THE COMPONENTS OF THE EXTRINSIC APOPTOTIC PATHWAY IN MATURE ERYTHROCYTES (BRIEF REVIEW)
Abstract
The programmed cell death – apoptosis plays an important role in the life of the nucleated cells. It is a vital component of different processes, like normal cell cycle, embryonic development, development and functioning of the immune system, etc. There are at least two signalling pathways that lead to apoptosis of the nucleated cells – the extrinsic pathway of the apoptosis and the intrinsic pathway of the apoptosis. The extrinsic pathway of apoptosis begins outside a cell, when conditions in the extracellular environment determine that a cell must die. The intrinsic pathway of apoptosis begins when an injury occurs within the cell and the resulting stress activates the apoptotic pathway. Erythrocytes, like nucleated cells, may undergo a form of suicidal cell death called eryptosis. The fact is that erythrocytes, which are devoid of nuclei, contain most components of the receptor-dependent apoptotic pathway. The components of the extrinsic and intrinsic apoptotic pathways play a significant role at the different stages of erythropoiesis and even in mature erythrocytes. Mature erythrocytes contain most components of the receptor-dependent apoptotic pathway, however, common inducers of apoptosis do not activate this pathway. Studies based on an animal model suggested that other stimuli, such as ROS or cholesterol accumulation, could activate the extrinsic apoptotic pathway. The data also demonstrate important effects of caspases-8 and caspase-3 on red cell membrane and membrane skeleton proteins, which are crucial in determining cell shape and erythrocyte deformability and therefore erythrocyte survival in the circulation. Understanding all of these processes may help to explain the pathophysiology of anemia. Despite extensive research, it is still unclear what the direct mechanism of apoptosis of erythroid cells is.
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P. Arese, F. Turrini, and E. Schwarzer, “Band 3/complement mediated recognition and removal of normally senescent and pathological human erythrocytes,” Cellular Physiology and Biochemistry, 2005, vol. 16, no. 4–6, pp. 133–146.
G. J. C. G. M. Bosman, F. L. A. Willekens, and J. M. Werre, “Erythrocyte aging: a more than superficial resemblance to apoptosis?” Cellular Physiology and Biochemistry, 2005 vol. 16, no. 1– 3, pp. 1–8.
H. U. Lutz, “Innate immune and non-immune mediators of erythrocyte clearance,” Cellular and Molecular Biology, vol. 50, no. 2, pp. 107–116, 2004
Föller, M., Huber, S. M., and Lang, F. (2008b). Erythrocyte programmed cell death. IUBMB Life 2008, vol. 60, 661–668.
K.A.Pyrshev, A.S.Klymchenko, G. Csucs, A.P Demchenko `Apoptosis and eryptosis; Striking differences on biomembrane level~, BBA Biomembranes, 2018, vol. 1860, pp. 1362-1372.
Repsold, L., and Joubert, A. M. Eryptosis: an erythrocyte’s suicidal type of cell death. Biomed. Res. Intern. 2018:9405617.
Lang, E., and Lang, F. Triggers, inhibitors, mechanisms, and significance of eryptosis: the suicidal erythrocyte death. Biomed. Res. Intern. 2015:513-518.
PA Lang, DS Kempe, V.Tanneur, BA Klark, S. Missina, G. Hesler, SM Huber, F.Lang, T.Wieder Stimulation of erythrocyte ceramide formation by platelet-activating factor J.Cell Sci., 2005, v. 118, pp1233-1243.
K. S. Lang, C. Duranton, H. Poehlmann et al., “Cation channels trigger apoptotic death of erythrocytes,” Cell Death and Differentiation, 2003, vol. 10, no. 2, pp. 249–256.
F. Lang, M. Abed, E. Lang, and M. Foller, “Oxidative stress and suicidal erythrocyte death,”Antioxidants & Redox Signaling,2014, vol. 21, no. 1, pp. 138–153.
B. A. Klarl, P. A. Lang, D. S. Kempe et al., “Protein kinase C mediates erythrocyte “programmed cell death” following glucose depletion,” The American Journal of Physiology-Cell Physiology, 2006, vol. 290, no. 1, pp. C244–C253.
M. Foller, H. Mahmud, S. Gu et al., “Participation of leukotriene C4 in the regulation of suicidal erythrocyte death,” Journal of Physiology and Pharmacology, 2009, vol. 60, no. 3, pp. 135–143.
J. P. Nicolay, G. Liebig, O. M. Niemoeller et al., “Inhibition of suicidal erythrocyte death by nitric oxide,” Pflugers Archiv European Journal of Physiology, 2008, vol. 456, no. 2, pp. 293–305.
D. M. Vota, R. L. Crisp, A. B. Nesse, and D. C. Vittori, “Oxidative stress due to aluminum exposure induces eryptosis which is prevented by erythropoietin,” 2012, Journal of Cellular Biochemistry, vol. 113, no. 5, pp. 1581–1589.
Senthil Velan Bhoopalan, Lily Jun-shen Huang, Mitchell J. Weiss, Erythropoetin regulation of Erythropoietin regulation of red blood cell production: from bench to bedside and back. F1000Research 2020, 9; 1-17.
Listowski, M.A.; Heger, E.; Bogusławska, D.M.; Machnicka, B.; Kuliczkowski, K.; Leluk, J.; Sikorski, A.F. MicroRNAs: Fine tuning of erythropoiesis. Cell. Mol. Biol. Lett. 2012, 18, 34–46.
Testa, U. Apoptotic mechanisms in the control of erythropoiesis. Leukemia 2004, 18, 1176–1199.
Dzierzak, E.; Philipsen, S. Erythropoiesis: Development and Differentiation. Cold Spring Harb. Perspect. Med. 2013, 3, a011601.
Dicato, M.; Morceau, F.; Diederich, M. Pro-inflammatory cytokine-mediated anemia: Regarding molecular mechanisms of erythropoiesis. Mediators Inflamm. 2009, 2009, 405016.
Li, J.; Yin, Q.; Wu, H. Structural Basis of Signal Transduction in the TNF Receptor Superfamily. Adv. Immunol. 2013, 119, 135–153.
Jacobs-Helber, S.M.; Roh, K.; Bailey, D.; Dessypris, E.N.; Ryan, J.J.; Chen, J.; Wickrema, A.; Barber, D.L.; Dent, P.; Sawyer, S.T. Tumor necrosis factor-alpha expressed constitutively in erythroid cells or induced by erythropoietin has negative and stimulatory roles in normal erythropoiesis and erythroleukemia. Blood 2003, 101, 524–531.
Grigorakaki, C.; Morceau, F.; Chateauvieux, S.; Dicato, M.; Diederich, M. Tumor necrosis factor alpha-mediated inhibition of erythropoiesis involves GATA-1/GATA-2 balance impairment and PU.1 over-expression. Biochem. Pharmacol. 2011, 82, 156–166.
Gibellini, D.; Bassini, A.; Re, M.C.; Ponti, C.; Miscia, S.; Gonelli, A.; La Placa, M.; Zauli, G. Stroma-derived factor 1alpha induces a selective inhibition of human erythroid development via the functional upregulation of Fas/CD95 ligand. Br. J. Haematol. 2000, 111, 432–440.
Boehm, D.; Mazurier, C.; Giarratana, M.C.; Darghouth, D.; Faussat, A.M.; Harmand, L.; Douay, L. Caspase-3 Is Involved in the Signalling in Erythroid Differentiation by Targeting Late Progenitors. PLoS ONE 2013, 8, e62303.
Carlile, G.W.; Smith, D.H.; Wiedmann, M. Caspase-3 has a nonapoptotic function in erythroid maturation. Blood 2004, 103, 4310–4316
Berg, C.P.; Engels, I.H.; Rothbart, A.; Lauber, K.; Renz, A.; Schlosser, S.F.; Schulze-Osthoff, K.; Wesselborg, S. Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis. Cell Death Differ. 2001, 8, 1197–1206.
Sagan, D.; Jermnim, N.; Tangvarasittichai, O. CD95 is not functional in human erythrocytes. Int. J. Lab. Hematol. 2010, 32, 244–247.
Toporkiewicz, M.; Grzybek, M.; Meissner, J.; Michalczyk, I.; Dubielecka, P.M.; Korycka, J.; Seweryn, E.; Sikorski, A.F. Release of an ~55kDa fragment containing the actin-binding domain of β-spectrin by caspase-8 during FND-induced apoptosis depends on the presence of protein 4.1. Arch. Biochem. Biophys. 2013, 535, 205–213.
Mandal, D.; Baudin-Creuza, V.; Bhattacharyya, A.; Pathak, S.; Delaunay, J.; Kundu, M.; Basu, J. Caspase 3-mediated Proteolysis of the N-terminal Cytoplasmic Domain of the Human Erythroid Anion Exchanger 1 (Band 3). J. Biol. Chem. 2003, 278, 52551–52558.
Machnicka, B.; Grochowalska, R.; Bogusławska, D.M.; Sikorski, A.F. The role of spectrin in cell adhesion and cell–cell contact. Exp. Biol. Med. 2019, 1303–1312.
Miki, Y.; Tazawa, T.; Hirano, K.; Matsushima, H.; Kumamoto, S.; Hamasaki, N.; Yamaguchi, T.; Beppu, M. Clearance of oxidized erythrocytes by macrophages: Involvement of caspases in the generation of clearance signal at band 3 glycoprotein. Biochem. Biophys. Res. Commun. 2007, 363, 57–62.
Mandal, D.; Mazumder, A.; Das, P.; Kundu, M.; Basu, J. Fas-, caspase 8-, and caspase 3-dependent signaling regulates the activity of the aminophospholipid translocase and phosphatidylserine externalization in human erythrocytes. J. Biol. Chem. 2005, 280, 39460–39467.
Mandal, S.; Mukherjee, S.; Chowdhury, K.D.; Sarkar, A.; Basu, K.; Paul, S.; Karmakar, D.; Chatterjee, M.; Biswas, T.; Sadhukhan, G.C.; et al. S-allyl cysteine in combination with clotrimazole downregulates Fas induced apoptotic events in erythrocytes of mice exposed to lead. Biochim. Biophys. Acta-Gen. Subj. 2012, 1820, 9–23.
Biswas, D.; Banerjee, M.; Sen, G.; Das, J.K.; Banerjee, A.; Sau, T.J.; Pandit, S.; Giri, A.K.; Biswas, T. Mechanism of erythrocyte death in human population exposed to arsenic through drinking water. Toxicol. Appl. Pharmacol. 2008, 230, 57–66.