Raphael Chinweike Okolo^1,2*, Silas A Ufelle¹, Peter U Achukwu¹ and Emmanuel S Ngwu²

¹Department of Medical Laboratory Sciences, Faculty of Health Sciences and Technology, University of Nigeria, Nsukka, Nigeria
²District Hospital Nsukka, Nsukka Enugu State, Nigeria

*Corresponding Author: Raphael Chinweike Okolo, Department of Medical Laboratory Sciences, Faculty of Health Sciences and Technology, University of Nigeria, Nsukka, Nigeria.

Received: November 08, 2022; Published: November 28, 2022

Abstract

The red blood cells are biconcave disc in shape, flattened and depressed in the center. The shape with its high surface area to volume (SAPV) ratio helps to accelerate diffusion of gases. The red cell membrane consists of bilayers of proteins and lipids which are rich in the glycosphingolipids that reside on the red blood cells and serve as the major determinants for the discovery of blood groups that are of major importance in blood group serology, paternity dispute and in transfusion medicine. Not only that, the membrane proteins carry the various blood group antigens, transporting ions, endothelial cells as signaling receptors and adhesive properties. This makes the red blood cells possible not to experience protein synthesis and for that no viral attack on them. The red blood cell abnormalities are being regulated by three constitutive characteristics namely, the geometry of the cell that is the cell surface to volume ratio, cytoplasm viscosity powered by intracellular haemoglobin concentration and membrane deformability. This review highlights on the importance of the red blood cell in our diagnosis and also its importance in study of red blood cell morphology to assist in the classification of numerous disease condition which can be treated with mere blood film microscopy.

Keywords: Red blood Cells; Haemoglobins; Membrane Proteins; Oxygen; Erythropoiesis

References

1. Bitesize-GSCE Biology-Revision 2. www.bbc.co.uk Reprieved 2017-11-26.
2. D’Alessandro Angelo. “Red blood cell proteomics update: is there more discovery?” Blood Transfusion2 (2017): 182-187.
3. Erich Sackman. “Biological membrane Architecture and Functions”. Hand book of Biological Physics (ed.R.Lipowsky and E.sackman. Elsevier 1 (1995).
4. Blom JA. “Monitoring Respiration and circulatory”. CRC Press (2005): 27.
5. Ruud JT. “Vertebrate without erythrocyte and blood pigments”. Nature 4410 (1954): 848-850.
6. Pierigé F., et al. “Cell-based drug delivery”. Advanced Reviews2 (2008): 286-95.
7. McLaren C E., et al. “Statistical and graphical evaluation of erythrocyte volume distribution”. American Journal of Physiology 252 (1987): H857-866.
8. Gregory TR. “The bigger the C-value; the larger the cell: genome size and red blood cell size in vertebrates”. Blood Cells, Molecules and Diseases5 (2001): 830-843.
9. Kabanova S., et al. “Gene expression analysis of human red blood cells”. International Journal of Medical Sciences4 (2009): 156-159.
10. Zimmer Carl. “Scientists explore ways to lure viruses to them” (2007).
11. Lang F., et al. “Physiology and Path Physiology of eryptosis”. Transfusion Medicine and Hemotherapy5 (2012): 308-314.
12. Swammerdam Jam (1637-1680). Mc Graw Hill Access Science (2007).
13. Max F Perutz-Biographical. Nobel Prize.org. Retrieved 23 October (2018).
14. Gorter E and Grendel F. “On the bimolecular layers of lipids on the chromocytes of the blood”. Journal of Experimental Medicine 41 (1975): 439-443.
15. Singer SJ and Nicolson GL. “The fluid mosaic model of the structure of cell membranes”. Science 175 (1972): 720-731.
16. Marchesi VT and Steers E. “Selective solubilization of a protein component of the red cell membrane”. Science 159 (1968): 203-204.
17. Steck TL., et al. “Distortion of the major proteins in the isolated erythrocyte membrane. Proteolysis dissection”. Biochemistry 10 (1971): 2617-2624.
18. Mohandas N and Gallaghar PG. “Red cell membrane: past, present, future”. Blood10 (2008): 3939-3948.
19. Rodi PM., et al. “Factors determining detergent resistance of erythrocyte membranes”. Bio Physical Chemistry 1-3 (2003): 14-18.
20. Iolascon A., et al. “Red blood cell membrane defeats”. Reviews in Clinical and Experimental Haematology1 (2003): 22-56.
21. Denomme G A. “The structure and function of the molecules that carry human red blood cell and platelet antigens”. Transfusion Medicine Reviews3 (2004): 203-231.
22. Tokamasu F., et al. “Modification in erythrocyte membrane zeta potential by plasmodium falcipanum infection”. Experimental Parasitology (2012).
23. Wan J., et al. “Dynamics of shear-induced ATP release from red blood cells”. Proceedings of the National Academy of Sciences of the United State of America43 (2008): 16432-16437.
24. Benavides Gloria A., et al. “Hydrogen - sulfide mediation the vasoactivity of garlic”. Proceedings of the National Academy of Sciences of the United States of America46 (2007): 17977-17982.
25. Kesara Shobara. “Red blood cells do more than just carry oxygen; New finding by NUS team show they aggressively attack bacteria too ‘2007”. The straits Times Retrieved (2013).
26. Jiang N., et al. “Respiratory protein-generated reactive oxygen: species as an antimicrobial strategy”. Nature Immunology10 (2007): 1114-1122.
27. Borochou H., et al. “The effect of phosphatidyl choline to sphingomyelin mole ratio on the dynamic properties of sheep erythrocytes membrane”. Biochimica et Biophysica Acta 470 (1977): 382-388.
28. Amstee DJ. “Blood group active components of the human red cell Antigens and antibodies”. ed Garrantty G, Amer. Assoc. Blood Banks, Arlington V.A. (1986): 1-15.
29. Lux SE. “Disorder of the red cell membrane skeleton: hereditary spherocytosis and hereditary elliptosis/n”. The metabolic Basis of inherited Disease ed Stanbury JB pp 1573-1605. Mc Graw-Hill. New York (1983).
30. Zwaal R F and Schroit A J. “Patholophysiologic implication of membrane phospholipids asymmetry in blood cells”. Blood 189 (1997): 1121-1132.
31. Reid M E and Mohandas N. “Red blood cell blood group antigens: structure and function”. Seminar in Haematology 41 (2004): 93-117.
32. Bennett V. “Proteins involved in membrane-cytoskeleton association in human erythrocytes, spectrin, ankyrin and band 3”. Methods of Enzymology 96 (1983): 313-324.
33. Nicholas V., et al. “Rh - RhAG/ankyrin-R - a New interaction site impaired by Rh (null)-associated mutation”. Journal of Biological Chemistry 278 (2003): 25526-25533.
34. Reid ME., et al. “Glycophorins C content of human erythrocyte membrane is regulated by protein 4.1”. Blood 72 (1990)2229-2234.
35. Marfatia S M., et al. “In vitro binding studies suggest a membrane-association complex between erythroid p55, protein 4.1, and glycophorin C”. Journal of Biological Chemistry 269 (1994): 8631-8634.
36. Mohandas N., et al. “The influence of membrane skeleton on red cell deformability, membrane material properties, and shape”. Seminar on Haematology 20 (1983): 225-242.
37. Mohandas N and Chasis JA. “Red blood cell deformability, membrane material properties and shape regulation by transmembrane, skeletal and cytosolic proteins and lipids”. Seminar on Haematology 36 (1993): 171-192.
38. Mohandas N and Evans E. “Mechanical properties of the red blood cell membrane in relation to molecular structure and genetic defects”. Annual Review of Biophysics and Biomolecular Structure 23 (1994): 787-818.
39. Discher DE. “New insights into erythrocyte membrane organization and micro elasticity”. Current Opinion in Hematology 7 (2000): 117-122.
40. Delaunay J. “The molecular basis of hereditary red cell membrane disorder”. Blood Review 21 (2007): 1-20.
41. Salzer U and Prochaska R. “Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts”. Blood 97 (2001): 1141-1143.
42. Murphy Sc., et al. “Erythrocyte detergent-resistant membrane proteins; their characterization and selective uptake during material infection”. Blood 103 (2004): 1920-1928.
43. Estes J W., et al. “A new hereditary acanthocytosis syndrome”. American Journal of Medicine 42 (1967): 868-881.
44. Mier M., et al. “Acanthocytosis, pigmented degeneration of the retina and ataxic neuropathy: a genetically determined syndrome with associated metabolic disorder”. Blood 16 (1960): 1586-1608.
45. Salt H B., et al. “On having no beta-lipoprotein: a syndrome comparing a beta- lipoproteinaemia, acanthocytosis and steartorrhoea”. Lancet ii (1960): 325-329.
46. Wimer B M., et al. “Haematological changes associated with the Mcleod phenotype of the Kell blood group system”. British Journal of Haematology 36 (1977): 219-224.
47. Silber R., et al. “Spur-shaped erythrocytes in Laennec’s cirrhosis”. New England Journal of Medicine 275 (1966): 639-643.

Citation

Citation: Raphael Chinweike Okolo., et al. “The Red Blood Cell Not Only for Colour Identity but with Complex Material Properties”.Acta Scientific Medical Sciences 6.12 (2022): 121-126.

Copyright

Copyright: © 2022 Raphael Chinweike Okolo., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.