When Unstable Hemoglobin Lansing Interacts with Alpha Thalassemia Along with HbS: An Interesting Case with Unique

Adwait Marhatta1, Jui Choudhuri1, Joseph J Mulvey1

  • 1Department of Pathology, Montefiore Medical Center/Albert Einstein College of Medicine, Bronx, New York, USA.

Hemoglobin
|July 27, 2025
PubMed

Hemoglobin (Hb) Lansing is a rare mildly unstable variant of α globin. Here, we report the first case of compound Hb Lansing/HbS coinherited with a single α thalassemia deletion (-alpha3.7) in a 27-year-old woman. The patient exhibited moderate hemolytic anemia and low oxygen saturation by pulse oximetry, which failed to improve with supplemental oxygen. Notably, her oxygen saturation levels were normal by arterial blood gas. Capillary electrophoresis and high-performance liquid chromatography showed an HbS peak along with other abnormal peaks. Subsequent α globin gene sequencing revealed one copy of the -alpha3.7 α-globin deletion and one copy of Hb Lansing variant in the alpha2-globin gene. Hemoglobin Lansing is known to cause spuriously low pulse oximetry. Additionally, the co-inheritance of the Hb Lansing and a single α thalassemia deletion may contribute to her moderate hemolytic anemia. The timely identification of hemoglobin variants is crucial for understanding the underlying cause when encountering unexpectedly low pulse oximetry, facilitating genetic counseling, and preventing unnecessary investigations and treatments. Further research is also needed to enhance our comprehension of the interactions among various hemoglobin variants; especially those associated with single a α thalassemia deletion.

Related Concept Videos

Multiple Allele Traits01:49

Multiple Allele Traits

The Concept of Multiple Allelism
34.9K
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...
4.4K
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,...
3.3K
Rh Blood Group01:19

Rh Blood Group

The Rhesus (Rh) antigen is crucial in determining blood groups and ensuring compatibility during blood transfusions.
1.8K
Blood Transfusion and Agglutination02:45

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...
11.2K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.0K