The effect of 2-hexadecenal on the formation of reactive oxygen and chlorine species (ROCS) in neutrophils stimulated to phagocytosis has been determined by the chemiluminescence method. It has been established that at low concentrations this aldehyde demonstrates a priming effect on the cells, enhancing ROCS production, and at higher concentrations — significantly suppresses this process. Comparison of the results of chemiluminescence and fluorescence analysis of the cell characteristics suggests that 2-hexadecenal is a signaling molecule, which exhibits the properties of the neutrophil function regulator by modifying intracellular signaling processes associated with changes in ROCS production, cytoskeleton reorganization, increase in the level of unbound calcium ions in the cytoplasm, reduction of mitochondrial membrane potential. It also induces apoptosis.
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C. Nathan, Nat. Rev. Immunol., 6, 173–182 (2006).
T. N. Mayadas, X. Cullere, and C. A. Lowell, Annu. Rev. Pathol., 9, 181–218 (2014).
B. Amulic, C. Cazalet, G. L. Hayes, K. D. Metzler, and A. Zychlinsky, Annu. Rev. Immunol., 30, 459–489 (2012).
R. Grecian, M. K. B. Whyte, and S. R. Walmsley, Br. Med. Bul., 128, 5–14 (2018).
A. C. Carr, C. L. Hawkins, S. R. Thomas, R. Stocker, and B. Frei, Free Radic. Biol. Med., 30, No. 5, 526–536 (2001).
J. M. Robinson, Histochem. Cell Biol., 130, 281–297 (2008).
J. Arnhold and J. Flemmig, Arch. Biochem. Biophys., 500, No. 1, 92–106 (2010).
Yu. A. Vladimirov and Ye. V. Proskurnina, Uspekhi Biol. Khim., 49, 341–388 (2009).
T. Kuznetsova, T. Kulahava, I. Zholnerevich, N. Amaegberi, G. Semenkova, O. Shadyro, J. and Arnhold, Mol. Immunol., 87, 317–324 (2017).
G. Semenkova, I. Zholnerevich, T. Kulahava, and Z. Kvacheva, Free Rad. Biol. Med., 120, Suppl. 1, S100 (2018).
A. A. Krjukov, G. N. Semenkova, S. N. Cherenkevich, and V. Gerein, BioFactors, 26, 283–292 (2006).
B. Halliwell, M. V. Clement, and L. H. Longa, FEBS Lett., 486, 10–13 (2000).
M. M. Tarpey, D. A. Wink, and M. B. Grisham, Am. J. Physiol. Regul. Integr. Comp. Physiol., 286, 431–444 (2004).
F. Caldefie-Che′zet, S. Walrand, C. Moinard, A. Tridon, J. Chassagne, and M.-P. Vasson, Clin. Chim. Acta, 319, 9–17 (2002).
C. P. LeBel, H. Ischiropoulos, and S. C. Bondy, Chem. Res. Toxicol., 5, 227–231 (1992).
M. Karlsson, T. Kurz, U. T. Brunk, S. E. Nilsson, and C. I. Frennesson, Biochem. J., 428, 183–190 (2010).
S. L. Hempel, G. R. Buettner, Y. Q. O′Malley, D. A. Wessels, and D. M. Flaherty, Free Radic. Biol. Med., 27, 146–159 (1999).
B. Kalyanaramana, V. Darley-Usmar, K. J. A. Davies, P. A. Dennery, H. J. Formanc, M. B. Grisham, G. E. Mann, K. Moore, L. J. Roberts II, and H. Ischiropoulos, Free Radic. Biol. Med., 52, No. 1, 1–6 (2012).
N. Bartke and Y. A. Hannun, J. Lipid Res., 50, 591–596 (2009).
O. Shadyro, A. Lisovskaya, G. Semenkova, I. Edimecheva, and N. Amaegberi, Lipid Insight., 8, 1–9 (2015).
N. V. Amaegberi, G. N. Semenkova, A. G. Lisovskaya, Z. B. Kvacheva, and O. I. Shadyro, Biofizika, 64, No. 3, 544–551 (2019).
N. V. Amaegberi, G. N. Semenkova, Z. B. Kvacheva, A. G. Lisovskaya, S. V. Pinchuk, and O. I. Shadyro, Cell Biochem. Funct., 1–9 (2019).
A. Kumar, H. S. Byun, R. Bittman, and J. Saba, Cell Signal., 23, 1144–1152 (2011).
Z. Liu, Y. Gong, H. S. Byun, and R. Bittman, New J. Chem., 34, 470–475 (2010)
A. Böyum, Scand. J. Immunol., 5, 9–15 (1976).
F. Kato, M. Tanaka, and K. Nakamura, Toxicol. in Vitro, 13, 923–929 (1999).
D. Shugar, Biochim. Biophys. Acta, 8, 302–309 (1952).
F. Sivandzade, A. Bhalerao, and L. Cucullo, Bio. Protoc., 9, No. 1, 1–13 (2019).
R. A. Hirst, C. Harrison, K. Hirota, and D. G. Lambert, Methods in Molecular Biology, Calcium Signaling Protocols, 2nd edn., Humana Press Inc., Totowa (1997), pp. 37–45.
A. Ishaque and M. Al-Rubeai, In: Methods in Biotechnology, Animal Cell Biotechnology, Methods and Protocols, 2nd edn., Humana Press Inc., Totowa (2007), pp. 285–299.
A. I. Kavalenka, G. N. Semenkova, and S. N. Cherenkevich, Cell Tissue Biol., 1, No. 6, 551–559 (2007).
J. Zhang, X. Wang, V. Vikash, Q. Ye, D. Wu, Y. Liu, and W. Dong, Oxid. Med. Cell. Longev. (2016); ID 4350965, https://doi.org/10.1155/2016/4350965.
A. Mo′csai, B. Walzog, and C. A. Lowell, Cardiovasc. Res., 107, 373–385 (2015).
B. M. Babior, J. D. Lambeth, and W. Nauseef, Arch. Biochem. Biophys., 397, 342–344 (2002).
B. Samuelsson, Z. Rheumatol., 50, Suppl. 1, 3–6 (1991).
V. S. Hanna and E. A. A. Hafez, J. Adv. Res., 11, 23–32 (2018).
K. Futosi, S. Fodor, and A. Mócsai, Int. Immunopharmacol., 17, 638–650 (2013).
M. Reyes-Reyes, N. Mora, A. Zentella, and C. Rosales, J. Cell Sci., 114, 1579–1589 (2001).
A. Bertram and K. Ley, Arch. Immunol. Ther. Exp. (Warsz), 59, No. 2, 79–87 (2011).
G. Huang, L. Z. Shi, and H. Chi, Cytokine, 48, No. 3, 161–169 (2009).
D. Kim and C. L. Haynes, Analyst, 138, No. 22, 1–17 (2013).
S. Elmore, Toxicol. Pathol., 35, 495–516 (2007).
P. Pinton, C. Giorgi, R. Siviero, E. Zecchini, and R. Rizzuto, Oncogen., 27, No. 50, 6407–6418 (2008).
E. A. Papakonstanti and C. Stournaras, FEBS Lett., 582, 2120–2127 (2008).
G. Forgacs, S. H. Yook, P. A. Janmey, H. Jeong, and C. G. Burd, J. Cell Sci., 117, 2769–2775 (2004).
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Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 86, No. 4, pp. 582–589, July–August 2019.
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Amaegberi, N.V., Semenkova, G.N., Lisovskaya, A.G. et al. Investigation of the Regulatory Effect of 2-Hexadecenal on Neutrophils by the Chemiluminescence Method. J Appl Spectrosc 86, 636–642 (2019). https://doi.org/10.1007/s10812-019-00871-9
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DOI: https://doi.org/10.1007/s10812-019-00871-9