Polyamines as Universal Bioregulators across Kingdoms and Their role in Cellular Longevity and Death

References

• Agostinelli, E., Belli, F., Molinari, A., Condello, M., Palmigiani, P., Dalla Vedova, L., Marra, M., Seiler, N., and Arancia, G. 2006. Toxicity of enzymatic oxidation products of spermine to human melanoma cells (M14): sensitization by heat and MDL 72527. Biochim. Biophys. Acta. 1763:1040–1050. doi:10.1016/j.bbamcr.2006.07.014
   PubMed Web of Science ®Google Scholar
• Agostinelli, E., Marques, M., Calheiros, R., Gil, F., Tempera, G., Viceconte, N., Battaglia, V., Grancara, S., and Toninello, A. 2010a. Polyamines: fundamental characters in chemistry and biology. Amino Acids. 38:393–403. doi:10.1007/s00726-009-0396-7
   PubMed Web of Science ®Google Scholar
• Agostinelli, E., Tempera, G., Viceconte, N., Saccoccio, S., Battaglia, V., Grancara, S., Toninello, A., and Stevanato, R. 2010b. Potential anticancer application of polyamine oxidation products formed by amine oxidase: a new therapeutic approach. Amino Acids. 38:353–368. doi:10.1007/s00726-009-0431-8
   PubMed Web of Science ®Google Scholar
• Ahou, A., Martignago, D., Alabdallah, O., Tavazza, R., Stano, P., Macone, A., Pivato, M., Masi, A., Rambla, J. L., Vera-Sirera, F., Angelini, R., Federico, R., and Tavladoraki, P. 2014. A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines. J. Exp. Bot. 65:1585–1603. doi:10.1093/jxb/eru016
   PubMed Web of Science ®Google Scholar
• Al-Kafaji, G., Al-Muhtaresh, H. A., and Salem, A. H. 2021. Expression and clinical significance of miR‑1 and miR‑133 in pre‑diabetes. Biomed. Rep. 14:33. doi:10.3892/br.2021.1409
   PubMed Web of Science ®Google Scholar
• Alcázar, R., Marco, F., Cuevas, J. C., Patron, M., Ferrando, A., Carrasco, P., Tiburcio, A. F., and Altabella, T. 2006. Involvement of polyamines in plant response to abiotic stress. Biotechnol. Lett. 28:1867–1876. doi:10.1007/s10529-006-9179-3
   PubMed Web of Science ®Google Scholar
• Alexander, E. T., Mariner, K., Donnelly, J., Phanstiel, O., and Gilmour, S. K. 2020. Polyamine blocking therapy decreases survival of tumor-infiltrating immunosuppressive myeloid cells and enhances the antitumor efficacy of PD-1 blockade. Mol. Cancer Ther. 19:2012–2022. doi:10.1158/1535-7163.MCT-19-1116
   PubMed Web of Science ®Google Scholar
• Alexander, E. T., Minton, A., Peters, M. C., Phanstiel, O., and Gilmour, S. K. 2017. A novel polyamine blockade therapy activates an anti-tumor immune response. Oncotarget 8:84140–84152. doi:10.18632/oncotarget.20493
   PubMedGoogle Scholar
• Angelini, R., Tisi, A., Rea, G., Chen, M. M., Botta, M., Federico, R., and Cona, A. 2008. Involvement of polyamine oxidase in wound healing. Plant Physiol. 146:162–177. doi:10.1104/pp.107.108902
   PubMed Web of Science ®Google Scholar
• Asgher, M., Khan, M. I. R., Anjum, N. A., Verma, S., Vyas, D., Per, T. S., Masood, A., and Khan, N. A. 2018. Ethylene and polyamines in counteracting heavy metal phytotoxicity: a crosstalk perspective. J. Plant Growth Regul. 37:1050–1065. doi:10.1007/s00344-018-9823-x
   Web of Science ®Google Scholar
• Aye, I. L., Gong, S., Avellino, G., Barbagallo, R., Gaccioli, F., Jenkins, B. J., Koulman, A., Murray, A. J., Stephen Charnock-Jones, D., and Smith, G. C. 2022. Placental sex-dependent spermine synthesis regulates trophoblast gene expression through acetyl-coA metabolism and histone acetylation. Commun. Biol. 5:586. doi:10.1038/s42003-022-03530-6
   PubMed Web of Science ®Google Scholar
• Bachrach, U. 2005. Naturally occurring polyamines: interaction with macromolecules. Curr. Protein Pept. Sci. 6:559–566. doi:10.2174/138920305774933240
   PubMed Web of Science ®Google Scholar
• Bachrach, U. 2010. The early history of polyamine research. Plant Physiol. Biochem. 48:490–495. doi:10.1016/j.plaphy.2010.02.003
   PubMed Web of Science ®Google Scholar
• Bagni, N., and Tassoni, A. 2001. Biosynthesis, oxidation and conjugation of aliphatic polyamines in higher plants. Amino Acids. 20:301–317. doi:10.1007/s007260170046
   PubMed Web of Science ®Google Scholar
• Basu, S., Roychoudhury, A., and Sengupta, D. N. 2014. Deciphering the role of various cis-acting regulatory elements in controlling SamDC gene expression in rice. Plant Signal. Behav. 9:e28391. doi:10.4161/psb.28391
   PubMedGoogle Scholar
• Belda-Palazón, B., Almendáriz, C., Martí, E., Carbonell, J., and Ferrando, A. 2016. Relevance of the axis spermidine/eIF5A for plant growth and development. Front. Plant Sci. 7:245. doi:10.3389/fpls.2016.00245
   PubMed Web of Science ®Google Scholar
• Bell, E., and Malmberg, R. L. 1990. Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing. Mol. Gen. Genet. 224:431–436. doi:10.1007/BF00262438
   PubMedGoogle Scholar
• Biłas, R., Szafran, K., Hnatuszko-Konka, K., and Kononowicz, A. K. 2016. Cis-regulatory elements used to control gene expression in plants. Plant Cell. Tiss. Organ Cult. 127:269–287. doi:10.1007/s11240-016-1057-7
   Web of Science ®Google Scholar
• Biswas, M. S., and Mano, J. 2015. Lipid peroxide-derived short-chain carbonyls mediate hydrogen peroxide-induced and salt-induced programmed cell death in plants. Plant Physiol. 168:885–898. doi:10.1104/pp.115.256834
   PubMed Web of Science ®Google Scholar
• Biswas, M. S., and Mano, J. 2016. Reactive carbonyl species activate caspase-3-like protease to initiate programmed cell death in plants. Plant Cell Physiol. 57:1432–1442. doi:10.1093/pcp/pcw053
   PubMed Web of Science ®Google Scholar
• Brooks, W. H. 2013. Increased polyamines alter chromatin and stabilize autoantigens in autoimmune diseases. Front. Immunol. 4:91. doi:10.3389/fimmu.2013.00091
   PubMed Web of Science ®Google Scholar
• Burcham, P. C., Raso, A., and Kaminskas, L. M. 2012. Chaperone heat shock protein 90 mobilization and hydralazine cytoprotection against acrolein-induced carbonyl stress. Mol. Pharmacol. 82:876–886. doi:10.1124/mol.112.078956
   PubMed Web of Science ®Google Scholar
• Byers, T. L., Lakanen, J. R., Coward, J. K., and Pegg, A. E. 1994. The role of hypusine depletion in cytostasis induced by S-adenosyl-L-methionine decarboxylase inhibition: new evidence provided by 1-methylspermidine and 1,12-dimethylspermine. Biochem. J. 303 (Pt 2):363–368. doi:10.1042/bj3030363
   PubMed Web of Science ®Google Scholar
• Cervelli, M., Polticelli, F., Federico, R., and Mariottini, P. 2003. Heterologous expression and characterization of mouse spermine oxidase. J. Biol. Chem. 278:5271–5276. doi:10.1074/jbc.M207888200
   PubMed Web of Science ®Google Scholar
• Chattopadhyay, M. K., Park, M. H., and Tabor, H. 2008. Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine. Proc. Natl. Acad. Sci. U S A. U S A 105:6554–6559. doi:10.1073/pnas.0710970105
   PubMed Web of Science ®Google Scholar
• Chattopadhyay, M. K., Tabor, C. W., and Tabor, H. 2003. Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase. Proc. Natl. Acad. Sci. USA. 100:13869–13874. doi:10.1073/pnas.1835918100
   PubMed Web of Science ®Google Scholar
• Che, H., Ma, C., Li, H., Yu, F., Wei, Y., Chen, H., Wu, J., and Ren, Y. 2022. Rebalance of the polyamine metabolism suppresses oxidative stress and delays senescence in nucleus pulposus cells. Oxid. Med. Cell. Longev. 2022:8033353. doi:10.1155/2022/8033353
   PubMed Web of Science ®Google Scholar
• Chen, H. J., Wang, C. C., Chan, D. C., Chiu, C. Y., Yang, R. S., and Liu, S. H. 2019. Adverse effects of acrolein, a ubiquitous environmental toxicant, on muscle regeneration and mass. J. Cachexia. Sarcopenia Muscle. 10:165–176. doi:10.1002/jcsm.12362
   PubMed Web of Science ®Google Scholar
• Chen, K. Y. 1983. An 18000-dalton protein metabolically labeled by polyamines in various mammalian cell lines. Biochim. Biophys. Acta. 756:395–402. doi:10.1016/0304-4165(83)90350-1
   PubMedGoogle Scholar
• Cona, A., Rea, G., Angelini, R., Federico, R., and Tavladoraki, P. 2006. Functions of amine oxidases in plant development and defence. Trends Plant Sci. 11:80–88. doi:10.1016/j.tplants.2005.12.009
   PubMed Web of Science ®Google Scholar
• Cooper, H. L., Park, M. H., and Folk, J. E. 1982. Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth. Cell 29:791–797. doi:10.1016/0092-8674(82)90441-x
   PubMed Web of Science ®Google Scholar
• Cooper, H. L., Park, M. H., Folk, J. E., Safer, B., and Braverman, R. 1983. Identification of the hypusine-containing protein hy + as translation initiation factor eIF-4D. Proc. Natl. Acad. Sci. U S A. U S A 80:1854–1857. doi:10.1073/pnas.80.7.1854
   PubMed Web of Science ®Google Scholar
• Daimon, M., Sugiyama, K., Kameda, W., Saitoh, T., Oizumi, T., Hirata, A., Yamaguchi, H., Ohnuma, H., Igarashi, M., and Kato, T. 2003. Increased urinary levels of pentosidine, pyrraline and acrolein adduct in type 2 diabetes. Endocr. J. 50:61–67. doi:10.1507/endocrj.50.61
   PubMed Web of Science ®Google Scholar
• Dobrovolskaite, A., Gardner, R. A., Delcros, J.-G., and Phanstiel, O. 2022. Development of polyamine lassos as polyamine transport inhibitors. ACS Med. Chem. Lett. 13:319–326. doi:10.1021/acsmedchemlett.1c00557
   PubMed Web of Science ®Google Scholar
• Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., and Rodnina, M. V. 2013. EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339:85–88. doi:10.1126/science.1229017
   PubMed Web of Science ®Google Scholar
• Duguay, J., Jamal, S., Liu, Z., Wang, T. W., and Thompson, J. E. 2007. Leaf-specific suppression of deoxyhypusine synthase in Arabidopsis thaliana enhances growth without negative pleiotropic effects. J. Plant Physiol. 164:408–420. doi:10.1016/j.jplph.2006.02.001
   PubMed Web of Science ®Google Scholar
• Eisenberg, T., Abdellatif, M., Schroeder, S., Primessnig, U., Stekovic, S., Pendl, T., Harger, A., Schipke, J., Zimmermann, A., Schmidt, A., Tong, M., Ruckenstuhl, C., Dammbrueck, C., Gross, A. S., Herbst, V., Magnes, C., Trausinger, G., Narath, S., Meinitzer, A., Hu, Z., Kirsch, A., Eller, K., Carmona-Gutierrez, D., Büttner, S., Pietrocola, F., Knittelfelder, O., Schrepfer, E., Rockenfeller, P., Simonini, C., Rahn, A., Horsch, M., Moreth, K., Beckers, J., Fuchs, H., Gailus-Durner, V., Neff, F., Janik, D., Rathkolb, B., Rozman, J., De Angelis, M. H., Moustafa, T., Haemmerle, G., Mayr, M., Willeit, P., Von Frieling-Salewsky, M., Pieske, B., Scorrano, L., Pieber, T., Pechlaner, R., Willeit, J., Sigrist, S. J., Linke, W. A., Mühlfeld, C., Sadoshima, J., Dengjel, J., Kiechl, S., Kroemer, G., Sedej, S., and Madeo, F. 2016. Cardioprotection and lifespan extension by the natural polyamine spermidine. Nat. Med. 22:1428–1438. doi:10.1038/nm.4222
   PubMed Web of Science ®Google Scholar
• Eisenberg, T., Knauer, H., Schauer, A., Büttner, S., Ruckenstuhl, C., Carmona-Gutierrez, D., Ring, J., Schroeder, S., Magnes, C., Antonacci, L., Fussi, H., Deszcz, L., Hartl, R., Schraml, E., Criollo, A., Megalou, E., Weiskopf, D., Laun, P., Heeren, G., Breitenbach, M., Grubeck-Loebenstein, B., Herker, E., Fahrenkrog, B., Fröhlich, K.-U., Sinner, F., Tavernarakis, N., Minois, N., Kroemer, G., and Madeo, F. 2009. Induction of autophagy by spermidine promotes longevity. Nat. Cell Biol. 11:1305–1314. doi:10.1038/ncb1975
   PubMed Web of Science ®Google Scholar
• Faundes, V., Jennings, M. D., Crilly, S., Legraie, S., Withers, S. E., Cuvertino, S., Davies, S. J., Douglas, A. G. L., Fry, A. E., Harrison, V., Amiel, J., Lehalle, D., Newman, W. G., Newkirk, P., Ranells, J., Splitt, M., Cross, L. A., Saunders, C. J., Sullivan, B. R., Granadillo, J. L., Gordon, C. T., Kasher, P. R., Pavitt, G. D., and Banka, S. 2021. Impaired eIF5A function causes a Mendelian disorder that is partially rescued in model systems by spermidine. Nat. Commun. 12:833. doi:10.1038/s41467-021-21053-2
   PubMed Web of Science ®Google Scholar
• Frostesjö, L., Holm, I., Grahn, B., Page, A. W., Bestor, T. H., and Heby, O. 1997. Interference with DNA methyltransferase activity and genome methylation during F9 teratocarcinoma stem cell differentiation induced by polyamine depletion. J. Biol. Chem. 272:4359–4366. doi:10.1074/jbc.272.7.4359
   PubMed Web of Science ®Google Scholar
• Fuell, C., Elliott, K. A., Hanfrey, C. C., Franceschetti, M., and Michael, A. J. 2010. Polyamine biosynthetic diversity in plants and algae. Plant Physiol. Biochem. 48:513–520. doi:10.1016/j.plaphy.2010.02.008
   PubMed Web of Science ®Google Scholar
• Fukui, T., Soda, K., Takao, K., and Rikiyama, T. 2019. Extracellular spermine activates DNA methyltransferase 3A and 3B. Int. J. Mol. Sci. 20:1254. doi:10.3390/ijms20051254
   PubMed Web of Science ®Google Scholar
• Gerlin, L., Baroukh, C., and Genin, S. 2021. Polyamines: double agents in disease and plant immunity. Trends Plant Sci. 26:1061–1071. doi:10.1016/j.tplants.2021.05.007
   PubMed Web of Science ®Google Scholar
• Gerner, E. W., Mamont, P. S., Bernhardt, A., and Siat, M. 1986. Post-translational modification of the protein-synthesis initiation factor eIF-4D by spermidine in rat hepatoma cells. Biochem. J. 239:379–386. doi:10.1042/bj2390379
   PubMed Web of Science ®Google Scholar
• Gonzalez, M. E., Jasso‐Robles, F. I., Flores‐Hernández, E., Rodríguez‐Kessler, M., and Pieckenstain, F. L. 2021. Current status and perspectives on the role of polyamines in plant immunity. Ann. Appl. Biol. 178:244–255. doi:10.1111/aab.12670
   Web of Science ®Google Scholar
• Green, D. R. 2019. Polyamines and aging: a CLEAR connection? Mol. Cell. 76:5–7. doi:10.1016/j.molcel.2019.09.003
   PubMed Web of Science ®Google Scholar
• Guo, Y., Ye, Q., Deng, P., Cao, Y., He, D., Zhou, Z., Wang, C., Zaytseva, Y. Y., Schwartz, C. E., Lee, E. Y., Evers, B. M., Morris, A. J., Liu, S., and She, Q.-B. 2020. Spermine synthase and MYC cooperate to maintain colorectal cancer cell survival by repressing Bim expression. Nat. Commun. 11:3243. doi:10.1038/s41467-020-17067-x
   PubMed Web of Science ®Google Scholar
• Gutierrez, E., Shin, B. S., Woolstenhulme, C. J., Kim, J. R., Saini, P., Buskirk, A. R., and Dever, T. E. 2013. eIF5A promotes translation of polyproline motifs. Mol. Cell. 51:35–45. doi:10.1016/j.molcel.2013.04.021
   PubMed Web of Science ®Google Scholar
• Hackenberg, M., Gustafson, P., Langridge, P., and Shi, B. J. 2015. Differential expression of micro RNAs and other small RNAs in barley between water and drought conditions. Plant Biotechnol. J. 13:2–13. doi:10.1111/pbi.12220
   PubMed Web of Science ®Google Scholar
• Hajdinák, P., Czobor, Á., and Szarka, A. 2019. The potential role of acrolein in plant ferroptosis-like cell death. PLOS One. 14:e0227278. doi:10.1371/journal.pone.0227278
   PubMed Web of Science ®Google Scholar
• Hanauske-Abel, H., Park, M.-H., Hanauske, A.-R., Popowicz, A., Lalande, M., and Folk, J. 1994. Inhibition of the G1-S transition of the cell cycle by inhibitors of deoxyhypusine hydroxylation. Biochim. Biophys. Acta. 1221:115–124. doi:10.1016/0167-4889(94)90003-5
   PubMed Web of Science ®Google Scholar
• Handa, A. K., Fatima, T., and Mattoo, A. K. 2018. Polyamines: bio-molecules with diverse functions in plant and human health and disease. Front. Chem. 6:10. doi:10.3389/fchem.2018.00010
   PubMed Web of Science ®Google Scholar
• Hanfrey, C. C., Pearson, B. M., Hazeldine, S., Lee, J., Gaskin, D. J., Woster, P. M., Phillips, M. A., and Michael, A. J. 2011. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286:43301–43312. doi:10.1074/jbc.M111.307835
   PubMed Web of Science ®Google Scholar
• Hiramatsu, K., Sugimoto, M., Kamei, S., Hoshino, M., Kinoshita, K., Iwasaki, K., and Kawakita, M. 1997. Diagnostic and prognostic usefulness of N 1, N 8-diacetylspermidine and N 1, N 12-diacetylspermine in urine as novel markers of malignancy. J. Cancer Res. Clin. Oncol. 123:539–545. doi:10.1007/s004320050102
   PubMed Web of Science ®Google Scholar
• Hiramatsu, K., Takahashi, K., Yamaguchi, T., Matsumoto, H., Miyamoto, H., Tanaka, S., Tanaka, C., Tamamori, Y., Imajo, M., Kawaguchi, M., Toi, M., Mori, T., and Kawakita, M. 2005. N 1, N 12-diacetylspermine as a sensitive and specific novel marker for early-and late-stage colorectal and breast cancers. Clin. Cancer Res. 11:2986–2990. doi:10.1158/1078-0432.CCR-04-2275
   PubMed Web of Science ®Google Scholar
• Hussain, A., Saraiva, L. R., Ferrero, D. M., Ahuja, G., Krishna, V. S., Liberles, S. D., and Korsching, S. I. 2013. High-affinity olfactory receptor for the death-associated odor cadaverine. Proc. Natl. Acad. Sci. U S A. U S A 110:19579–19584. doi:10.1073/pnas.1318596110
   PubMed Web of Science ®Google Scholar
• Igarashi, K., and Kashiwagi, K. 2000. Polyamines: mysterious modulators of cellular functions. Biochem. Biophys. Res. Commun. 271:559–564. doi:10.1006/bbrc.2000.2601
   PubMed Web of Science ®Google Scholar
• Igarashi, K., and Kashiwagi, K. 2006. Polyamine modulon in Escherichia coli: genes involved in the stimulation of cell growth by polyamines. J. Biochem. 139:11–16. doi:10.1093/jb/mvj020
   PubMed Web of Science ®Google Scholar
• Igarashi, K., and Kashiwagi, K. 2010. Modulation of cellular function by polyamines. Int. J. Biochem. Cell Biol. 42:39–51. doi:10.1016/j.biocel.2009.07.009
   PubMed Web of Science ®Google Scholar
• Igarashi, K., and Kashiwagi, K. 2011. Protein-conjugated acrolein as a biochemical marker of brain infarction. Mol. Nutr. Food Res. 55:1332–1341. doi:10.1002/mnfr.201100068
   PubMed Web of Science ®Google Scholar
• Igarashi, K., and Kashiwagi, K. 2018. Effects of polyamines on protein synthesis and growth of Escherichia coli. J. Biol. Chem. 293:18702–18709. doi:10.1074/jbc.TM118.003465
   PubMed Web of Science ®Google Scholar
• Igarashi, K., and Kashiwagi, K. 2019. The functional role of polyamines in eukaryotic cells. Int. J. Biochem. Cell Biol. 107:104–115. doi:10.1016/j.biocel.2018.12.012
   PubMed Web of Science ®Google Scholar
• Imre, L., Niaki, E. F., Bosire, R., Nanasi, P., Jr, Nagy, P., Bacso, Z., Hamidova, N., Pommier, Y., Jordan, A., and Szabo, G. 2022. Nucleosome destabilization by polyamines. Arch. Biochem. Biophys. 722:109184. doi:10.1016/j.abb.2022.109184
   PubMed Web of Science ®Google Scholar
• Inal, B., Türktaş, M., Eren, H., Ilhan, E., Okay, S., Atak, M., Erayman, M., and Unver, T. 2014. Genome-wide fungal stress responsive miRNA expression in wheat. Planta 240:1287–1298. doi:10.1007/s00425-014-2153-8
   PubMed Web of Science ®Google Scholar
• Ioannidis, N. E., Zschiesche, W., Barth, O., Kotakis, C., Navakoudis, E., Humbeck, K., and Kotzabasis, K. 2014. The genetic reprogramming of polyamine homeostasis during the functional assembly, maturation, and senescence-specific decline of the photosynthetic apparatus in Hordeum vulgare. J. Plant Growth Regul. 33:77–90. doi:10.1007/s00344-013-9387-8
   Web of Science ®Google Scholar
• Kamada-Nobusada, T., Hayashi, M., Fukazawa, M., Sakakibara, H., and Nishimura, M. 2008. A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana. Plant Cell Physiol. 49:1272–1282. doi:10.1093/pcp/pcn114
   PubMed Web of Science ®Google Scholar
• Kambis, T. N., Tofilau, H., Gawargi, F. I., Chandra, S., and Mishra, P. K. 2021. Regulating polyamine metabolism by miRNAs in diabetic cardiomyopathy. Curr. Diab. Rep. 21:52. doi:10.1007/s11892-021-01429-w
   PubMed Web of Science ®Google Scholar
• Kano, Y., Soda, K., and Konishi, F. 2013. Suppression of LFA-1 expression by spermine is associated with enhanced methylation of ITGAL, the LFA-1 promoter area. PLoS One. 8:e56056. doi:10.1371/journal.pone.0056056
   PubMedGoogle Scholar
• Kiechl, S., Pechlaner, R., Willeit, P., Notdurfter, M., Paulweber, B., Willeit, K., Werner, P., Ruckenstuhl, C., Iglseder, B., Weger, S., Mairhofer, B., Gartner, M., Kedenko, L., Chmelikova, M., Stekovic, S., Stuppner, H., Oberhollenzer, F., Kroemer, G., Mayr, M., Eisenberg, T., Tilg, H., Madeo, F., and Willeit, J. 2018. Higher spermidine intake is linked to lower mortality: a prospective population-based study. Am. J. Clin. Nutr. 108:371–380. doi:10.1093/ajcn/nqy102
   PubMed Web of Science ®Google Scholar
• Kim, T. H., Nosella, M. L., Bolik-Coulon, N., Harkness, R. W., Huang, S. K., and Kay, L. E. 2023. Correlating histone acetylation with nucleosome core particle dynamics and function. Proc. Natl. Acad. Sci. U S A. U S A 120:e2301063120. doi:10.1073/pnas.2301063120
   PubMed Web of Science ®Google Scholar
• Kimes, B. W., and Morris, D. R. 1971. Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidized polyamines and acrolein. Biochim. Biophys. Acta. 228:235–244. doi:10.1016/0005-2787(71)90563-6
   PubMed Web of Science ®Google Scholar
• Kirschner, K. M., Braun, J. F. W., Jacobi, C. L., Rudigier, L. J., Persson, A. B., and Scholz, H. 2014. Amine oxidase copper-containing 1 (AOC1) is a downstream target gene of the wilms tumor protein, WT1, during kidney development. J. Biol. Chem. 289:24452–24462. doi:10.1074/jbc.M114.564336
   PubMed Web of Science ®Google Scholar
• Kumar, V., Thakur, J. K., and Prasad, M. 2021. Histone acetylation dynamics regulating plant development and stress responses. Cell. Mol. Life Sci. 78:4467–4486. doi:10.1007/s00018-021-03794-x
   PubMed Web of Science ®Google Scholar
• Kusano, T., Berberich, T., Tateda, C., and Takahashi, Y. 2008. Polyamines: essential factors for growth and survival. Planta 228:367–381. doi:10.1007/s00425-008-0772-7
   PubMed Web of Science ®Google Scholar
• Lasanajak, Y., Minocha, R., Minocha, S. C., Goyal, R., Fatima, T., Handa, A. K., and Mattoo, A. K. 2014. Enhanced flux of substrates into polyamine biosynthesis but not ethylene in tomato fruit engineered with yeast S-adenosylmethionine decarboxylase gene. Amino Acids. 46:729–742. doi:10.1007/s00726-013-1624-8
   PubMed Web of Science ®Google Scholar
• Lenis, Y. Y., Elmetwally, M. A., Maldonado-Estrada, J. G., and Bazer, F. W. 2017. Physiological importance of polyamines. Zygote 25:244–255. doi:10.1017/S0967199417000120
   PubMed Web of Science ®Google Scholar
• Liu, B., and Sun, G. 2017. Micro RNA s contribute to enhanced salt adaptation of the autopolyploid Hordeum bulbosum compared with its diploid ancestor. Plant J. 91:57–69. doi:10.1111/tpj.13546
   PubMed Web of Science ®Google Scholar
• Liu, J., Chang, X., Ding, B., Zhong, S., Peng, L., Wei, Q., Meng, J., and Yu, Y. 2019. PhDHS Is Involved in Chloroplast Development in Petunia. Front. Plant Sci. 10:284. doi:10.3389/fpls.2019.00284
   PubMed Web of Science ®Google Scholar
• Liu, L., Santora, R., Rao, J. N., Guo, X., Zou, T., Zhang, H. M., Turner, D. J., and Wang, J.-Y. 2003. Activation of TGF-β-Smad signaling pathway following polyamine depletion in intestinal epithelial cells. Am. J. Physiol. Gastrointest. Liver Physiol. 285:G1056–G1067. doi:10.1152/ajpgi.00151.2003
   PubMed Web of Science ®Google Scholar
• Liu, T., Huang, B., Chen, L., Xian, Z., Song, S., Chen, R., and Hao, Y. 2018. Genome-wide identification, phylogenetic analysis, and expression profiling of polyamine synthesis gene family members in tomato. Gene 661:1–10. doi:10.1016/j.gene.2018.03.084
   PubMed Web of Science ®Google Scholar
• Liu, X., Liu, S., Chen, X., Prasanna, B. M., Ni, Z., Li, X., He, Y., Fan, Z., and Zhou, T. 2022. Maize miR167-ARF3/30-polyamine oxidase 1 module-regulated H2O2 production confers resistance to maize chlorotic mottle virus. Plant Physiol. 189:1065–1082. doi:10.1093/plphys/kiac099
   PubMed Web of Science ®Google Scholar
• Liu, Z., Duguay, J., Ma, F., Wang, T. W., Tshin, R., Hopkins, M. T., Mcnamara, L., and Thompson, J. E. 2008. Modulation of eIF5A1 expression alters xylem abundance in Arabidopsis thaliana. J. Exp. Bot. 59:939–950. doi:10.1093/jxb/ern017
   PubMed Web of Science ®Google Scholar
• Locke, J. M., Bryce, J. H., and Morris, P. C. 2000. Contrasting effects of ethylene perception and biosynthesis inhibitors on germination and seedling growth of barley (Hordeum vulgare L.). J. Exp. Bot. 51:1843–1849. doi:10.1093/jexbot/51.352.1843
   PubMed Web of Science ®Google Scholar
• Lopez, J. P., Fiori, L. M., Gross, J. A., Labonte, B., Yerko, V., Mechawar, N., and Turecki, G. 2014. Regulatory role of miRNAs in polyamine gene expression in the prefrontal cortex of depressed suicide completers. Int. J. Neuropsychopharmacol. 17:23–32. doi:10.1017/S1461145713000941
   PubMed Web of Science ®Google Scholar
• Lou, Y. R., Ahmed, S., Yan, J., Adio, A. M., Powell, H. M., Morris, P. F., and Jander, G. 2020. Arabidopsis ADC1 functions as an Nδ‐acetylornithine decarboxylase. J. Integr. Plant Biol. 62:601–613. doi:10.1111/jipb.12821
   PubMed Web of Science ®Google Scholar
• Lou, Y. R., Bor, M., Yan, J., Preuss, A. S., and Jander, G. 2016. Arabidopsis NATA1 acetylates putrescine and decreases defense-related hydrogen peroxide accumulation. Plant Physiol. 171:1443–1455. doi:10.1104/pp.16.00446
   PubMed Web of Science ®Google Scholar
• Luka, Z., Mudd, S. H., and Wagner, C. 2009. Glycine N-methyltransferase and regulation of S-adenosylmethionine levels. J. Biol. Chem. 284:22507–22511. doi:10.1074/jbc.R109.019273
   PubMed Web of Science ®Google Scholar
• Ma, F., Liu, Z., Wang, T. W., Hopkins, M. T., Peterson, C. A., and Thompson, J. E. 2010. Arabidopsis eIF5A3 influences growth and the response to osmotic and nutrient stress. Plant. Cell Environ. 33:1682–1696. doi:10.1111/j.1365-3040.2010.02173.x
   PubMed Web of Science ®Google Scholar
• Madeo, F., Eisenberg, T., Büttner, S., Ruckenstuhl, C., and Kroemer, G. 2010. Spermidine: a novel autophagy inducer and longevity elixir. Autophagy 6:160–162. doi:10.4161/auto.6.1.10600
   PubMed Web of Science ®Google Scholar
• Mahajan, U. V., Varma, V. R., Griswold, M. E., Blackshear, C. T., An, Y., Oommen, A. M., Varma, S., Troncoso, J. C., Pletnikova, O., O'Brien, R., Hohman, T. J., Legido-Quigley, C., and Thambisetty, M. 2020. Dysregulation of multiple metabolic networks related to brain transmethylation and polyamine pathways in Alzheimer disease: a targeted metabolomic and transcriptomic study. PLOS Med. 17:e1003012. doi:10.1371/journal.pmed.1003012
   PubMed Web of Science ®Google Scholar
• Majumdar, R., Shao, L., Turlapati, S. A., and Minocha, S. C. 2017. Polyamines in the life of Arabidopsis: profiling the expression of S-adenosylmethionine decarboxylase (SAMDC) gene family during its life cycle. BMC Plant Biol. 17:264. doi:10.1186/s12870-017-1208-y
   PubMed Web of Science ®Google Scholar
• Mano, J., Ishibashi, A., Muneuchi, H., Morita, C., Sakai, H., Biswas, M. S., Koeduka, T., and Kitajima, S. 2017. Acrolein-detoxifying isozymes of glutathione transferase in plants. Planta 245:255–264. doi:10.1007/s00425-016-2604-5
   PubMed Web of Science ®Google Scholar
• Mano, J., Miyatake, F., Hiraoka, E., and Tamoi, M. 2009. Evaluation of the toxicity of stress-related aldehydes to photosynthesis in chloroplasts. Planta 230:639–648. doi:10.1007/s00425-009-0964-9
   PubMed Web of Science ®Google Scholar
• Mano, J. I., Tokushige, K., Mizoguchi, H., Fujii, H., and Khorobrykh, S. 2010. Accumulation of lipid peroxide-derived, toxic α, β-unsaturated aldehydes (E)-2-pentenal, acrolein and (E)-2-hexenal in leaves under photoinhibitory illumination. Plant Biotechnology 27:193–197. doi:10.5511/plantbiotechnology.27.193
   Web of Science ®Google Scholar
• Matsumoto, M. 2015. Polyamines and Longevity in Mammals. In: Kusano, T., Suzuki, H. (eds) Polyamines. Springer: Tokyo.
   Google Scholar
• Mattoo, A., Fatima, T., Upadhyay, R., and Handa, A. 2015. Polyamines in plants: biosynthesis from arginine, and metabolic, physiological and stress-response roles. Amino Acids in Higher Plants, D’Mello, JPF, Ed., CABI: Wallingford, UK, p. 177–194.
   Google Scholar
• Mattoo, A. K., Minocha, S. C., Minocha, R., and Handa, A. K. 2010. Polyamines and cellular metabolism in plants: transgenic approaches reveal different responses to diamine putrescine versus higher polyamines spermidine and spermine. Amino Acids. 38:405–413. doi:10.1007/s00726-009-0399-4
   PubMed Web of Science ®Google Scholar
• McKenna, J., Kapfhamer, D., Kinchen, J. M., Wasek, B., Dunworth, M., Murray-Stewart, T., Bottiglieri, T., Casero, R. A., and Gambello, M. J. 2018. Metabolomic studies identify changes in transmethylation and polyamine metabolism in a brain-specific mouse model of tuberous sclerosis complex. Hum. Mol. Genet. 27:2113–2124. doi:10.1093/hmg/ddy118
   PubMed Web of Science ®Google Scholar
• Michael, A. J., Furze, J. M., Rhodes, M. J., and Burtin, D. 1996. Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA. Biochem. J. 314 (Pt 1):, 241–248. doi:10.1042/bj3140241
   PubMed Web of Science ®Google Scholar
• Minguet, E. G., Vera-Sirera, F., Marina, A., Carbonell, J., and Blázquez, M. A. 2008. Evolutionary diversification in polyamine biosynthesis. Mol. Biol. Evol. 25:2119–2128. doi:10.1093/molbev/msn161
   PubMed Web of Science ®Google Scholar
• Mizoi, M., Yoshida, M., Saiki, R., Waragai, M., Uemura, K., Akatsu, H., Kashiwagi, K., and Igarashi, K. 2014. Distinction between mild cognitive impairment and Alzheimer’s disease by CSF amyloid β40 and β42, and protein-conjugated acrolein. Clin. Chim. Acta. 430:150–155. doi:10.1016/j.cca.2014.01.007
   PubMed Web of Science ®Google Scholar
• Moghe, A., Ghare, S., Lamoreau, B., Mohammad, M., Barve, S., Mcclain, C., and Joshi-Barve, S. 2015. Molecular mechanisms of acrolein toxicity: relevance to human disease. Toxicol. Sci. 143:242–255. doi:10.1093/toxsci/kfu233
   PubMed Web of Science ®Google Scholar
• Moschou, P. N., Sanmartin, M., Andriopoulou, A. H., Rojo, E., Sanchez-Serrano, J. J., and Roubelakis-Angelakis, K. A. 2008. Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis. Plant Physiol. 147:1845–1857. doi:10.1104/pp.108.123802
   PubMed Web of Science ®Google Scholar
• Muth, A., Pandey, V., Kaur, N., Wason, M., Baker, C., Han, X., Johnson, T. R., Altomare, D. A., and Phanstiel, O. 2014. Synthesis and biological evaluation of antimetastatic agents predicated upon dihydromotuporamine C and its carbocyclic derivatives. J. Med. Chem. 57:4023–4034. doi:10.1021/jm401906v
   PubMed Web of Science ®Google Scholar
• Nathanson, J. A., Hunnicutt, E. J., Kantham, L., and Scavone, C. 1993. Cocaine as a naturally occurring insecticide. Proc. Natl. Acad. Sci. U S A. U S A 90:9645–9648. doi:10.1073/pnas.90.20.9645
   PubMed Web of Science ®Google Scholar
• Navakoudis, E., and Kotzabasis, K. 2022. Polyamines: α bioenergetic smart switch for plant protection and development. J. Plant Physiol. 270:153618. doi:10.1016/j.jplph.2022.153618
   PubMed Web of Science ®Google Scholar
• Nishimura, K., Lee, S. B., Park, J. H., and Park, M. H. 2012. Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development. Amino Acids. 42:703–710. doi:10.1007/s00726-011-0986-z
   PubMed Web of Science ®Google Scholar
• Nishio, T., Yoshikawa, Y., Fukuda, W., Umezawa, N., Higuchi, T., Fujiwara, S., Imanaka, T., and Yoshikawa, K. 2018. Branched‐chain polyamine found in hyperthermophiles induces unique temperature‐dependent structural changes in genome‐size DNA. Chemphyschem 19:2299–2304. doi:10.1002/cphc.201800396
   PubMed Web of Science ®Google Scholar
• Ober, D., Gibas, L., Witte, L., and Hartmann, T. 2003. Evidence for general occurrence of homospermidine in plants and its supposed origin as by-product of deoxyhypusine synthase. Phytochemistry 62:339–344. doi:10.1016/s0031-9422(02)00553-8
   PubMed Web of Science ®Google Scholar
• Ober, D., and Hartmann, T. 1999. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. U S A. U S A 96:14777–14782. doi:10.1073/pnas.96.26.14777
   PubMed Web of Science ®Google Scholar
• Pagnussat, G. C., Yu, H. J., Ngo, Q. A., Rajani, S., Mayalagu, S., Johnson, C. S., Capron, A., Xie, L. F., Ye, D., and Sundaresan, V. 2005. Genetic and molecular identification of genes required for female gametophyte development and function in Arabidopsis. Development 132:603–614. doi:10.1242/dev.01595
   PubMed Web of Science ®Google Scholar
• Pálfi, P., Bakacsy, L., Kovács, H., and Szepesi, Á. 2021. Hypusination, a Metabolic Posttranslational Modification of eIF5A in Plants during Development and Environmental Stress Responses. Plants 10:1261. doi:10.3390/plants10071261
   Google Scholar
• Pällmann, N., Braig, M., Sievert, H., Preukschas, M., Hermans-Borgmeyer, I., Schweizer, M., Nagel, C. H., Neumann, M., Wild, P., Haralambieva, E., Hagel, C., Bokemeyer, C., Hauber, J., and Balabanov, S. 2015. Biological relevance and therapeutic potential of the hypusine modification system. J. Biol. Chem. 290:18343–18360. doi:10.1074/jbc.M115.664490
   PubMed Web of Science ®Google Scholar
• Park, M., Nishimura, K., Zanelli, C. F., and Valentini, S. R. 2010. Functional significance of eIF5A and its hypusine modification in eukaryotes. Amino Acids. 38:491–500. doi:10.1007/s00726-009-0408-7
   PubMed Web of Science ®Google Scholar
• Park, M. H. 2006. The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A). J. Biochem. 139:161–169. doi:10.1093/jb/mvj034
   PubMed Web of Science ®Google Scholar
• Park, M. H., Cooper, H. L., and Folk, J. E. 1981. Identification of hypusine, an unusual amino acid, in a protein from human lymphocytes and of spermidine as its biosynthetic precursor. Proc. Natl. Acad. Sci. U S A. U S A 78:2869–2873. doi:10.1073/pnas.78.5.2869
   PubMed Web of Science ®Google Scholar
• Park, M. H., and Igarashi, K. 2013. Polyamines and their metabolites as diagnostic markers of human diseases. Biomol. Ther. 21:1–9. doi:10.4062/biomolther.2012.097
   PubMed Web of Science ®Google Scholar
• Park, M. H., Joe, Y. A., and Kang, K. R. 1998. Deoxyhypusine synthase activity is essential for cell viability in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 273:1677–1683. doi:10.1074/jbc.273.3.1677
   PubMedGoogle Scholar
• Park, M. H., and Wolff, E. C. 2018. Hypusine, a polyamine-derived amino acid critical for eukaryotic translation. J. Biol. Chem. 293:18710–18718. doi:10.1074/jbc.TM118.003341
   PubMed Web of Science ®Google Scholar
• Park, M. H., Wolff, E. C., Lee, Y. B., and Folk, J. 1994. Antiproliferative effects of inhibitors of deoxyhypusine synthase. Inhibition of growth of Chinese hamster ovary cells by guanyl diamines. J. Biol. Chem. 269:27827–27832.
   PubMed Web of Science ®Google Scholar
• Parrish, R. R., Buckingham, S. C., Mascia, K. L., Johnson, J. J., Matyjasik, M. M., Lockhart, R. M., and Lubin, F. D. 2015. Methionine increases BDNF DNA methylation and improves memory in epilepsy. Ann. Clin. Transl. Neurol. 2:401–416. doi:10.1002/acn3.183
   PubMed Web of Science ®Google Scholar
• Parrotta, L., Tanwar, U. K., Aloisi, I., Sobieszczuk-Nowicka, E., Arasimowicz-Jelonek, M., and Del Duca, S. 2022. Plant transglutaminases: new insights in biochemistry, genetics, and physiology. Cells 11:1529. doi:10.3390/cells11091529
   PubMed Web of Science ®Google Scholar
• Patel, A. R., Li, J., Bass, B. L., and Wang, J.-Y. 1998. Expression of the transforming growth factor-β gene during growth inhibition following polyamine depletion. Am. J. Physiol. 275:C590–C598. doi:10.1152/ajpcell.1998.275.2.C590
   PubMedGoogle Scholar
• Patel, J., Ariyaratne, M., Ahmed, S., Ge, L., Phuntumart, V., Kalinoski, A., and Morris, P. F. 2017. Dual functioning of plant arginases provides a third route for putrescine synthesis. Plant Sci. 262:62–73. doi:10.1016/j.plantsci.2017.05.011
   PubMed Web of Science ®Google Scholar
• Pegg, A. E. 2008. Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator. Am. J. Physiol. Endocrinol. Metab. 294:E995–1010. doi:10.1152/ajpendo.90217.2008
   PubMed Web of Science ®Google Scholar
• Pegg, A. E. 2013. Toxicity of polyamines and their metabolic products. Chem. Res. Toxicol. 26:1782–1800. doi:10.1021/tx400316s
   PubMed Web of Science ®Google Scholar
• Perez, R. F., Tejedor, J. R., Bayon, G. F., Fernández, A. F., and Fraga, M. F. 2018. Distinct chromatin signatures of DNA hypomethylation in aging and cancer. Aging Cell. 17:e12744. doi:10.1111/acel.12744
   PubMed Web of Science ®Google Scholar
• Poidevin, L., Unal, D., Belda-Palazón, B., and Ferrando, A. 2019. Polyamines as Quality Control Metabolites Operating at the Post-Transcriptional Level. Plants (Basel) 8:109. doi:10.3390/plants8040109
   PubMedGoogle Scholar
• Pollard, K. J., Samuels, M. L., Crowley, K. A., Hansen, J. C., and Peterson, C. L. 1999. Functional interaction between GCN5 and polyamines: a new role for core histone acetylation. Embo J. 18:5622–5633. doi:10.1093/emboj/18.20.5622
   PubMed Web of Science ®Google Scholar
• Pucciarelli, S., Moreschini, B., Micozzi, D., De Fronzo, G. S., Carpi, F. M., Polzonetti, V., Vincenzetti, S., Mignini, F., and Napolioni, V. 2012. Spermidine and spermine are enriched in whole blood of nona/centenarians. Rejuvenation Res. 15:590–595. doi:10.1089/rej.2012.1349
   PubMed Web of Science ®Google Scholar
• Rao, J. N., Li, L., Bass, B. L., and Wang, J.-Y. 2000. Expression of the TGF-β receptor gene and sensitivity to growth inhibition following polyamine depletion. Am. J. Physiol. Cell Physiol. 279:C1034–C1044. doi:10.1152/ajpcell.2000.279.4.C1034
   PubMed Web of Science ®Google Scholar
• Raspaud, E., Chaperon, I., Leforestier, A., and Livolant, F. 1999. Spermine-induced aggregation of DNA, nucleosome, and chromatin. Biophys. J. 77:1547–1555. doi:10.1016/S0006-3495(99)77002-5
   PubMed Web of Science ®Google Scholar
• Robertson, L., Backer, J., Biemans, C., Van Doorn, J., Krab, K., and Reijnders, W. 2016. Antoni Van Leeuwenhoek: Master of the Minuscule, Brill, Leiden: Boston.
   Google Scholar
• Saiki, R., Nishimura, K., Ishii, I., Omura, T., Okuyama, S., Kashiwagi, K., and Igarashi, K. 2009. Intense correlation between brain infarction and protein-conjugated acrolein. Stroke 40:3356–3361. doi:10.1161/STROKEAHA.109.553248
   PubMed Web of Science ®Google Scholar
• Saiki, R., Park, H., Ishii, I., Yoshida, M., Nishimura, K., Toida, T., Tatsukawa, H., Kojima, S., Ikeguchi, Y., Pegg, A. E., Kashiwagi, K., and Igarashi, K. 2011. Brain infarction correlates more closely with acrolein than with reactive oxygen species. Biochem. Biophys. Res. Commun. 404:1044–1049. doi:10.1016/j.bbrc.2010.12.107
   PubMed Web of Science ®Google Scholar
• Saini, P., Eyler, D. E., Green, R., and Dever, T. E. 2009. Hypusine-containing protein eIF5A promotes translation elongation. Nature 459:118–121. doi:10.1038/nature08034
   PubMed Web of Science ®Google Scholar
• Sakamoto, A., Terui, Y., Uemura, T., Igarashi, K., and Kashiwagi, K. 2020. Polyamines regulate gene expression by stimulating translation of histone acetyltransferase mRNAs. J. Biol. Chem. 295:8736–8745. doi:10.1074/jbc.RA120.013833
   PubMed Web of Science ®Google Scholar
• Sakata, K., Kashiwagi, K., Sharmin, S., Ueda, S., Irie, Y., Murotani, N., and Igarashi, K. 2003. Increase in putrescine, amine oxidase, and acrolein in plasma of renal failure patients. Biochem. Biophys. Res. Commun. 305:143–149. doi:10.1016/s0006-291x(03)00716-2
   PubMed Web of Science ®Google Scholar
• Sánchez-Jiménez, F., Medina, M. Á., Villalobos-Rueda, L., and Urdiales, J. L. 2019. Polyamines in mammalian pathophysiology. Cell. Mol. Life Sci. 76:3987–4008. doi:10.1007/s00018-019-03196-0
   PubMed Web of Science ®Google Scholar
• Sasaki, K., Abid, R., and Miyazaki, M. 1996. Deoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae. FEBS Lett. 384:151–154. doi:10.1016/0014-5793(96)00310-9
   PubMed Web of Science ®Google Scholar
• Schipper, R. G., van den Heuvel, L.P., Verhofstad. A.A., De Abreu, R.A. 2007. Polyamines and DNA methylation in childhood leukaemia. Biochem. Soc. Trans. 35:331–335. doi:10.1042/BST0350331
   Google Scholar
• Schnier, J., Schwelberger, H., Smit-Mcbride, Z., Kang, H. A., and Hershey, J. 1991. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 11:3105–3114. doi:10.1128/mcb.11.6.3105-3114.1991
   PubMed Web of Science ®Google Scholar
• Schuller, A. P., Wu, C. C., Dever, T. E., Buskirk, A. R., and Green, R. 2017. eIF5A functions globally in translation elongation and termination. Mol. Cell. 66:194–205.e5. doi:10.1016/j.molcel.2017.03.003
   PubMed Web of Science ®Google Scholar
• Seiler, N. 2004. Catabolism of polyamines. Amino Acids. 26:217–233. doi:10.1007/s00726-004-0070-z
   PubMed Web of Science ®Google Scholar
• Sekhar, V., Andl, T., and Phanstiel, O. 2022. ATP13A3 facilitates polyamine transport in human pancreatic cancer cells. Sci. Rep. 12:4045. doi:10.1038/s41598-022-07712-4
   PubMed Web of Science ®Google Scholar
• Sequera-Mutiozabal, M. I., Erban, A., Kopka, J., Atanasov, K. E., Bastida, J., Fotopoulos, V., Alcázar, R., and Tiburcio, A. F. 2016. Global metabolic profiling of Arabidopsis polyamine oxidase 4 (AtPAO4) loss-of-function mutants exhibiting delayed dark-induced senescence. Front. Plant Sci. 7:173. doi:10.3389/fpls.2016.00173
   PubMed Web of Science ®Google Scholar
• Shiba, T., Mizote, H., Kaneko, T., Nakajima, T., Yasuo, K., and Sano, I. 1971. Hypusine, a new amino acid occurring in bovine brain: isolation and structural determination. Biochim. Biophys. Acta. 244:523–531. doi:10.1016/0304-4165(71)90069-9
   PubMedGoogle Scholar
• Shojaei Saadi, H. A., Gagné, D., Fournier, É., Baldoceda Baldeon, L. M., Sirard, M.-A., and Robert, C. 2016. Responses of bovine early embryos to S-adenosyl methionine supplementation in culture. Epigenomics 8:1039–1060. doi:10.2217/epi-2016-0022
   PubMed Web of Science ®Google Scholar
• Sobieszczuk-Nowicka, E. 2017. Polyamine catabolism adds fuel to leaf senescence. Amino Acids. 49:49–56. doi:10.1007/s00726-016-2377-y
   PubMed Web of Science ®Google Scholar
• Sobieszczuk-Nowicka, E., Kubala, S., Zmienko, A., Małecka, A., and Legocka, J. 2015a. From accumulation to degradation: reprogramming polyamine metabolism facilitates dark-induced senescence in barley leaf cells. Front. Plant Sci. 6:1198. doi:10.3389/fpls.2015.01198
   PubMed Web of Science ®Google Scholar
• Sobieszczuk-Nowicka, E., Zmienko, A., Samelak-Czajka, A., Łuczak, M., Pietrowska-Borek, M., Iorio, R., Del Duca, S., Figlerowicz, M., and Legocka, J. 2015b. Dark-induced senescence of barley leaves involves activation of plastid transglutaminases. Amino Acids. 47:825–838. doi:10.1007/s00726-014-1912-y
   PubMed Web of Science ®Google Scholar
• Soda, K., Kano, Y., Chiba, F., Koizumi, K., and Miyaki, Y. 2013. Increased polyamine intake inhibits age-associated alteration in global DNA methylation and 1, 2-dimethylhydrazine-induced tumorigenesis. PLOS One. 8:e64357. doi:10.1371/journal.pone.0064357
   PubMed Web of Science ®Google Scholar
• Stephenson, A., and Seidel, E. 2006. Analysis of the interactions of Nrf-2, PMF-1, and CSN-7 with the 5′-flanking sequence of the mouse 4E-BP1 gene. Life Sci. 79:1221–1227. doi:10.1016/j.lfs.2006.03.042
   PubMed Web of Science ®Google Scholar
• Stewart, T. M., Dunston, T. T., Woster, P. M., and Casero, R. A. 2018. Polyamine catabolism and oxidative damage. J. Biol. Chem. 293:18736–18745. doi:10.1074/jbc.TM118.003337
   PubMed Web of Science ®Google Scholar
• Tabor, C. W., and Tabor, H. 1984. Polyamines. Annu. Rev. Biochem. 53:749–790. doi:10.1146/annurev.bi.53.070184.003533
   PubMed Web of Science ®Google Scholar
• Tabor, C. W., Tabor, H., and Bachrach, U. 1964. Identification of the aminoaldehydes produced by the oxidation of spermine and spermidine with purified plasma amine oxidase. J. Biol. Chem. 239:2194–2203.
   PubMed Web of Science ®Google Scholar
• Takahashi, T., and Tong, W. 2015. Regulation and Diversity of Polyamine Biosynthesis in Plants. In: Kusano, T., Suzuki, H. (eds.), Polyamines. Springer: Tokyo.
   Google Scholar
• Tanwar, U. K., Stolarska, E., Paluch-Lubawa, E., Mattoo, A. K., Arasimowicz-Jelonek, M., and Sobieszczuk-Nowicka, E. 2022. Unraveling the genetics of polyamine metabolism in barley for senescence-related crop improvement. Int. J. Biol. Macromol. 221:585–603. doi:10.1016/j.ijbiomac.2022.09.006
   PubMed Web of Science ®Google Scholar
• Tari, I., and Csiszár, J. 2003. Effects of NO2− or NO3− supply on polyamine accumulation and ethylene production of wheat roots at acidic and neutral pH: implications for root growth. Plant Growth Regulation 40:121–128. doi:10.1023/A:1024235211395
   Web of Science ®Google Scholar
• Tassoni, A., Van Buuren, M., Franceschetti, M., Fornalè, S., and Bagni, N. 2000. Polyamine content and metabolism in Arabidopsis thaliana and effect of spermidine on plant development. Plant Physiol. Biochem. 38:383–393. doi:10.1016/S0981-9428(00)00757-9
   Web of Science ®Google Scholar
• Tavladoraki, P., Cona, A., Federico, R., Tempera, G., Viceconte, N., Saccoccio, S., Battaglia, V., Toninello, A., and Agostinelli, E. 2012. Polyamine catabolism: target for antiproliferative therapies in animals and stress tolerance strategies in plants. Amino Acids. 42:411–426. doi:10.1007/s00726-011-1012-1
   PubMed Web of Science ®Google Scholar
• Tavladoraki, P., Rossi, M. N., Saccuti, G., Perez-Amador, M. A., Polticelli, F., Angelini, R., and Federico, R. 2006. Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion. Plant Physiol. 141:1519–1532. doi:10.1104/pp.106.080911
   PubMed Web of Science ®Google Scholar
• Ten Dijke, P., Goumans, M. J., Itoh, F., and Itoh, S. 2002. Regulation of cell proliferation by Smad proteins. J. Cell. Physiol. 191:1–16. doi:10.1002/jcp.10066
   PubMed Web of Science ®Google Scholar
• Thomas, T., and Thomas, T. J. 2001. Polyamines in cell growth and cell death: molecular mechanisms and therapeutic applications. Cell. Mol. Life Sci. 58:244–258. doi:10.1007/PL00000852
   PubMed Web of Science ®Google Scholar
• Thomas, T., Tajmir-Riahi, H., and Thomas, T. 2016. Polyamine–DNA interactions and development of gene delivery vehicles. Amino Acids. 48:2423–2431. doi:10.1007/s00726-016-2246-8
   PubMed Web of Science ®Google Scholar
• Thompson, J. E., Hopkins, M. T., Taylor, C., and Wang, T. W. 2004. Regulation of senescence by eukaryotic translation initiation factor 5A: implications for plant growth and development. Trends Plant Sci. 9:174–179. doi:10.1016/j.tplants.2004.02.008
   PubMed Web of Science ®Google Scholar
• Tiburcio, A. F., Altabella, T., Bitrián, M., and Alcázar, R. 2014. The roles of polyamines during the lifespan of plants: from development to stress. Planta 240:1–18. doi:10.1007/s00425-014-2055-9
   PubMed Web of Science ®Google Scholar
• Torres, M. A., Jones, J. D., and Dangl, J. L. 2005. Pathogen-induced, NADPH oxidase-derived reactive oxygen intermediates suppress spread of cell death in Arabidopsis thaliana. Nat. Genet. 37:1130–1134. doi:10.1038/ng1639
   PubMed Web of Science ®Google Scholar
• Toumi, I., Pagoulatou, M. G., Margaritopoulou, T., Milioni, D., and Roubelakis-Angelakis, K. A. 2019. Genetically modified heat shock protein90s and polyamine oxidases in Arabidopsis reveal their interaction under heat stress affecting polyamine acetylation, oxidation and homeostasis of reactive oxygen species. Plants 8:323. doi:10.3390/plants8090323
   Google Scholar
• Tse, R.T.-H., Ding, X., Wong, C.Y.-P., Cheng, C.K.-L., Chiu, P.K.-F., Ng, C.-F. 2022.The Association between Spermidine/Spermine N1-Acetyltransferase (SSAT) and Human Malignancies. Int. J. Mol. Sci. 23:5926. doi:10.3390/ijms23115926
   Google Scholar
• Uchida, K., Kanematsu, M., Morimitsu, Y., Osawa, T., Noguchi, N., and Niki, E. 1998. Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins. J. Biol. Chem. 273:16058–16066. doi:10.1074/jbc.273.26.16058
   PubMed Web of Science ®Google Scholar
• Upadhyay, R. K., Fatima, T., Handa, A. K., and Mattoo, A. K. 2020. Polyamines and their biosynthesis/catabolism genes are differentially modulated in response to heat versus cold stress in tomato leaves (Solanum lycopersicum L.). Cells 9:1749. doi:10.3390/cells9081749
   PubMed Web of Science ®Google Scholar
• Upadhyay, R. K., Fatima, T., Handa, A. K., and Mattoo, A. K. 2021a. Differential association of free, conjugated, and bound forms of polyamines and transcript abundance of their biosynthetic and catabolic genes during drought/salinity stress in tomato (Solanum lycopersicum L.) Leaves. Front. Plant Sci. 12:743568. doi:10.3389/fpls.2021.743568
   PubMed Web of Science ®Google Scholar
• Upadhyay, R. K., Shao, J., and Mattoo, A. K. 2021b. Genomic analysis of the polyamine biosynthesis pathway in duckweed Spirodela polyrhiza L.: presence of the arginine decarboxylase pathway, absence of the ornithine decarboxylase pathway, and response to abiotic stresses. Planta 254:108. doi:10.1007/s00425-021-03755-5
   PubMed Web of Science ®Google Scholar
• Van De Poel, B., Bulens, I., Oppermann, Y., Hertog, M. L., Nicolai, B. M., Sauter, M., and Geeraerd, A. H. 2013. S‐adenosyl‐l‐methionine usage during climacteric ripening of tomato in relation to ethylene and polyamine biosynthesis and transmethylation capacity. Physiol. Plant. 148:176–188. doi:10.1111/j.1399-3054.2012.01703.x
   PubMed Web of Science ®Google Scholar
• Van Den Oever, S. P., and Mayer, H. K. 2022. Can oligomeric proanthocyanidins interfere with UHPLC analysis of spermidine in nutritional supplements? J. Food Compos. Anal. 109:104466. doi:10.1016/j.jfca.2022.104466
   Web of Science ®Google Scholar
• Vera-Sirera, F., Minguet, E. G., Singh, S. K., Ljung, K., Tuominen, H., Blázquez, M. A., and Carbonell, J. 2010. Role of polyamines in plant vascular development. Plant Physiol. Biochem. 48:534–539. doi:10.1016/j.plaphy.2010.01.011
   PubMed Web of Science ®Google Scholar
• Visvanathan, A., Ahmed, K., Even-Faitelson, L., Lleres, D., Bazett-Jones, D. P., and Lamond, A. I. 2013. Modulation of higher order chromatin conformation in mammalian cell nuclei can be mediated by polyamines and divalent cations. PLOS One. 8:e67689. doi:10.1371/journal.pone.0067689
   PubMed Web of Science ®Google Scholar
• Vujcic, S., Diegelman, P., Bacchi, C. J., Kramer, D. L., and Porter, C. W. 2002. Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Biochem. J. 367:665–675. doi:10.1042/BJ20020720
   PubMed Web of Science ®Google Scholar
• Walters, D. R. 2003. Polyamines and plant disease. Phytochem. 64:97–107. doi:10.1016/s0031-9422(03)00329-7
   Google Scholar
• Wahlfors, J., Hiltunen, H., Heinonen, K., Hamalainen, E., Alhonen, L. & Janne, J. 1992. Genomic hypomethylation in human chronic lymphocytic leukemia. Blood, 80:2074–80. doi:10.1182/blood.V80.8.2074.2074
   Google Scholar
• Wang, T. W., Lu, L., Wang, D., and Thompson, J. E. 2001a. Isolation and characterization of senescence-induced cDNAs encoding deoxyhypusine synthase and eucaryotic translation initiation factor 5A from tomato. J. Biol. Chem. 276:17541–17549. doi:10.1074/jbc.M008544200
   PubMed Web of Science ®Google Scholar
• Wang, T. W., Lu, L., Zhang, C. G., Taylor, C., and Thompson, J. E. 2003. Pleiotropic effects of suppressing deoxyhypusine synthase expression in Arabidopsis thaliana. Plant Mol. Biol. 52:1223–1235. doi:10.1023/b:plan.0000004332.80792.4d
   PubMed Web of Science ®Google Scholar
• Wang, T. W., Zhang, C. G., Wu, W., Nowack, L. M., Madey, E., and Thompson, J. E. 2005. Antisense suppression of deoxyhypusine synthase in tomato delays fruit softening and alters growth and development. Plant Physiol. 138:1372–1382. doi:10.1104/pp.105.060194
   PubMed Web of Science ®Google Scholar
• Wang, W., and Liu, J.-H. 2015. Genome-wide identification and expression analysis of the polyamine oxidase gene family in sweet orange (Citrus sinensis). Gene 555:421–429. doi:10.1016/j.gene.2014.11.042
   PubMed Web of Science ®Google Scholar
• Wang, X., Ying, W., Dunlap, K. A., Lin, G., Satterfield, M. C., Burghardt, R. C., Wu, G., and Bazer, F. W. 2014. Arginine decarboxylase and agmatinase: an alternative pathway for de novo biosynthesis of polyamines for development of mammalian conceptuses. Biol. Reprod. 90:84. doi:10.1095/biolreprod.113.114637
   PubMed Web of Science ®Google Scholar
• Wang, Y., Devereux, W., Stewart, T. M., and Casero, R. A. 1999. Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermineN 1-Acetyltransferase gene. J. Biol. Chem. 274:22095–22101. doi:10.1074/jbc.274.31.22095
   PubMed Web of Science ®Google Scholar
• Wang, Y., Devereux, W., Woster, P. M., Stewart, T. M., Hacker, A., and Casero, R. A. Jr, 2001b. Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Research 61:5370–5373.
   PubMed Web of Science ®Google Scholar
• Waragai, M., Yoshida, M., Mizoi, M., Saiki, R., Kashiwagi, K., Takagi, K., Arai, H., Tashiro, J., Hashimoto, M., Iwai, N., Uemura, K., and Igarashi, K. 2012. Increased protein-conjugated acrolein and amyloid-β40/42 ratio in plasma of patients with mild cognitive impairment and Alzheimer’s disease. J. Alzheimers. Dis. 32:33–41. doi:10.3233/JAD-2012-120253
   PubMed Web of Science ®Google Scholar
• Wirth, A., Wolf, B., Huang, C.-K., Glage, S., Hofer, S. J., Bankstahl, M., Bär, C., Thum, T., Kahl, K. G., Sigrist, S. J., Madeo, F., Bankstahl, J. P., and Ponimaskin, E. 2021. Novel aspects of age-protection by spermidine supplementation are associated with preserved telomere length. Geroscience. 43:673–690. doi:10.1007/s11357-020-00310-0
   PubMed Web of Science ®Google Scholar
• Wöhl, T., Klier, H., Ammer, H., Lottspeich, F., and Magdolen, V. 1993. The HYP2 gene of Saccharomyces cerevisiae is essential for aerobic growth: characterization of different isoforms of the hypusine-containing protein Hyp2p and analysis of gene disruption mutants. Mol. Gen. Genet. 241:305–311. doi:10.1007/BF00284682
   PubMedGoogle Scholar
• Wood, P. L., Khan, M. A., and Moskal, J. R. 2007. The concept of “aldehyde load” in neurodegenerative mechanisms: cytotoxicity of the polyamine degradation products hydrogen peroxide, acrolein, 3-aminopropanal, 3-acetamidopropanal and 4-aminobutanal in a retinal ganglion cell line. Brain Res. 1145:150–156. doi:10.1016/j.brainres.2006.10.004
   PubMed Web of Science ®Google Scholar
• Wu, D., von Roepenack-Lahaye, E., Buntru, M., de Lange, O., Schandry, N., Pérez-Quintero, A. L., Weinberg, Z., Lowe-Power, T. M., Szurek, B., Michael, A. J., Allen, C., Schillberg, S., and Lahaye, T. 2019. A plant pathogen type III effector protein subverts translational regulation to boost host polyamine levels. Cell Host Microbe. 26:638–649. e5. doi:10.1016/j.chom.2019.09.014
   PubMed Web of Science ®Google Scholar
• Yamamoto, D., Shima, K., Matsuo, K., Nishioka, T., Chen, C. Y., Hu, G.-F., Sasaki, A., and Tsuji, T. 2010. Ornithine decarboxylase antizyme induces hypomethylation of genome DNA and histone H3 lysine 9 dimethylation (H3K9me2) in human oral cancer cell line. PloS One. 5:e12554. doi:10.1371/journal.pone.0012554
   PubMed Web of Science ®Google Scholar
• Yamauchi, Y., Hasegawa, A., Mizutani, M., and Sugimoto, Y. 2012. Chloroplastic NADPH-dependent alkenal/one oxidoreductase contributes to the detoxification of reactive carbonyls produced under oxidative stress. FEBS Lett. 586:1208–1213. doi:10.1016/j.febslet.2012.03.013
   PubMed Web of Science ®Google Scholar
• Yin, L., Mano, J., Wang, S., Tsuji, W., and Tanaka, K. 2010. The involvement of lipid peroxide-derived aldehydes in aluminum toxicity of tobacco roots. Plant Physiol. 152:1406–1417. doi:10.1104/pp.109.151449
   PubMed Web of Science ®Google Scholar
• Yoda, H., Hiroi, Y., and Sano, H. 2006. Polyamine oxidase is one of the key elements for oxidative burst to induce programmed cell death in tobacco cultured cells. Plant Physiol. 142:193–206. doi:10.1104/pp.106.080515
   PubMed Web of Science ®Google Scholar
• Yoda, H., Yamaguchi, Y., and Sano, H. 2003. Induction of hypersensitive cell death by hydrogen peroxide produced through polyamine degradation in tobacco plants. Plant Physiol. 132:1973–1981. doi:10.1104/pp.103.024737
   PubMed Web of Science ®Google Scholar
• Yoshida, M., Tomitori, H., Machi, Y., Katagiri, D., Ueda, S., Horiguchi, K., Kobayashi, E., Saeki, N., Nishimura, K., Ishii, I., Kashiwagi, K., and Igarashi, K. 2009. Acrolein, IL-6 and CRP as markers of silent brain infarction. Atherosclerosis 203:557–562. doi:10.1016/j.atherosclerosis.2008.07.022
   PubMed Web of Science ®Google Scholar
• Yu, Y., Jin, C., Sun, C., Wang, J., Ye, Y., Zhou, W., Lu, L., and Lin, X. 2016. Inhibition of ethylene production by putrescine alleviates aluminium-induced root inhibition in wheat plants. Sci. Rep. 6:18888. doi:10.1038/srep18888
   PubMed Web of Science ®Google Scholar
• Zahedi, K., Huttinger, F., Morrison, R., Murray-Stewart, T., Casero, R. A., and Strauss, K. I. 2010. Polyamine catabolism is enhanced after traumatic brain injury. J. Neurotrauma. 27:515–525. doi:10.1089/neu.2009.1097
   PubMed Web of Science ®Google Scholar
• Zeesman, S., Kjaergaard, S., Hove, H. D., Kirchhoff, M., Stevens, J. M., and Nowaczyk, M. J. 2012. Microdeletion in distal 17p13.1: a recognizable phenotype with microcephaly, distinctive facial features, and intellectual disability. Am. J. Med. Genet. A. 158a:1832–1836. doi:10.1002/ajmg.a.35508
   PubMed Web of Science ®Google Scholar
• Zhang, H., Alsaleh, G., Feltham, J., Sun, Y., Napolitano, G., Riffelmacher, T., Charles, P., Frau, L., Hublitz, P., Yu, Z., Mohammed, S., Ballabio, A., Balabanov, S., Mellor, J., and Simon, A. K. 2019. Polyamines control eIF5A hypusination, TFEB translation, and autophagy to reverse B cell senescence. Mol. Cell. 76:110–125. e9. doi:10.1016/j.molcel.2019.08.005
   PubMed Web of Science ®Google Scholar
• Zhao, J., Missihoun, T. D., and Bartels, D. 2017. The role of Arabidopsis aldehyde dehydrogenase genes in response to high temperature and stress combinations. J. Exp. Bot. 68:4295–4308. doi:10.1093/jxb/erx194
   PubMed Web of Science ®Google Scholar