Erythrocytes shape

SEM is a more informative method of studying erythrocyte form. It allows examining changes in the erythrocyte shape and the surface microrelief [4-8]. 

In the majority of patients with sickle cell disease, anemia is not the major problem the anemia is generally well compensated even though such individuals have a chronically low hematocrit (20-30%), a low serum hemoglobin level (7-10 g/dL), and an elevated reticulocyte count. Instead, the primary problem is that deoxygenated HbS chains form polymeric structures that dramatically change erythrocyte shape, reduce deformability, and elicit membrane permeability changes that further promote hemoglobin polymerization. Abnormal erythrocytes... 

HEMOGLOBIN OXYGEN BINDING, ERYTHROCYTE SHAPE TRANSFORMATIONS, AND MODELING OF CELL DIFFERENTIATION AS EXAMPLES OF THEORETICAL APPROACHES IN STUDYING THE STRUCTURE-FUNCTION RELATIONSHIP IN BIOLOGICAL SYSTEMS... 

Glaser, R. Gengnagel, C. Donath, J. The influence of valinomycin induced membrane potential on erythrocyte shape. Biomed. Biochim. Acta 1991, 50, 869-877. 

Figure 8.4 The relationship between lipid composition and erythrocyte shape. Reproduced with kind permission of Professor LLM. van Deenen and Elsevier Trends Journals, from Trends in Biochemical Sciences (1985), p. 322, Figure 3.

The processes of electron transport and oxidative phosphorylation are membrane-associated. Bacteria are the simplest life form, and bacterial cells typically consist of a single cellular compartment surrounded by a plasma membrane and a more rigid cell wall. In such a system, the conversion of energy from NADH and [FADHg] to the energy of ATP via electron transport and oxidative phosphorylation is carried out at (and across) the plasma membrane. In eukaryotic cells, electron transport and oxidative phosphorylation are localized in mitochondria, which are also the sites of TCA cycle activity and (as we shall see in Chapter 24) fatty acid oxidation. Mammalian cells contain from 800 to 2500 mitochondria other types of cells may have as few as one or two or as many as half a million mitochondria. Human erythrocytes, whose purpose is simply to transport oxygen to tissues, contain no mitochondria at all. The typical mitochondrion is about 0.5 0.3 microns in diameter and from 0.5 micron to several microns long its overall shape is sensitive to metabolic conditions in the cell. 

Microtubules are universally present in eukaryotes from protozoa to the cells of higher animals and plants (Porter, 1966 Hardham and Gunning, 1978 Lloyd, 1987), but they are absent in mammalian erythrocytes and in prokaryotes. Microtubules participate in a number of cellular functions including the maintenance of cell shape and polarity, mitosis, cytokinesis, the positioning of organelles, intracellular transport to specific domains, axoplasmic transport, and cell locomotion. The diversity of microtubule fimctions suggests that not all microtubules are identical and that different classes of microtubules are present in different cell types or are localized in distinct domains in the same cell type (Ginzburg et al., 1989). 

Submembranous microtubules are often present in parallel bundles beneath the plasma membrane in the cells of higher plants, particularly during cell wall formation (Hardham and Gimning, 1978). Circular submembranous bundles of microtubules are a feature of bird erythrocytes and mammalian blood platelets, where they maintain the discoid shape of these structures (Dustin, 1980). 

In sickle cell hemoglobin (HbS), Val replaces the P6 Glu of HbA, creating a sticky patch that has a complement on deoxyHb (but not on oxyHb). De-oxyHbS polymerizes at low O2 concentrations, forming fibers that distort erythrocytes into sickle shapes. 

ERYTHROCYTES. Erythrocytes are biconcave diskshaped, blood cells (with pits or depressions in the center on both sides), the primary function of which is to transport hemoglobin, the oxygen-carrying protein. The biconcave shape of the erythrocyte provides a large surface volume ratio and thereby facilitates exchange of oxygen. The average diameter of erythrocytes is 7.5 pm, and thickness at the rim is 2.6 pm and in the center about 0.8 pm. The normal concentration of erythrocytes in blood is approximately 3.9-5.5 million cells per pL in women and 4.1-6 million cells per pL in men. The total life span of erythrocytes in blood is 120 days. 

In erythrocytes and most other cells, the major structural link of plasma membranes to the cytoskeleton is mediated by interactions between ankyrin and various integral membrane proteins, including Cf/HCOj antiporters, sodium ion pumps and voltage-dependent sodium ion channels. Ankyrin also binds to the =100 nm, rod-shaped, antiparallel a(3 heterodimers of spectrin and thus secures the cytoskeleton to the plasma membrane. Spectrin dimers self-associate to form tetramers and further to form a polygonal network parallel to the plasma membrane (Fig. 2-9D). Neurons contain both spectrin I, also termed erythroid spectrin, and spectrin II, also termed fodrin. Spectrin II is found throughout neurons, including axons, and binds to microtubules, whereas spectrin I occurs only in the soma and dendrites. 

Seigneuret, M. and Deveaux, P.F., 1984, ATP-dependent asymmetric distribution ofspin-labeUed phosphohpids in the erythrocyte membrane relation to shape changes. Proc. Natl. Acad. Scl, U.S.A., 81 3751-3755. 

Another group of non-histone proteins have been identified as essential components for the formation of the condensed chromosome (Table 1). Topoisomerase II (topo II) localizes in the scaffold/matrix fraction of the interphase nuclear (Berrios et al., 1985) and the mitotic chromosome (Maeshima and Laemmli, 2003) (see section 3.1). Topo II forms a ring-shaped homodimer (Berger et al, 1996 Nettikadan et al, 1998) and catalyzes the decatenation and relaxation of DNA double strand (Wang, 2002). In fission yeast, chromosomes cannot be condensed without functional topo II (Uemura et al, 1987). In addition, in in vitro experiment, mitotic extracts containing topo II induce chromatin condensation in the isolated nuclei from HeLa and chicken erythrocyte cells (Adachi et al., 1991). 

The prototype of a small pore-forming toxin is the S. aureus a-toxin, also called ct-hemolysin, that has been extensively investigated hy Bhakdi and coworkers. Monomers of ct-hemolysin (33 kDa) hind to the surface of erythrocytes, and after lateral diffusion within the lipid hilayer, seven monomers oligomerize to form pores in the cell membrane. The ct-hemolysin forms mushroom-shaped pores with an outer diameter of lOnm and an inner diameter of approximately 2.5 nm. Small molecules can pass through the pore and diffuse into/out of the cytosol, along with water. As a consequence of such movement, cell homeostasis is greatly disturbed and pushed into an unhealthy state. In animals, the a-hemolysin represents a major virulence factor of S. aureus which causes hemolysis as well as tissue destruction. ... 

The red blood cell has no mitochondria and is totally dependent on anaerobic glycolysis for ATP. In pyruvate kinase deficiency, the decrease in ATP causes the erythrocyte to lose its characteristic biconcave shape and signals its destruction in the spleen. In addition, decreased ion pumping by Na /K -ATPase results in loss of ion balance and causes osmotic fragility, leading to swelling and lysis. 

The sickled shape of erythrocytes in patients with sickle cell anemia occurs because of the tendency for HbS to polymerize. HbS differs from HbA by substitution of a solvent-exposed glutamate by valine in 3-globin, which forms a sticky patch that promotes abrogation and polymerization of the protein. 

The human red blood cell (erythrocyte) has a shape of biconcave disc with minimal (D ) and maximal (D ) thickness and radius R (Fig. 10.1a). The optical scheme of a reflected microscope with deposited red blood cells is shown in Fig. 10. lb. The light scattering process takes place at the interface of three media air-erythrocyte-substrate with refractive index n, n and n respectively. Since the erythrocyte thickness is of the same order of magnitude as the wavelength of incidental light, the interference phenomena take place on these blood cells. The reflective capacity of an interface between two media with refractive indices n, and n is described by Eq. 10.1 [10] ... 

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