmyocardial infarction injury via increasing Tom70 expression
Pei, H.-F., Hou, J.-N., Wei, F.-P., Xue, Q., Zhang, F., Peng, C.-F., Yang, Y., Tian, Y., Feng, J., Du, J., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12371 · Cited by 78
Yang, M., Tao, J., Chai, M., Wu, H., Wang, J., Li, G., He, C., Xie, L., Ji, P., Dai, Y., et al. (2017) · Molecules · doi:10.3390/molecules22122059 · Cited by 78 · cited 1×
“during the embryo development, melatonin seems not to inhibit mitochondrial fission capacity since melatonin supplement always promotes the normal distribution of mitochondria in these cells (144, 145).”
BackgroundMelatonin as a mitochondrial protector in neurodegenerative diseases
Wongprayoon, P., & Govitrapong, P. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2614-x · Cited by 76
Delivery of nascent polypeptides to the mitochondrial surface.
Beddoe, T., & Lithgow, T. (2002) · Biochimica et Biophysica Acta · doi:10.1016/s0167-4889(02)00262-8 · Cited by 74 · cited 1×
“The mitochondrial-targeted transient peptides are both necessary and sufficient for import of the proteins into mitochondria that contain them (45, 46).”
BackgroundKlingenspor, M., Fromme, T., Hughes, D. A., Manzke, L. H., Polymeropoulos, E. T., Riemann, T., Trzcionka, M., Hirschberg, V., & Jastroch, M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.006 · Cited by 74
Haghi‐Aminjan, H., Farhood, B., Rahimifard, M., Didari, T., Baeeri, M., Hassani, S., Hosseini, R., & Abdollahi, M. R. (2018) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2018.1513492 · Cited by 74
Melatonin promotes adipogenesis and mitochondrial biogenesis in 3T3‐L1 preadipocytes
Kato, H., Tanaka, G., Masuda, S., Ogasawara, J., Sakurai, T., Kizaki, T., Ohno, H., & Izawa, T. (2015) · Journal of Pineal Research · doi:10.1111/jpi.12259 · Cited by 72 · cited 1×
“melatonin increased the citrate synthase activity, and upregulated expression of PPAR-γ coactivator 1 α, nuclear respiratory factor-1, and transcription factor A (148); in liver and neurons, melatonin also enhanced mDNA level, mDNA copy numbers and oxidative phosphorylation proteins (149, 150).”
BackgroundYu, L., Fan, C., Li, Z., Zhang, J., Xue, X., Xu, Y., Zhao, G., Yang, Y., & Wang, H. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12375 · Cited by 72
Interaction of neurons and astrocytes underlies the mechanism of Aβ-induced neurotoxicity
Angelova, P. R., & Abramov, A. Y. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140153 · Cited by 71
Melatonin, mitochondria, and the metabolic syndrome
Cardinali, D. P., & Vigo, D. E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2611-0 · Cited by 70
Glucose‐based microbial production of the hormone melatonin in yeast Saccharomyces cerevisiae
Germann, S. M., Jacobsen, S. A. B., Schneider, K., et al. (2016) · Biotechnology Journal · doi:10.1002/biot.201500143 · Cited by 66 · cited 1×
“Yeasts use glucose as a starting material to synthesize melatonin (32).”
BackgroundNeuroprotection by Radical Avoidance: Search for Suitable Agents
Hardeland, R. (2009) · Molecules · doi:10.3390/molecules14125054 · Cited by 65
A Metabolomic Perspective of Melatonin Metabolism in the Mouse
Ma, X., Chen, C., Krausz, K. W., Idle, J. R., & Gonzalez, F. J. (2008) · Endocrinology · doi:10.1210/en.2007-1412 · Cited by 62
Karamitri, A., Plouffe, B., Bonnefond, A., Chen, M., Gallion, J., Guillaume, J.-L., Hegron, A., Boissel, M., Canouil, M., Langenberg, C., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aan6622 · Cited by 62
Silva, S. D. O., Ximenes, V. F., LIVRAMENTO, J. A., Catalani, L. H., & Čampa, A. (2005) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2005.00247.x · Cited by 61 · cited 1×
“amounts were far below its tissue or CSF levels (55, 56).”
BackgroundTwo types of brown adipose tissue in humans
Lidell, M. E., Betz, M. J., & Enerbäck, S. (2013) · Adipocyte · doi:10.4161/adip.26896 · Cited by 61
Petrosillo, G., Benedictis, V. D., Ruggiero, F. M., & Paradies, G. (2013) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9505-0 · Cited by 60
Urinary metabolites and antioxidant products of exogenous melatonin in the mouse
Ma, X., Idle, J., Krausz, K. W., et al. (2006) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2006.00321.x · Cited by 59 · cited 1×
“AFMK has been identified in urine of rats and humans (53, 54) and its blood level might associate with breast cancer of human (50); however, its urinary”
BackgroundSelf-citationByeon, Y., Lee, H. Y., Choi, D., & Back, K. (2014) · Journal of Experimental Botany · doi:10.1093/jxb/eru357 · Cited by 59
Sleep, Melatonin, and the Menopausal Transition: What Are the Links?
Jehan, S., Jean‐Louis, G., Zizi, F., Auguste, E. E., Pandi-Perumal, S. R., Gupta, R. M., Attarian, H. P., McFarlane, S. I., Hardeland, R., & Brzezinski, A. (2017) · Sleep Science · doi:10.5935/1984-0063.20170003 · Cited by 55
Thomas, A. P., Hoang, J. D., Vongbunyong, K. E., Nguyen, A., Rakshit, K., & Matveyenko, A. V. (2016) · Endocrinology · doi:10.1210/en.2016-1309 · Cited by 54
Woyda-Ploszczyca, A. M., & Jarmuszkiewicz, W. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.10.003 · Cited by 52 · cited 1×
“Different from the mtPTP, UCPs can be positively regulated to protect the mitochondria (117).”
BackgroundShrestha, S., Zhu, J., Wang, Q., Du, X., Liu, F., Jiang, J., Song, J., Xing, J., Sun, D., Hou, Q., et al. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4097 · Cited by 52
Govender, J., Loos, B., Marais, E., & Engelbrecht, A. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.06.031 · Cited by 50
Yu, Z., Tian, X.-G., Peng, Y., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12478 · Cited by 49 · cited 5×
“Tryp: tryptophan, TPH: tryptophan 5-hydroxylase, 5HTryp: 5-hydroxyltryptophan, AADC: aromatic amino acid decarboxylase, 5HT: 5-hydroxyltryptomine (serotonin), SNAT (formal AANAT): serotonin N-acetyltrasferase, NAS: N-acetylserotonin, ASMT (formally HIOMT): Nacetylserotonin methyltrasferase, MT: melatonin.”
BackgroundInfluentialMelatonin enhances hyperthermia‐induced apoptotic cell death in human leukemia cells
Quintana, C., Cabrera, J., Perdomo, J., Estévez, F., Loro-Ferrer, J. F., Reiter, R. J., & Quintana, J. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12356 · Cited by 48
Self-citationChen, C., Chen, C., Wang, S., Yeh, C., Su, S., Ueng, S., Chuang, W., Hsueh, C., & Wang, T. (2018) · Cancers · doi:10.3390/cancers10090320 · Cited by 48
Choroid plexus is an additional source of melatonin in the brain
Quintela, T., Gonçalves, I., da Silva, M. G., Duarte, A. C., Guedes, P. R., Andrade, K. H. S., Freitas, F., Talhada, D., Albuquerque, T., Tavares, S., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12528 · Cited by 46 · cited 15×
“In mitochondria, due to the presence of CP4501B1 and ASMT (39), N-acetyl serotonin is either the precursor or the product of melatonin (Fig.3).”
BackgroundInfluentialPark, S., Byeon, Y., Lee, H., et al. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12174 · Cited by 45
Waseem, M., Tabassum, H., & Parvez, S. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.08.005 · Cited by 42
Ahluwalia, A., Brzozowska, I. M., Hoa, N. T., Jones, M. K., & Tarnawski, A. S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722131115 · Cited by 41 · cited 1×
“To date, not only MT1 but also the MT2 are reportedly present in the mitochondria of the gastric endothelial cells (166).”
BackgroundSarti, P., Magnifico, M. C., Fabio Altieri, F., Mastronicola, D., & Arese, M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140611259 · Cited by 40 · cited 1×
“Couple of studies has shown that melatonin application indeed reduces the ATP production in tumor cells (138) and in transformed human skin cells (139).”
BackgroundMelatonin inhibits paraquat‐induced cell death in bovine preimplantation embryos
Pang, Y., Sun, Y., Sun, W., Du, W., Hao, H., Zhao, S., & Zhu, H. (2015) · Journal of Pineal Research · doi:10.1111/jpi.12297 · Cited by 40
Ryu, V., Zarebidaki, E., Albers, H. E., Xue, B., & Bartness, T. J. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2017.07.011 · Cited by 39
Liu, V., Yau, W., Tam, C. W., Yao, K., & Shiu, S. Y. W. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061130 · Cited by 37
Uncoupling proteins of invertebrates: A review
Słocińska, M., Barylski, J., & Jarmuszkiewicz, W. (2016) · IUBMB Life · doi:10.1002/iub.1535 · Cited by 37 · cited 1×
“32794/mr11250011 52 species and a variety of cell types (119, 120).”
Yun, C. W., Kim, S., Lee, J. H., & Lee, S. H. (2018) · Anticancer Research · doi:10.21873/anticanres.12681 · Cited by 36
Scarpelli, P. H., Tessarin‐Almeida, G., Viçoso, K. L., Lima, W. R., Borges‐Pereira, L., Meissner, K. A., Wrenger, C., Raffaello, A., Rizzuto, R., Pozzan, T., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12484 · Cited by 36
Lo, C., Lin, S., Chang, J., & Chien, Y. (2017) · Nutrients · doi:10.3390/nu9111187 · Cited by 36
Yang, M., Tao, J., Wu, H., Guan, S., Liu, L., Zhang, L., Deng, S., He, C., Ji, P., Liu, J., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7555 · Cited by 33 · cited 1×
“In contrast, Yang et al observed that the SNAT was present in the mitochondrial intermembrane space close to the outer membrane (42).”
BackgroundSun, B., Yang, S., Li, S., et al. (2018) · Medical Science Monitor · doi:10.12659/msm.909221 · Cited by 31 · cited 1×
“reports documented the inhibitory action of melatonin on mitophagy (157) and others report that melatonin promotes mitophagy depending on the study conditions and experimental models (84, 158, 159).”
BackgroundZheng, C., Man, C. D., Cobelli, C., Groop, L., Zhao, H., Bale, A. E., Shaw, M. M., Duran, E. J., Pierpont, B. M., Caprio, S., et al. (2015) · Obesity · doi:10.1002/oby.21030 · Cited by 30
Goñi, L., Cuervo, M., Milagro, F. I., & Martínez, J. A. (2014) · Lifestyle Genomics · doi:10.1159/000380951 · Cited by 29
Feng, J. H., Chen, X., Liu, R., et al. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1461215 · Cited by 29 · cited 1×
“In addition, it also stimulates the activity of the mitochondrial antioxidative enzymes, Mn-SOD in animals and also in plants (28-31).”
BackgroundMelatonin and the brain in photoperiodic mammals.
Hastings, M. H., Herbert, J., Martensz, N. D., et al. (1985) · Ciba Foundation symposium · doi:10.1002/9780470720981.ch5 · Cited by 27 · cited 1×
“In vertebrates, melatonin also serves as the signalling molecule to transduce environmental photoperiodic information to their neuroendocrine system (13-15).”
BackgroundRadioimmunoassay of N-acetyl-N-formyl-5-methoxykynuramine (AFMK): a melatonin oxidative metabolite.
Harthé, C., Claudy, D., Déchaud, H., et al. (2003) · Life Science · doi:10.1016/s0024-3205(03)00483-1 · Cited by 26 · cited 1×
“AFMK has been identified in urine of rats and humans (53, 54) and its blood level might associate with breast cancer of human (50); however, its urinary”
BackgroundHsiao, C., Peng, T., Peng, A. C., Reiter, R. J., Tanaka, M., Lai, Y., & Jou, M. (2012) · Journal of Pineal Research · doi:10.1111/jpi.12004 · Cited by 24
Self-citationGaudry, M. J., Campbell, K. L., & Jastroch, M. (2018) · Handbook of Experimental Pharmacology · doi:10.1007/164_2018_116 · Cited by 24 · cited 1×
“UCP1 is exclusively present in the mitochondria of brown adipose tissue (118); other family members (homologs) of UCPs including UCPs 2-5 are distributed in the mitochondria of different”
BackgroundCodenotti, S., Battistelli, M., Burattini, S., et al. (2015) · Oncology Report · doi:10.3892/or.2015.3987 · Cited by 22
Figueiro‐Silva, J., Antequera, D., Pascual, C., Revenga, M. D. L. F., Volt, H., Acuña-Castroviejo, D., Rodríguez-Franco, M. I., & Carro, E. (2018) · Cell Transplantation · doi:10.1177/0963689717721217 · Cited by 21 · cited 1×
“melatonin increased the citrate synthase activity, and upregulated expression of PPAR-γ coactivator 1 α, nuclear respiratory factor-1, and transcription factor A (148); in liver and neurons, melatonin also enhanced mDNA level, mDNA copy numbers and oxidative phosphorylation proteins (149, 150).”
BackgroundDíaz-Casado, M. E., Rusanova, I., Aranda‐Martínez, P., Fernández‐Ortiz, M., Sayed, R. K. A., Fernández-Gil, B. I., Hidalgo‐Gutiérrez, A., Escames, G., López, L. C., & Acuña-Castroviejo, D. (2017) · Zebrafish · doi:10.1089/zeb.2017.1479 · Cited by 21 · cited 2×
“For example, melatonin improves aging-related ATP deficiency in cybrids (96), restores the normal ATP production in a parkinsonian phenotype zebra fish which express high oxidative stress (88) and increases ATP levels in neural stem cells (NSCs) which require high energy to differentiate into oligodendrocytes and neur…”
BackgroundMelatonin Synthetic Analogs as Nitric Oxide Synthase Inhibitors
Camacho, M. E., Carriòn, M. D., Lopez-Cara, L. C., Entrena, A., Gallo, M. Á., Espinosa, A., Escames, G., & Acuna-Castroviejo, D. (2012) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955712800626674 · Cited by 20
Localizing acethyl-serotonin transferase by electron microscopy
Kerényi, N. A., Sótonyi, P., & Somogyi, E. (1975) · Histochemistry · doi:10.1007/bf02463562 · Cited by 18 · cited 1×
“This seems to support the observations of Kerenyi et al (43, 44) that SNAT product was observed in the mitochondrial intermembrane space of pinealocytes.”
ResultMadhu, P., Reddy, K. P., & Reddy, P. S. (2015) · Journal of Experimental Zoology Part A Ecological Genetics and Physiology · doi:10.1002/jez.1917 · Cited by 17
Neuroprotective effects of melatonin on erectile dysfunction in streptozotocin-induced diabetic rats
Zhang, J., Hui, Y., Zhou, F., et al. (2018) · International Urology and Nephrology · doi:10.1007/s11255-018-1989-4 · Cited by 15
Ma, C., Pathak, C., Jang, S., et al. (2014) · Biochimica et Biophysica Acta · doi:10.1016/j.bbapap.2014.07.011 · Cited by 15 · cited 1×
“A homolog of melatonin synthetic gene N-acetyltransferase (NAT) has been reported in archaea (2) and a structure of NAT in another archaea (Thermoplasma volcanium) has been identified belonging to N-acetyltransferase family member; it has the capacity to bind acetyl coenzyme A (3).”
BackgroundAkinci, A., Eşrefoğlu, M., Çetin, A., et al. (2015) · Archives of medical science : AMS · doi:10.5114/aoms.2015.54870 · Cited by 14
Wang, B.-Q., Yang, Q.-H., Xu, R.-K., et al. (2013) · Chinese Medical Journal · doi:10.3760/cma.j.issn.0366-6999.20131965 · Cited by 14 · cited 1×
“Couple of studies has shown that melatonin application indeed reduces the ATP production in tumor cells (138) and in transformed human skin cells (139).”
BackgroundUltrastructural Studies on the Pinealocyte Mitochondria During the Daytime and at Night
Krakowski, G., & Cieciura, L. (1985) · Journal of Pineal Research · doi:10.1111/j.1600-079x.1985.tb00712.x · Cited by 13 · cited 1×
“Decades ago, it was noted that the morphology of mitochondria in pinealocytes are dynamically changed during a 24-hour period (147).”
BackgroundKim, C. H., Jeung, E., & Yoo, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102929 · Cited by 13 · cited 1×
“In addition, it also stimulates the activity of the mitochondrial antioxidative enzymes, Mn-SOD in animals and also in plants (28-31).”
BackgroundAl-Sarraf, I., Kasabri, V. N., Akour, A. A., & Naffa, R. G. (2018) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2018-0016 · Cited by 9
Melatonin receptor 1B gene associated with hyperglycemia in bipolar disorder
Hukic, D. S., Lavebratt, C., Frisén, L., Backlund, L., Hilding, A., Gu, H. F., Östenson, C., Erlinge, D., Ehrenborg, E., Schalling, M., et al. (2016) · Psychiatric Genetics · doi:10.1097/ypg.0000000000000131 · Cited by 6
Biarrotte-Sorin, S., & Mayer, C. (2005) · Acta Crystallographica. Section F : Structural Biology and Crystallization Communications · doi:10.1107/s174430910500223x · Cited by 6 · cited 1×
“A homolog of melatonin synthetic gene N-acetyltransferase (NAT) has been reported in archaea (2) and a structure of NAT in another archaea (Thermoplasma volcanium) has been identified belonging to N-acetyltransferase family member; it has the capacity to bind acetyl coenzyme A (3).”
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Self-citationMelatonin: Roles in influenza, Covid‐19, and other viral infections
Anderson, G., & Reiter, R. J. (2020) · Reviews in Medical Virology · doi:10.1002/rmv.2109 · Cited by 212
“melatonin to be intimately associated with mitochondrial function, and thereby with immune system regulation.(6) The interactions of our “bacterial-driven” coexistence with viruses have provided a “War of the Worlds” from which plant and animal evolution have emerged, and in which evolution has acted to tolerate and l…”
BackgroundSelf-citation
Metadata
- Authors
- Tan, D.-X., & Reiter, R. J.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- ORCID
- Reiter, Russel. J.
- Venue
- Melatonin Research
- Publisher
- ST Bio-life
- Published
- 2019-02-28
- Volume
- 2
- Issue
- 1
- Pages
- 44-66
- ISSN
- 2641-0281 (ISSN-L)
- OpenAlex
- W2919912171
- Cited by
- 172
- References
- 168
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 12 · 2023: 20 · 2022: 20 · 2021: 38 · 2020: 41 · 2019: 32
- FWCI
- 18.08
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Melatonin Research (publishedVersion, cc-by)
- Topics
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Keywords
- melatonin synthesis, mitochondria, serotonin N-acetyltransferase, mitochondrial matrix, intermembrane space, melatonin receptors, MT1 receptor, MT2 receptor, cerebral ischemia-reperfusion injury, neuronal injury, N-acetylserotonin, melatonin metabolism, circadian rhythm, anticancer activity
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