eISSN: 2221-6197 DOI: 10.31301/2221-6197

The multiplicity of hemoglobin functional forms in human organism: the modern view and practical applications

Year: 2018

Pages: 251-267

Number: Volume 10, issue 3

Type: scientific article

Summary:

The main functional forms of erythrocytic hemoglobin found in human organism are considered. Among them are oxidized hemoglobin, and forms appearing under the action of reactive compounds at oxidative, nitrosative and carbonyl stress conditions. The special attention is paid to hemoglobin forms, which are still little used in medical practice (e.g., membrane-bound one). The necessity and possibility of their use in diagnostics is explaining, i.e. in computer diagnostic systems.

 

Keywords:

hemoglobin, multiply forms, reactive oxygen and nitrogen species, glycosylation, methemoglobin, membrane-bound hemoglobin

References:

1. Andreyuk G.M., Kisel' M.A. The formation of hemichrome upon interaction of hemoglobin with polar phosphatidylcholine derivatives. Russian Journal of Bioorganic Chemistry. 1997. V. 23(4). P. 268-271.

  1. Galenok V.A., Bodnar P.N., Dikker V.E., Romashkan S.V. Glikozilirovannye proteiny. Novosibirsk: Nauka. Sib. otdelenie. 1989. 258 p. [Glycosylated proteins]. (In Russian)
  2. Grigorieva D.V., Gorudko I.V., Sokolov A.V., Kosmachevskaya O.V., Topunov A.F., Buko I.V., Konstantinova E.E., Cherenkevich S.N., Panasenko O.N. Measurement of Plasma Hemoglobin Peroxidase Activity. Bulletin of Experimental Biology and Medicine. 2013. V. 155(1). P. 118-121. DOI: 10.1007/s10517-013-2094-4
  3. Gromov P.S., Zakharov S.F., Shishkin S.S., Ilinskii R.V. Two-dimensional map of human-erythrocyte membrane-proteins. Biochemistry (Moscow). 1988. V. 53(8). P. 1146-1155.
  4. Kosmachevskaya O.V., Topunov A.F. Method of determination of the content of hemoglobin-like proteins in heterogenic mixtures. Applied Biochemistry and Microbiology. 2007. V.43(3). P.313-319. DOI: 10.1134/S0003683807030131
  5. Kosmachevskaya O.V., Topunov A.F. Hemoglobins: Diversity of structures and functions. Applied Biochemistry and Microbiology. 2009. V. 45(6). P. 563-587. DOI: 10.1134/S0003683809060015
  6. Kosmachevskaya O.V., Shumaev K.B., Topunov A.F. Signal and regulatory effects of methylglyoxal in eukaryotic cells. Applied Biochemistry and Microbiology. 2017. V. 53(3). P. 273–289. DOI: 10.1134/S0003683817030103
  7. Luneva O.G., Sidorenko S.V., Maksimov G.V., Grygorczyk R., Orlov S.N. Erythrocytes as regulators of blood vessel tone. Biochemistry, Supplemental Series A. 2015. V. 9(3). P. 161-171. DOI: 10.1134/S1990747815040078
  8. Nasledstvennye anemii i gemoglobinopatii. (Red.: Tokarev Ju.N., Hollan S.R., Korralja-Al'monte H.S.) M.: Medicina. 1983. 336 p. [Hereditary anemies and hemoglobinopathies. (Eds.: Tokarev Ju.N., Hollan S.R., Korralja-Al'monte H.S.)]. (In Russian)
  9. Nasybullina E.I., Nikitaev V.G., Pronichev A.N., Blindar V.N., Kosmachevskaya O.V., Topunov A.F. Expert diagnostic system for hemoglobinopathies using the data on blood, erythrocyte, and hemoglobin state. Bulletin of the Lebedev Physics Institute. 2015. V. 42(7). P. 206-208. DOI: 10.3103/S1068335615070039
  10. Toktamyssova Z.S., Birshanova N.H. O membranosvjazannom gemoglobine. Biofizika. 1990. V. 35(6). P. 1019-1020. [On the membrane-bound hemoglobin]. (In Russian)
  11. Topunov A.F., Golubeva L.I. Reduktazy, vosstanavlivajushhie kislorodperenosjashhie gemoproteidy: gemoglobin, mioglobin i legoglobin. [Reductases reducing oxygen-carrying hemoproteins: hemoglobin, myoglobin and leghemoglobin]. Uspehi biologicheskoj himii. [Advances in Biological Chemistry]. 1989. V. 30. P. 239-252. (In Russian)
  12. Topunov A.F., Kosmachevskaya O.V. Fermentativnoe vosstanovlenie gemoglobina i metgemoglobinemija. [Enzymatic reduction of hemoglobin and methemoglobinemia]. Materialy Suhumskoj mezhdunarodnoj nauchno-prakticheskoj konferencii: Aktual'nye voprosy jeksperimental'noj biologii i mediciny [Proceedings of the Sukhum International scientific-practical conference: Actual issues of experimental biology and medicine]. Sukhum, 2017. P. 413-421. (In Russian)
  13. Topunov A.F., Kosmachevskaya O.V., Shumaev K.B. GemoglobinÓm – nabor vseh gemoglobinov organizma. [Hemoglobinome – the enlistment of all organism’s hemoglobins]. Trudy XXI mezhdunarodnoj konferencii «Novye informacionnye tehnologii v medicine, biologii, farmakologii i jekologii». Ukraina, Krym, Jalta-Gurzuf, 2013. [Proceedings of 21th International conference: New information technologies in medicine, biology, pharmacology and ecology. Ukraine, Crimea, Yalta-Gurzuf, 2013]. P. 150-152. (In Russian)
  14. Topunov A.F., Petrova N.E. Gemoglobiny: jevoljucija, rasprostranenie i geterogennost'. [Hemoglobins: evolution, widespreading and heterogeneity]. Uspehi biologicheskoj himii. [Advances in Biological Chemistry]. 2001. V. 41. P. 199-228. (In Russian)
  15. Shumaev K.B., Gubkin A.A., Gubkina S.A., Gudkov L.L., Sviryaeva I.V., Timoshin A.A., Topunov A.F., Vanin A.F., Ruuge E.K. The interaction between dinitrosyl iron complexes and intermediates of oxidative stress. Biophysics. 2006. V.51(3). P.423-428. DOI: 10.1134/S0006350906030134
  16. Shumaev K. B., Sviryaeva I. V., Gubkina S. A., Krivova T. S., Topunov A. F., Vanin A. F., Ruuge E. K. Formation of dinitrosyl iron complexes in cardiac mitochondria. Biophysics. 2010. V. 55(3). P. 406-411. DOI: 10.1134/S0006350910030097
  17. Alayash A.I., Ryan B.A., Cashon R.E. Peroxynitrite-mediated heme oxidation and protein modification of native and chemically modified hemoglobins. Arch. Biochem. Biophys. 1998. V. 349(1). P. 65-73. DOI: 10.1006/abbi.1997.0449
  18. Anderson H.M., Turner J.C. Relation of hemoglobin to the red cell membrane. J. Clin. Invest. 1960. V. 39(1). P. 1-7. DOI: 10.1172/JCI104007
  19. Angelo M., Singel D., Stamler J. An S-nitrosothiol (SNO) synthase function of hemoglobin that utilizes nitrite as a substrate. Proc. Natl. Acad. Sci. USA. 2006. V. 103(22). P. 8366-8371. DOI: 10.1073/pnas.0600942103
  20. Ascenzi P., Brunori M. Myoglobin: a pseudo-enzymatic scavenger of nitric oxide. Biochemistry and Molecular Biology Education. 2001. V. 29(5). P. 183-185. DOI: 10.1016/S1470-8175(01)00082-0
  21. Benesch B.R., Benesch R.E. Preparation and properties of hemoglobin modified with derivatives of pyridoxal. Methods in Enzymology. 1981. V. 76. P. 147-159. DOI: 10.1016/0076-6879(81)76123-8
  22. Chandalia H.B., Krishnaswamy P.R. Glycated hemoglobin. Current Science. 2002. V. 83(12). P. 1522-1532.
  23. Demehin A.A., Abugo O.O., Jayakumar J.R., Rifkind J.M. Binding of hemoglobin to red cell membranes with eosin-5-maleimide-Labeled Band 3: analysis of centrifugation and fluorescence data. Biochemistry. 2002. V. 41(27). P. 8630-8637. DOI: 10.1021/bi012007e
  24. Discombe G. Sulfhaemoglobinaemia and glutathione. Lancet. 1960. V. 276(7146). P. 371-372. DOI: 10.1016/S0140-6736(60)91518-X
  25. Dolhofer R., Renner R., Wieland O.H. Different behaviour of haemoglobin A1a−c and glycosylalbumin levels during recovery from diabetic ketoacidosis and non-acidotic coma. Diabetologia. 1981. V. 21(3). P. 211-215.
  26. Eich R.F., Li T., Lemon D.D., Doherty D.H., Curry S.R., Aitken J.F., Mathews A.J., Johnson K.A., Smith R.D., Phillips G.N., Olson J.S. Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry. 1996. V. 35(22). P. 6976-6983. DOI: 10.1021/bi960442g
  27. Eisinger J., Flores J., Salhany J.M. Association of cytosol hemoglobin with the membrane in intact erythrocytes. Proc. Natl. Acad. Sci. USA. 1982. V. 79(2). P. 408-412. DOI: 10.1073/pnas.79.2.408
  28. Fluckiger R., Berger W., Winterhalter K.H. Haemoglobin A1c, a reliable index of diabetic control. Diabetologia. 1977. V. 13. P. 393-396.
  29. Fung L.W. Spin-label detection of hemoglobin-membrane interaction at physiological pH. Biochemistry. 1981. V. 20(25). P. 7162-7166. DOI: 10.1021/bi00528a017
  30. Gardner P.R., Gardner A.M., Martin L.A., Salzman A.L. Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proc. Natl. Acad. Sci. USA. 1998. V. 95(18). P. 10378-10383.
  31. Gladwin M.T., Raat N.J., Shiva S., Dezfulian C., Hogg N., Kim-Shapiro D.B., Patel R.P. Nitrite as a vascular endocrine nitric oxide reservoir that contributes to hypoxic signaling, cytoprotection, and vasodilation. Am. J. Physiol. Heart Circ. Physiol. 2006. V. 291(5). P. H2026–H2035. DOI: 10.1152/ajpheart.00407.2006
  32. Gow A.J., Luchsinger B.P., Pawloski J.R., Singel D.J., Stamler J.S. The oxyhemoglobin reaction of nitric oxide. Proc. Natl. Acad. Sci. USA. 1999. V. 96(16). P. 9027-9032. DOI: 10.1073/pnas.96.16.9027
  33. Hausladen A., Gow A., Stamler J.S. Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen. Proc. Natl. Acad. Sci. USA. 2001. V. 98(18). P. 10108-10112. DOI: 10.1073/pnas.181199698
  34. Herold S., Kalinga S., Matsui T., Watanabe Y. Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants. J. Am. Chem. Soc. 2004. V. 126(22). P. 6945-6955. DOI: 10.1021/ja0493300
  35. Huang Z., Shiva S., Kim-Shapiro D.B., Patel R.P., Ringwood L.A., Irby C.E., Huang K.T., Ho C., Hogg N., Schechter A.N., Gladwin M.T. Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control. J. Clin. Invest. 2005. V. 115(8). P. 2099–2107. DOI: 10.1172/JCI24650
  36. Ingram V. A specific chemical difference between globins of normal and sickle-cell anemia hemoglobins. Nature. 1956. V. 178(4537). P. 792-794. DOI: 10.1038/178792a0
  37. Jia L., Bonaventura C, Bonaventura J, Stamler JS. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature. 1996. V. 380(6571). P. 221–226. DOI: 10.1038/380221a0
  38. Kosmachevskaya O.V., Shumaev К.B., Nasybullina E.I., Gubkina S.А., Topunov А.F. Interaction of S-nitrosoglutathione with methemoglobin under conditions of modeling carbonyl stress. Hemoglobin. 2013. V. 37(3). P. 205-218. DOI: 10.3109/03630269.2013.773911
  39. Kosmachevskaya O.V., Shumaev К.B., Nasybullina E.I., Topunov A.F. Formation of nitri- and nitrosylhemoglobin in systems modeling the Maillard reaction. Clin. Chem. Lab. Med. 2014. V.52(1). P. 161-168. DOI: 10.1515/cclm-2012-0792
  40. Kreutzer U., Jue T. The role of myoglobin as a scavenger of cellular NO in myocardium. J. Physiol. Heart Circ. Physiol. 2004. V. 286(3). P. H985-H991. DOI: 10.1152/ajpheart.00115.2003
  41. Kriebardis A.G., Antonelou M.H., Stamoulis K.E., Economou-Petersen E., Margaritis L.H., Papassideri I.S. Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells. J. Cell. Mol. Med. 2007. V. 11(1). P. 148-155. DOI: 10.1111/j.1582-4934.2007.00008.x
  42. Kuma F., Prough R.A., Masters B.S.S. Studies on methemoglobin reductase. Immunochemical similarity of soluble methemoglobin reductase and cytochrome b5 of human erythrocytes with NADH-cytochrome b5 reductase and cytochrome b5 of rat liver microsomes. Arch. Biochem. Biophys. 1976. V. 172(2). P. 600-607. DOI: 10.1016/0003-9861(76)90113-2
  43. Kunkel H.G., Wallenius G. New hemoglobins in normal adult blood. Science. 1955. V. 122(3163). P. 288. DOI: 10.1126/science.122.3163.288
  44. Li D-J., Luo H., Wang L.-L., Zou G.-L. Potential of peroxynitrite to promote the conversion of oxyhemoglobin to methemoglobin. Acta Biochimica Biophysica Sinica. 2004. V. 36(2). P. 87-92.
  45. Lisitsa A., Moshkovskii S., Chernobrovkin A., Ponomarenko E., Archakov A. Profiling proteoforms: Promising follow-up of proteomics for biomarker discovery. Expert Review of Proteomics. 2014. V. 11(1). P.121-129. DOI: 10.1586/14789450.2014.878652
  46. Mansouri A. Methemoglobinemia. American Journal of Medical Sciences. 1985. V. 289(5). P. 200-209.
  47. McCutcheon A.D., Melb M.D., Flack E.H. Sulphaemoglobinaemia and glutathione. Lancet. 1960. V. 276(7144). P. 240-242. DOI: 10.1016/S0140-6736(60)91429-X
  48. Murayama M. The combining power of normal human hemoglobin for nitrosobenzene. J. Biol. Chem. 1960. V. 235(4). P. 1024-1028.
  49. Murphy K., Ryan C., Dempsey E.M., O’Toole P.W., Ross R.P., Stanton C., Ryan C.A. Neonatal sulfhemoglobinemia and hemolytic anemia associated with intestinal Morganella morganii. Pediatrics. 2015. V. 136(6). P. e1641-e1645. DOI: 10.1542/peds.2015-0996
  50. Nash G.B., Meiselman H.J. Red cell and ghost viscoelasticity. Effects of hemoglobin concentration and in vivo aging. Biophys. J. 1983. V. 43(1). P. 63–73. DOI: 10.1016/S0006-3495(83)84324-0
  51. Qiu Y., Sutton L., Riggs A.F. Identification of myoglobin in human smooth muscle. J. Biol. Chem. 1998. V. 273(36). P. 23426-23432. DOI: 10.1074/jbc.273.36.23426
  52. Park C.M., Nagel R.L. Sulfhemoglobinemia. Clinical and molecular aspects. N. Engl. J. Med. 1984. V. 310(24). P. 1579–1584. DOI: 10.1056/NEJM198406143102407
  53. Perutz M.F., Liquori A.M., Eirich F. X-ray and solubility studies of the haemoglobin of sickle-cell anaemia patients. Nature. 1951. V. 167(4258). P. 929-931.
  54. Rahbar S. An abnormal hemoglobin in red cells of diabetics. Clin. Chim. Acta. 1968. V. 22(2). P. 296–298. DOI: 10.1016/0009-8981(68)90372-0
  55. Ramdani G., Langsley G. ATP, an extracellular signaling molecule in red blood cells: a messenger for malaria? Biomed. J. 2014. V. 37(5). P. 284-292. DOI: 10.4103/2319-4170.132910
  56. Rassaf T., Flogel U., Drexhage C., Hendgen-Cotta U., Kelm M., Schrader J. Nitrite reductase function of deoxymyoglobin: oxygen sensor and regulator of cardiac energetics and function. Circ. Res. 2007. V. 100(12). P. 1749-1754. DOI: 10.1161/CIRCRESAHA.107.152488
  57. Reeder B., Wilson M. Hemoglobin and myoglobin associated oxidative stress: From molecular mechanisms to disease states. Curr. Med. Chem. 2005. V. 12(23). P. 2741-2751. DOI: 10.2174/092986705774463021
  58. Rifkind J.M., Nagababu E. Hemoglobin redox reactions and red blood cell aging. Antioxid. Redox Signal. 2013. V. 18(17). P. 2274-2283. DOI: 10.1089/ars.2012.4867
  59. Rifkind J., Nagababu E., Ramasamy S. Nitric oxide redox reactions and red cell biology. Antioxid. Redox Signal. 2006. V. 8(7-8). P. 1193-1203. DOI: 10.1089/ars.2006.8.1193
  60. Riggs A. Preparation of blood hemoglobins of vertebrates. Methods in Enzymology. 1981. V. 76. P. 5-29. DOI: 10.1016/0076-6879(81)76111-1
  61. Salhany J.M. Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of Band 3 (SLC4A1). Biochemistry. 2008. V. 47. P. 6059-6072. DOI: 10.1021/bi8000819
  62. Sears D.A., Lewis P.C. Measurement of hemoglobin chains bound to the erythrocyte membrane. J. Lab. Clin. Med. 1980. V. 96(2). P. 318-327.
  63. Shapiro R., Mc Manus M.J., Zalut C., Bunn H.F. Sites of nonenzymatic glycosylation of human hemoglobin A. J. Brit. Chem. 1980. V. 255(7). P. 3120-3127.
  64. Shiva S. Nitrite: A physiological store of nitric oxide and modulator of mitochondrial function. Redox Biology. 2013. V. 1(1). P. 40–44. DOI: 10.1016/j.redox.2012.11.005
  65. Scheler W. Binding of nitrosobenzene and nitrosobenzene derivatives to hemoglobin and hemoglobin compounds. Acta Biol. Med. Germ. 1960. V. 5. P. 382-397.
  66. Scott E.M., Griffith I.V. The enzymatic defect of hereditary methemoglobinemia: diaphorase. Biochim. Biophys. Acta. 1959. V. 34. P. 584-586. DOI: 10.1016/0006-3002(59)90324-5
  67. Sega M.F., Chu H., Christian J., Low P.S. Interaction of deoxyhemoglobin with the cytoplasmic domain of murine erythrocyte band 3. Biochemistry. 2012. V. 51(15). P. 3264-3272. DOI: 10.1021/bi201623v
  68. Shaklai N., Yguerabide J., Ranney H.M. Classification and localization of hemoglobin binding sites on the red blood cell membrane. Biochemistry. 1977. V. 16(25). P. 5593-5597. DOI: 10.1021/bi00644a032
  69. Shaklai N., Sharma V.S., Ranney H.M. Interaction of sickle cell hemoglobin with erythrocyte membranes. Proc .Natl. Acad. Sci. USA. 1981. V. 78(1). P. 65-68. DOI: 10.1073/pnas.78.1.65
  70. Shaklai N., Ranney H.R. Interaction of hemoglobin with membrane lipids: a source of pathological phenomena. Isr. J. Med. Sci. 1978. V. 14(11). P. 1152-1156.
  71. Shumaev К.B., Gubkin А.А., Serezhenkov V.А., Lobysheva I.I., Kosmachevskaya O.V., Ruuge E.К., Lankin V.Z., Topunov А.F., Vanin А.F. Interaction of reactive oxygen and nitrogen species with albumin- and hemoglobin-bound dinitrosyl iron complexes. Nitric Oxide. 2008a. V. 18(1). P. 37-46. DOI: 10.1016/j.niox.2007.09.085
  72. Shumaev K.B., Kosmachevskaya O.V., Timoshin A.A., Vanin A.F., Topunov A.F. Dinitrosyl iron complexes bound with haemoglobin as markers of oxidative stress. Methods in Enzymology. 2008b. V. 436. P. 441-457. DOI: 10.1016/S0076-6879(08)36025-X
  73. Sprague R.S., Ellsworth M.L., Stephenson A.H., Lonigro A.J. Participation of cAMP in a signal-transduction pathway relating erythrocyte deformation to ATP release. Am. J. Physiol. Cell. Physiol. 2001. V. 281(4). P. C1158-C1164. DOI: 10.1152/ajpcell.2001.281.4.C1158
  74. Stamler J.S., Jia L., Eu J.P., McMahon T.J., Demchenko I.T., Bonaventura J., Gernert K., Piantadosi C.A. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science. 1997. V. 276(5321). P. 2034-2037. DOI: 10.1126/science.276.5321.2034
  75. Stamler J.S., Singel D.J., Piantadosi C.A. SNO-hemoglobin and hypoxic vasodilation. Nature Medicine. 2008. V. 14(10). P. 1008-1009. DOI: 10.1038/nm1008-1008
  76. Talbot B., Brunori M., Antonini E., Wyman J. Studies on the reaction of isocyanides with haemproteins. I. Equilibria and kinetics of the binding to the isolated chains of human haemoglobin. J. Mol. Biol. 1971. V. 58(1). P. 261-276. DOI: 10.1016/0022-2836(71)90245-2
  77. Tsuneshige A., Imai K., Tyuma I. The binding of hemoglobin to red cell membrane lowers its oxygen affinity. J. Biochem. 1987. V. 101(3). P. 695-704.
  78. Vanin A.F., Serezhenkov V.A., Mikoyan V.D., Genkin M.V. The 2.03 signal as an indicator of dinitrosyl iron complexes with thiol-containing ligands. Nitric Oxide. 1998. V. 2(4). P. 224-234. DOI: 10.1006/niox.1998.0180
  79. Yim H.-S., Kang S.-O., Hah Y-C., Chock P.B., Yim M.B. Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals. J. Biol. Chem. 1995. V. 270(47). P. 28228-28233. DOI: 10.1074/jbc.270.47.28228
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eISSN: 2221-6197 DOI: 10.31301/2221-6197