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The criteria of life and aging from a molecular viewpoint. The role of protein aggregation in the process of aging

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Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Biological knowledge is expanding rapidly, delving deep into nature’s mechanisms. However, the essence of life as a molecular process still remains unclear. Organized and independently operating biological systems are commonly thought to be living. Unfortunately, these characteristics are too general and altogether insufficient to accurately delimit the boundaries of life. The problem of the relation of many primitive biological entities to the living world is still open. The properties of self-dependent biological systems clearly derive from their highly organized automatic nature. The comparative analysis of genomes of primitive biological organisms seems to be the most promising approach, which may eventually lead to the understanding of life at the molecular level and its definition. The erythrocyte appears to be of particular interest as a model of a living system that is at a boundary. Its biological origin, automatically controlled metabolism, and programmed death sharply defined in time qualify it as the living structure, even though it is completely deprived of a genetic apparatus. However, its membership among living systems seems to be well-founded. Protein aggregation is one of the common characteristics of aging. It is a consequence of abnormalities of protein structure induced by destructive actions but also by abnormalities of synthesis. Aggregation of membrane proteins probably affects the activity of certain enzymes or transport proteins, which are important as energy providers for aging erythrocytes. After the erythrocyte has passed through the vascular system a given number of times, it is not able to undergo a certain set of indispensable metabolic rearrangements. A living thing is then a form of animated nature which has the features of independence as a result of automation and possesses its own compatible with nature program of action which is time-limited beforehand.
Słowa kluczowe
Rocznik
Strony
23--30
Opis fizyczny
Bibliogr. 36 poz.
Twórcy
autor
  • Chair of Medical Biochemistry, Jagiellonian University – Collegium Medicum ul. Kopernika 7, 31-034 Krakow, Poland
autor
  • Chair of Medical Biochemistry, Jagiellonian University – Collegium Medicum ul. Kopernika 7, 31-034 Krakow, Poland
autor
  • Chair of Medical Biochemistry, Jagiellonian University – Collegium Medicum ul. Kopernika 7, 31-034 Krakow, Poland
autor
  • Chair of Medical Biochemistry, Jagiellonian University – Collegium Medicum ul. Kopernika 7, 31-034 Krakow, Poland
autor
  • Chair of Medical Biochemistry, Jagiellonian University – Collegium Medicum ul. Kopernika 7, 31-034 Krakow, Poland
autor
  • Chair of Medical Biochemistry, Jagiellonian University – Collegium Medicum ul. Kopernika 7, 31-034 Krakow, Poland
Bibliografia
  • 1. Jagers op Akkerhuis G.A.J.M. (2010), Towards a hierarchical definition of life , the organism, and death. Found Sci. 15, 245-262.
  • 2. Cleland C.E., Chyba C.F (2002), Defining ‘life’. Origins Life Evol. Biosph. 32, 387-393.
  • 3. McKay C.P. (2004), What is life – and how do we search for it in other worlds. PLoS Biol 2, 1260-1264.
  • 4. Joyce G.F. (1988), forward, in D.W. Deamer, G.R. Fleischaker (Eds.), Origins of life: the Central Concepts (Jones & Barlett, Boston), pp. xi-xii.
  • 5. Korzeniewski B. (2001), Cybernetic formulation of the definition of life. J. Theoretical Biology 209, 275-286.
  • 6. Gánti T (1986) : Podstawy życia PW “Wiedza powszechna” – Warszawa.
  • 7. Reppert S.M., Weaver D.R. (2002), Coordinating of circadian timing in mammals. Nature 418, 935-941.
  • 8. Van Gelder R.N., Herzog E.D., Schwartz W.J., Taghert P.H. (2003), Circadian rhythms: in the loop at last. Science 300, 1534-1535.
  • 9. Pasini E.M., Kirkegaard M, Mortensen P, Lutz H.U., Thomas A.W, Mann M. (2006), : In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 108, 791-801.
  • 10. Goodman S.R, Kurdia A, Ammann L, Kakhniashvili D, Daescu O. (2007), The human red blood cell proteome and interactome. Exp Biol Med 232, 1391-1408.
  • 11. Lichtman M., Beutler E., Kaushansky K., Kipps T., Seligsohn U., Prchal J. T. (2006), Williams: Hematology. 7th ed., Mc Graw-Hill New York, Chicago, San Francisco, Lisbon, London, Madrid, Mexico City, Milan, New Delhi, San Juan, Seoul, Singapore, Sydney, Toronto.
  • 12. Lang K. S., Lang P. A., Bauer C., Duranton C., Wieder T., Huber S. M., Lang F. (2005), Mechanisms of suicidal erythrocyte death. Cell Physiol Biochem 15, 195–202.
  • 13. Wallace W.J., Houtchens R.A., Maxwell J.C., Caughey W.S. (1982), Mechanism of autooxidation for hemoglobins and myoglobins. J Biol. Chem. 257: 4966-4977.
  • 14. Rifkind J.M., Nagababu E., Somasundaram R., Babu Ravi L. (2003), Hemoglobin redox reactions and oxidative stress. Redox report 8: 234-237.
  • 15. Föller M., Huber S. M., Lang F. (2008), Erythrocyte programmed cell death. IUBMB Life 60, 661–668.
  • 16. Dąbrowski Z. (red) (2000) Fizjologia krwi, wybrane zagadnienia część 2. Wydawnictwo Naukowe PWN, Warszawa.
  • 17. Asha D.S., Shiva Shankar Reddy C.S., Subramanyam M.V.V. (2009), Oxidative stress and intracellular pH in the young and old erythrocytes of rat. Biogerontology 10, 659-669.
  • 18. Cohen N.S., Ekholm J.E., Luthra M.G., Hanahan D.J. (1976), Biochemical characterization of density-separated human erythrocytes. BiochimBiophys Acta 419, 229-242.
  • 19. Beutler E. (1988), The relationship of red cell enzymes to red cell life-span. Blood Cells 14: 69-91.
  • 20. Kosower N.S. (1993), Altered properties of erythrocytes in the aged, Am J Hematol, 42, 241-247.
  • 21. Hirono A., Kanno H., Miwa S., Beutler E (2001), Pyruvate kinase deficiency and other enzymopathies of the erythrocyte. In: Scriver C.R., Beaudet A.L., Valle D., Sly W.S. et al, (eds.): The Metabolic and Molecular Bases of Inherited Disease. 8th Ed, New York: McGraw-Hill,: 4637 – 4664.
  • 22 Bosman G.J.C.G.M., Willekens F.L.A., Werre J.M. (2005), Erythrocyte aging: a more than superficial resemblance to apoptosis? Cell Physiol Biochem 16, 1-8.
  • 23. Kuypers F.A., De J. (2004): The role of phosphatidylserine in recognition and removal of erythrocytes. Cell Mol Biol 50,147-158.
  • 24. Daleke D.L. (2008), Regulation of phospholipid asymmetry in the erythrocyte membrane. Curr Opin Hematol 15, 191-195.
  • 25 Polenakovic M., Sikole A. (1996), Is erythropoietin a survival factor for red blood cells? J Am Soc Nephrol 7, 1178 – 1182.
  • 26. Greenwalt T.J. (2006), The how and why of exocytic vesicles. Transfusion 46, 143-152.
  • 27. Lingwood D., Simons K. (2010), Lipid rafts as a membraneorganizing principle. Science 327, 46–50.
  • 28 Bobrowska-Hägerstrand M, Hägerstrand H, Iglič A. (1998), Membrane skeleton and red blood cell vesiculation at low pH. Biochim. Biophys. Acta 1371, 123 – 128.
  • 29. Waugh R.E., Narla M., Jackson C.W., et al (1992), Rheologic properties of senescent erythrocytes: loss of surface area and volume with red blood cell age. Blood 79: 1351-1358.
  • 30. Suzuki T, Dale G.L. (1988), Senescent erythrocytes: isolation of in vivo aged cells and their biochemical characteristics. Proc. Natl. Acad. Sci. USA 85: 1647 – 1651.
  • 31. Kay M.M.B., Marchalonis J.J., Schluter S.F., Bosman G. (1991), Human erythrocyte aging: Cellular and molecular biology. Transfus Med Rev 5: 173-195.
  • 32. Low P.S., Kiyatkin A., Li Q., Harrison M.L. (1995), Control of erythrocyte metabolism by redox-regulated tyrosine phosphatases and kinases. Protoplasma 184, 196-202.
  • 33. Low P.S., Waugh P.S., Zinke K., Drenckhahn D. (1985), The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227, 531-533.
  • 34. Seaman C., Wyss S., Piomelli S. (1980), The decline in energetic metabolism with aging of the erythrocyte and its relationship to cell death. Am. J. Hematol 8, 31–42.
  • 35 Finkel T., Serrano M., Blanco M.A. (2007), The common biology of cancer and ageing. Nature 448, 767-774.
  • 36. Menaker M. (2003), Circadian photoreception. Science 299, 213-214.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-7cba560c-30f1-4991-8d7c-775852e5ebc9
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