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Related Concept Videos

Hemoglobin01:24

Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Oxygen Transport in the Blood01:27

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Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
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Structure and Function of Erythrocytes01:29

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There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
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Protein Denaturation01:28

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Disorders of Erythrocytes01:27

Disorders of Erythrocytes

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Disorders of erythrocytes, or red blood cells (RBCs), include a range of conditions affecting their number, shape, or function.
Erythrocyte disorders can be broadly categorized into two main types: anemic and polycythemic conditions.
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On the other...
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Factors Affecting Erythropoiesis01:24

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The cardiovascular system regulates the number of erythrocytes in the bloodstream to ensure optimal oxygen transport. It also prevents over-proliferation of these cells, which helps to maintain blood viscosity and flow rate.
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Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry
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Hemoglobin Binding to the Red Blood Cell (RBC) Membrane Is Associated with Decreased Cell Deformability.

Gregory Barshtein1, Leonid Livshits2, Alexander Gural3

  • 1Department of Biochemistry, The Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 9112001, Israel.

International Journal of Molecular Sciences
|June 19, 2024
PubMed
Summary
This summary is machine-generated.

Red blood cell (RBC) deformability decreases as hemoglobin (Hb) binds to the cell membrane. Increased membrane-bound Hb (MBHb) negatively impacts RBC mechanical properties, affecting oxygen delivery.

Keywords:
RBC deformabilityhemoglobinmembrane-bound hemoglobinred blood cells

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Area of Science:

  • Hematology
  • Biophysics
  • Cell Biology

Background:

  • Red blood cell (RBC) deformability is crucial for efficient oxygen delivery and microcirculation.
  • Aging, storage, or stress can alter RBC structure, leading to hemoglobin (Hb) redistribution.
  • Increased membrane-bound Hb (MBHb) can affect RBC mechanical properties, particularly deformability.

Purpose of the Study:

  • To investigate the correlation between membrane-bound Hb (MBHb) levels and RBC deformability.
  • To identify specific Hb subunits involved in altered RBC mechanics.

Main Methods:

  • Quantification of MBHb levels using mass spectrometry.
  • Assessment of RBC deformability through image analysis.
  • Statistical analysis to determine correlations between MBHb and deformability.

Main Results:

  • Six hemoglobin subunits were identified attached to RBC membranes.
  • RBC deformability showed a significant negative correlation with the levels of four specific Hb subunits.
  • A strong inter-correlation was observed among these four subunits.

Conclusions:

  • Hb redistribution and subsequent binding to the RBC membrane contribute to reduced RBC deformability.
  • MBHb accumulation negatively impacts RBC mechanical function.
  • Understanding this mechanism is vital for managing blood storage and treating related conditions.