Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Denaturation

Protein Denaturation

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...

Hemoglobin

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...

Lifecycle of Erythrocytes

Lifecycle of Erythrocytes

Erythrocytes, also known as red blood cells, constantly move through blood capillaries. As a result, they damage their plasma membrane due to the continuous friction. Typically, after 100 to 120 days, erythrocytes become rigid and fragile as they wear out. As they pass through small vessels in the spleen and liver, they can get trapped and break apart into fragments.
The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups....

Oxygen Transport in the Blood

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,...

Protein Buffers in Blood Plasma and Cells

Protein Buffers in Blood Plasma and Cells

The human body utilizes protein buffer systems to maintain a stable pH. These systems capitalize on the dual role of amino acids, which can act as acids or bases by accepting or releasing hydrogen ions in response to pH changes. Protein buffer systems are particularly significant in the extracellular fluid (ECF) and intracellular fluid (ICF) of active cells, where structural and functional proteins provide substantial buffering capacity.
Certain amino acids can exist in a zwitterion state at a...

Extracorporeal Removal of Drugs: Hemoperfusion and Hemofiltration

Extracorporeal Removal of Drugs: Hemoperfusion and Hemofiltration

Hemoperfusion and hemofiltration are critical techniques in medical treatments to eliminate accumulated drugs, metabolites, and electrolytes from the bloodstream. These methods are particularly vital in cases of accidental poisoning and drug overdose.Hemoperfusion involves passing blood through an adsorbent material to remove unwanted substances. The main adsorbents used in hemoperfusion include activated charcoal and Amberlite resins. Activated charcoal can adsorb both polar and nonpolar...

You might also read

Related Articles

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

Sort by

Same author

Plasma heme pool compartmentalization is linked to pathophysiology in Sickle Cell Disease.

PloS one·2026

Same author

Phase I study of the safety and pharmacokinetics of CSL889 (hemopexin) in adults with sickle cell anemia.

Haematologica·2026

Same author

CD39 polymorphism enables lung thrombosis in sickle cell disease.

Nature communications·2026

Same author

Ten-Year Longitudinal Study Clarifies Impact of Hemolysis and Pulmonary Hypertension on Patients with Sickle Cell Anemia.

American journal of respiratory and critical care medicine·2025

Same author

Targeted Proteomic Analysis of Sickle Cell Disease Patients With Elevated Tricuspid Regurgitation Velocity.

Proteomics. Clinical applications·2025

Same author

Small-molecule inhibitor screen to identify mechanisms of sickle hemoglobin clearance by liver endothelium.

Blood vessels, thrombosis & hemostasis·2025

Search research articles

Related Experiment Video

Updated: May 5, 2026

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

Published on: February 7, 2013

Haptoglobin halts hemoglobin's havoc.

Gregory J Kato¹

¹Sickle Cell Vascular Disease Section, Pulmonary and Vascular Medicine Branch, National Heart, Lung, and Blood Institute, and Critical Care Medicine Department, Clinical Center, National Institutes of Health, Maryland 20892-1476, USA. gkato@nhlbi.nih.gov

The Journal of Clinical Investigation

|July 22, 2009

Summary

Glucocorticoids increase haptoglobin (Hp) levels, which bind to free hemoglobin (Hb). This binding prevents Hb-induced hypertension and kidney damage, revealing an anti-inflammatory mechanism.

More Related Videos

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

Related Experiment Videos

Last Updated: May 5, 2026

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

Published on: February 7, 2013

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

Area of Science:

Cardiovascular Biology
Renal Physiology
Pharmacology

Background:

Intravascular hemolysis releases hemoglobin (Hb) into plasma, causing nitric oxide (NO) depletion, oxidative stress, and hypertension.
Free Hb contributes to vascular dysfunction and organ damage, particularly in the kidneys.
Haptoglobin (Hp) is the primary scavenger protein for cell-free Hb in circulation.

Discussion:

Glucocorticoids, at pharmacological doses, elevate plasma Hp levels in canine and guinea pig models.
Increased Hp effectively neutralizes free Hb, mitigating Hb-induced hypertension.
This Hp-mediated Hb neutralization is linked to the anti-inflammatory effects of glucocorticoids.

Key Insights:

Pharmacological glucocorticoids enhance the plasma Hb-scavenging capacity via increased Hp.
Haptoglobin plays a critical role in preventing hypertension and oxidant damage to the kidneys caused by free Hb.
Hb neutralization by Hp is a downstream anti-inflammatory pathway for glucocorticoids.

Outlook:

Further investigation into glucocorticoid-induced Hp modulation could offer novel therapeutic strategies for hemolytic conditions.
Understanding the interplay between Hb, Hp, and glucocorticoids may provide insights into managing hypertension associated with hemolysis.
Exploring Hp-based therapies could be a future direction for treating conditions involving free Hb toxicity.