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

Gene Families

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

Blood Transfusion and Agglutination

Blood Transfusion and Agglutination

Blood transfusion is a therapeutic measure to restore the blood volume after extensive blood loss due to an accident or a medical procedure. Blood transfusion involves drawing a certain amount of blood from a suitable donor and infusing it into the recipient.
History
The history of blood transfusion dates back to the 17th century, when early attempts were made in animals. In 1818 James Blundell, a British doctor, performed the first successful human blood transfusion. Later in 1900, Karl...

Role of Hematopoietic Growth Factors

Role of Hematopoietic Growth Factors

Hematopoietic growth factors are molecules that regulate the differentiation rate of hematopoietic stem cells (HSCs). Erythropoietin (EPO), primarily produced by the kidneys, plays a crucial role in erythrocyte production. When oxygen levels in the blood are low, EPO is released into the bloodstream, reaching the bone marrow, where it stimulates HSCs to differentiate and mature into erythrocytes, which are vital for oxygen transport.
Thrombopoietin (TPO), mainly released by the liver,...

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...

You might also read

Related Articles

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

Sort by

Same author

Hemoglobin gene therapy for β-thalassemia.

Hematology/oncology clinics of North America·2010

Same author

RD114 envelope proteins provide an effective and versatile approach to pseudotype lentiviral vectors.

Experimental biology and medicine (Maywood, N.J.)·2010

Same author

Transfusion independence and HMGA2 activation after gene therapy of human β-thalassaemia.

Nature·2010

Same author

On the road to gene therapy for beta-thalassemia and sickle cell anemia.

Pediatric hematology and oncology·2008

Same author

Activating Notch1 mutations are an early event in T-cell malignancy of Ikaros point mutant Plastic/+ mice.

Leukemia research·2006

Same author

Ikaros increases normal apoptosis in adult erythroid cells.

American journal of hematology·2005

Search research articles

Related Experiment Video

Updated: Jul 8, 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

AHSP: a novel hemoglobin helper.

¹Department of Medicine, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA. ab13@columbia.edu

The Journal of Clinical Investigation

|July 4, 2007

Summary

Alpha hemoglobin-stabilizing protein (AHSP) protects against beta thalassemia by stabilizing alpha-globin. New research shows AHSP also aids hemoglobin formation even with alpha-globin deficiency, revealing novel functions.

Area of Science:

Biochemistry
Molecular Biology
Hematology

Background:

Alpha hemoglobin-stabilizing protein (AHSP) is known to bind alpha-globin, preventing toxic aggregation in beta thalassemia.
Excess alpha-globin is a hallmark of beta thalassemia, leading to cellular damage and anemia.

Discussion:

This study reveals that AHSP plays a crucial role in stabilizing hemoglobin formation, independent of alpha-globin excess.
AHSP demonstrates a previously unrecognized function in supporting normal hemoglobin levels even under conditions of alpha-globin deficiency.

Key Insights:

AHSP is essential for stabilizing the structure of alpha-globin, mitigating its toxic effects.
AHSP facilitates hemoglobin assembly and stability, even when alpha-globin is scarce.

More Related Videos

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

Published on: December 7, 2016

A Point-of-Care Method with Integrated Decision Support Tool to Estimate Anemia at Population Level

A Point-of-Care Method with Integrated Decision Support Tool to Estimate Anemia at Population Level

Published on: January 19, 2024

Related Experiment Videos

Last Updated: Jul 8, 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

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

Published on: December 7, 2016

A Point-of-Care Method with Integrated Decision Support Tool to Estimate Anemia at Population Level

A Point-of-Care Method with Integrated Decision Support Tool to Estimate Anemia at Population Level

Published on: January 19, 2024

Outlook:

Further investigation into AHSP's multifaceted roles could uncover new therapeutic targets for hemoglobinopathies.
Understanding AHSP's regulatory mechanisms may offer insights into broader protein folding and stability processes in cells.