Function Of Haemoglobin In Red Blood Cells

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Function Of Haemoglobin In Red Blood Cells

Function Of Haemoglobin In Red Blood Cells

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The Immunological Functions Of Red Blood Cells

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What Is A Healthy Hemoglobin Level?

By Olga V. Kosmachevskaya Olga V. Kosmachevskaya Scilit Google Scholar 1 , Natalia N. Novikova Natalia N. Novikova Scilit Google Scholar 2 and Alexey F. Topunov Alexey F. Topunov Scilit Google Scholar 1, *

Received: December 10, 2020 / Revised: February 2, 2021 / Accepted: February 3, 2021 / Published: February 7, 2021

The thesis discusses the peculiarities of carbonyl stress in anucleated mammalian red blood cells (RBC). Some functional properties of red blood cells make them exceptionally sensitive to reactive carbonyl compounds (RCC) from both the plasma and the intracellular environment. In the first case, these chemical compounds arise due to an increased concentration of glucose or ketones in the plasma, and in the second – due to an imbalance in blood sugar control. RBCs are normally exposed to RCCs—methylglyoxal (MG), triglycerides—in the plasma of diabetic patients. MG modifies lipoproteins and membrane proteins of red blood cells and endothelial cells both alone and with reactive oxygen species (ROS). Together, these phenomena can lead to arterial hypertension, atherosclerosis, hemolytic anemia, vascular occlusion, local ischemia, and the development of a hypercoagulable phenotype. ROS, reactive nitrogen species (RNS), and RCC could also damage hemoglobin (Hb), the most abundant protein in the RBC cytoplasm. It was Hb whose nonenzymatic glycation was first demonstrated in living systems under physiological conditions. Glycated HbA1c is used as a very reliable and useful diagnostic marker. Investigating the effects of MG, ROS, and RNS on the physiological state of RBCs and Hb is undeniably important for basic and applied science.

Function Of Haemoglobin In Red Blood Cells

The term “stress” can be seen as both an external effect on an organism and a reaction to it. At the same time, it is known that stress is a universal physiological response to sufficiently strong influences, characterized by certain symptoms and stages (“general adaptation syndrome” according to Hans Selye) [1]. Furthermore, the term “stress” began to be used in biology and chemistry to describe the effects of certain compounds (or groups of compounds), usually chemically reactive, i.e. electrophiles and oxidants.

What Would Be The Consequences Of Deficiency Of Hemoglobin?

Currently, metabolism is defined as a network of enzymatic and non-enzymatic (autonomous) chemical reactions. An integral part of non-enzymatic metabolism is the synthesis and redox transformations of chemically reactive compounds. An excess of these substances leads to the development of a certain type of metabolic stress: oxidative stress, induced by reactive oxygen species (ROS), nitrosative – by reactive nitrogen species (RNS), carbonyl – by reactive carbonyl compounds (or reactive carbonyl). species) (RCC), and halogenating – with reactive halogen species, etc.

The main RCCs are linear (non-cyclic) forms of glucose and fructose, together with various aldehydes, ketones, ketoaldehydes and ketoacids, eg glyoxal, methylglyoxal (MG), acrolein, malondialdehyde, 3-deoxyglucosone, lipid oxidizers, etc. Every RCC contains an electrophilic carbon atom from a carbonyl group that can react with nucleophilic nitrogen atoms in amino acids, aminopeptides and guanine bases (non-enzymatic glycation reaction).

Living organisms have developed various ways to prevent non-enzymatic glycation. The most effective of these is the glyoxalase system [2, 3]. However, when the glycemic defense system cannot cope with excess RCC, a state of carbonyl stress develops. The concept of carbonyl stress was supported by Baynes in 1991 [4] based on several lines similar to the concept of oxidative stress recognized in biology as early as 1985 [5]. All eukaryotic cells are sensitive to carbonyl stress to some extent, including the anucleated red blood cells (RBCs) which appear to be one of the most sensitive sensors of chemically active compounds in many organisms.

In the review, we tried to generalize the data on carbonyl stress in erythrocytes, focusing on the metabolism of MG, which, together with glucose, is largely responsible for the negative consequences of diabetic hypoglycemia. We paid special attention to the relationship between carbonyl stress and oxidative and nitrosative stress and the effect of these processes on Hb.

Solution: Full Hb

There are two main ways in which carbonyl stress can develop in red blood cells: exogenous and endogenous (Figure 1). The first pathway is induced by increased concentrations of glucose or ketone bodies in blood plasma. The second is triggered by an imbalance in blood sugar control in the red blood cells themselves. Some factors contribute slightly to the development of carbonyl stress here. These include infection with malarial plasmodium, glycolytic enzymopathy, and mutations in the glucose transporter (GLUT1).

Levels of triglycerides, MG, and ROS were shown to increase in the plasma of type 1 and type 2 diabetic patients [ 3 , 6 , 7 ]. Experiments on isolated erythrocytes showed that intracellular MG concentration is directly dependent on the flow of glucose metabolized in the glycolytic pathway [2]. In the range of 5-100 mM glucose concentration, a dose-dependent increase in S-D-lactogluthione and MG concentrations was recorded [2]. Plasma MG can have several toxic effects: it modifies proteins and lipoproteins, generates ROS, and acts on RBCs and endothelial cells. These together with MG effects facilitate the development of arterial hypertension, atherosclerosis, hemolytic anemia, vascular occlusion, and local ischemia [ 8 , 9 ].

RBC metabolism is defined by the major role of glucose metabolism, where all the necessary energy received by the cell is obtained through glycolytic reactions and the pentose phosphate pathway. Intermediates of glucose breakdown (glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP)) represent the main sources of MG [ 10 , 11 ].

Function Of Haemoglobin In Red Blood Cells

Glucose for glycolysis is delivered to RBCs in an insulin-independent manner using light diffusion via the glucose transporter GLUT1. Thus, the concentration of glucose inside red blood cells is directly related to its concentration in plasma. Therefore, erythrocytes are among the first cells to detect hyperglycemia. At high glucose concentrations, oxygen binds to iron ions inside red blood cells, leading to the formation of RCC. Although RBCs contain powerful antioxidants and glyoxalase defense mechanisms [ 3 ], there is a high probability that carbonyl and oxidative stress development reinforce each other [ 12 , 13 ]. The main trigger of oxidative and carbonyl stress is that antioxidants and key glycolytic enzymes are damaged by ROS and RCC [ 14 ]. For example, nonenzymatic glycation of superoxide dismutase leads to enzyme inactivation [ 15 , 16 ]; thus, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) becomes unable to bind the substrate after oxidation or nitrosylation of SH groups in its active center [ 17 ]. These spontaneous changes in post-translational enzymes lead to the accumulation of ROS and triisophosphates – the main source of MG in the cell.

Erythrophagocytes In Hemolytic Anemia, Wound Healing, And Cancer: Trends In Molecular Medicine

The largest contribution to the pool of endogenous MG is made by non-enzymatic hydrolysis reactions of the phosphate group of triisophosphates: DHAP and G3P [ 10 , 11 ]. Two glycolytic enzymes are involved in this metabolism. They are triose phosphate isomerases that regulate the interconversion of DHAP and G3P, and GAPDH oxidizes G3P to phosphoglyceric acid. When the synthesis and activity of these enzymes is disrupted, MG is produced excessively. RBCs with mutant triisophosphate isomerase contain 20–40 times higher levels of DHAP than in the control variant [ 18 ]. The activity of these enzymes in red blood cells during carbonyl stress will be described in more detail in chapter 3.

A somewhat exotic cause of carbonyl stress produced in red blood cells may be Plasmodium malaria infection. Malaria was the first disease shown to be caused by protozoa (1880). Charles Louis Alphonse Laveran was awarded the Nobel Prize for this discovery in 1907. Several species of the Plasmodium genus (P. malariae, P. falciparum and P. vivax) are known to cause this infection. This is a rather rare case of intracellular infection, when a protozoan (hedge cell) forms inside a cell as small as an erythrocyte. Plasmodium feeds on the contents of red blood cells, primarily Hb, as the main protein of this cell. Both on drawings made by

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