Related Experiment Video

Updated: Jun 12, 2026

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

Red cell changes during storage

John R Hess1

  • 1University of Maryland School of Medicine, Baltimore, MD 21201, USA. jhess@umm.edu

Transfusion and Apheresis Science : Official Journal of the World Apheresis Association : Official Journal of the European Society for Haemapheresis
|June 19, 2010
PubMed

Red blood cells can be stored in liquid suspension in approved additive solutions for periods up to 6 weeks with 0.4% hemolysis, 84% 24-h in vivo recovery, and normal subsequent survival of the cells that persist in the circulation for at least 24h. However, while they are stored, the red cells undergo changes including the loss of adenosine triphosphate, diphosphoglycerate, and potassium, oxidative injury to proteins, lipids, and carbohydrates, loss of shape and membrane, increased adhesiveness, decreased flexibility, reduced capillary flow, and decreased oxygen delivery. Deaths have been reported related to the high potassium and lysophospholipids, but are rare.

More Related Videos

Antigens Protected Functional Red Blood Cells By The Membrane Grafting Of Compact Hyperbranched Polyglycerols11:31

Antigens Protected Functional Red Blood Cells By The Membrane Grafting Of Compact Hyperbranched Polyglycerols

Published on: January 2, 2013

Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry08:23

Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry

Published on: November 5, 2019

Related Concept Videos

Lifecycle of Erythrocytes01:22

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.
Erythropoiesis01:14

Erythropoiesis

Red blood cells  (RBCs) transport oxygen to all body tissues. These cells survive only for 120 days and then need to be replenished. Erythropoiesis is the process of RBC production. In healthy individuals, erythropoiesis ensures all tissues are amply supplied with oxygen. In addition, blood loss due to injury leads to a drop in the physiological oxygen level that will cause erythropoiesis. Any defect in erythropoiesis leads to several physiological disorders, including thalassemia, anemia, and...
Disorders of Erythrocytes01:27

Disorders of Erythrocytes

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.
A low oxygen-carrying capacity of the blood due to the loss, lower production, or destruction of erythrocytes is termed anemia. Hemorrhagic anemia, for example, occurs when bleeding from an external wound or internal ulcer reduces erythrocyte counts.
On the other...
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...
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,...
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...