Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Nitric Oxide Signaling Pathway01:28

Nitric Oxide Signaling Pathway

Nitric oxide (NO), an inorganic gas, acts as a potent second messenger in most animal and plant tissues. NO diffuses out of the cells that produce it and enters the neighboring cells to generate a downstream response. NO synthase (NOS) catalyzes NO production by the deamination of the amino acid arginine. There are three isoforms of NOS. Endothelial cells have endothelial NOS (eNOS), nerve and muscle cells have neuronal NOS (nNOS), and macrophages produce inducible NOS (iNOS) upon exposure to...
Factors Affecting Erythropoiesis01:24

Factors Affecting Erythropoiesis

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.
Several factors influence the erythrocyte production rate, with tissue oxygen level being among the most critical. Intense exercise or high altitudes can cause tissue hypoxia, which triggers the kidneys to release more erythropoietin (EPO) into the bloodstream.
EPO then...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
Hemoglobin01:24

Hemoglobin

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...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

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,...
Redox Reactions01:27

Redox Reactions

Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Red Blood Cells in Normal and Pathological States: Redox Reactions of Hemoglobin.

Molecules (Basel, Switzerland)·2026
Same author

The Role of Accessible Hematological Markers in Bullous Pemphigoid: A Systematic Review.

International journal of molecular sciences·2026
Same author

The Effect of Escin on the Plasma Membrane of Human Red Blood Cells.

International journal of molecular sciences·2025
Same author

Potential Compounds as Inhibitors of Staphylococcal Virulence Factors Involved in the Development of Thrombosis.

Toxins·2025
Same author

The Roles of Oxidative Stress and Red Blood Cells in the Pathology of the Varicose Vein.

International journal of molecular sciences·2025
Same author

Systematic Review of Sarcopenia Biomarkers in Hip Fracture Patients as a Potential Tool in Clinical Evaluation.

International journal of molecular sciences·2025

Related Experiment Video

Updated: Jul 10, 2026

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

Nitric oxide induced oxidative changes in erythrocyte membrane components.

Joanna Brzeszczynska1, Krzysztof Gwozdzinski

  • 1School of Life Sciences, Heriot-Watt University, Edinburgh EH14 4AS, UK. joanna.brzeszczynska@hw.ac.uk

Cell Biology International
|November 6, 2007
PubMed
Summary

Nitric oxide (NO) alters erythrocyte membrane structure and dynamics by increasing fluidity and lipid peroxidation. This suggests NO acts as a pro-oxidant, targeting the membrane before entering the cell.

More Related Videos

Immunostaining-Based Detection of Dynamic Alterations in Red Blood Cell Proteins
10:07

Immunostaining-Based Detection of Dynamic Alterations in Red Blood Cell Proteins

Published on: March 17, 2023

En Face Detection of Nitric Oxide and Superoxide in Endothelial Layer of Intact Arteries
08:58

En Face Detection of Nitric Oxide and Superoxide in Endothelial Layer of Intact Arteries

Published on: February 25, 2016

Related Experiment Videos

Last Updated: Jul 10, 2026

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds
08:23

Chemiluminescence-based Assays for Detection of Nitric Oxide and its Derivatives from Autoxidation and Nitrosated Compounds

Published on: February 16, 2022

Immunostaining-Based Detection of Dynamic Alterations in Red Blood Cell Proteins
10:07

Immunostaining-Based Detection of Dynamic Alterations in Red Blood Cell Proteins

Published on: March 17, 2023

En Face Detection of Nitric Oxide and Superoxide in Endothelial Layer of Intact Arteries
08:58

En Face Detection of Nitric Oxide and Superoxide in Endothelial Layer of Intact Arteries

Published on: February 25, 2016

Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Nitric oxide (NO) plays diverse roles in cellular environments.
  • Its precise mechanisms, especially at low concentrations, require further elucidation.
  • Understanding NO's interaction with cellular membranes is crucial.

Purpose of the Study:

  • To investigate the effects of low concentrations of NO on erythrocyte membrane structure and dynamics.
  • To elucidate the oxidative mechanism of NO-induced cellular membrane alterations.
  • To determine if NO acts as a pro-oxidant targeting the erythrocyte membrane.

Main Methods:

  • Exposure of erythrocytes to low concentrations of NO (0.1; 0.2 mmol/l).
  • Analysis of qualitative changes in membrane structure and dynamics.
  • Assessment of lipid peroxidation and conformational changes in cytoskeleton proteins.

Main Results:

  • NO significantly increased erythrocyte membrane fluidity at various lipid bilayer depths.
  • Increased lipid peroxidation was observed, correlated with increased membrane fluidity.
  • Statistically significant changes in the conformational state of cytoskeleton proteins were detected.
  • NO-induced oxidative alterations were independent of peroxynitrite (ONOOH) generation.

Conclusions:

  • Pure NO, not ONOOH, induces oxidative alterations in erythrocyte membranes at low concentrations.
  • NO influences erythrocyte membrane fluidity and lipid peroxidation.
  • NO affects the conformational state of cytoskeleton proteins, impacting rheological properties.
  • NO acts as a pro-oxidant, with the erythrocyte membrane as its initial target.