HBB

The alpha (HBA) and beta (HBB) loci determine the structure of the 2 types of polypeptide chains in adult hemoglobin, Hb A. The normal adult hemoglobin tetramer consists of two alpha chains and two beta chains. Mutant beta globin causes sickle cell anemia. Absence of beta chain causes beta-zero-thalassemia. Reduced amounts of detectable beta globin causes beta-plus-thalassemia. The order of the genes in the beta-globin cluster is 5'-epsilon -- gamma-G -- gamma-A -- delta -- beta--3'. [provided by RefSeq, Jul 2008]

Hemoglobin Subunit Beta

Involved in oxygen transport from the lung to the various peripheral tissues.

LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.

Spinorphin:
Functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.

Cellular oxidant detoxification Source: GOC
Hydrogen peroxide catabolic process Source: BHF-UCL
Nitric oxide transport Source: UniProtKB
Oxygen transport Source: UniProtKB
Platelet aggregation Source: UniProtKB
Positive regulation of cell death Source: BHF-UCL
Positive regulation of nitric oxide biosynthetic process Source: UniProtKB
Regulation of blood pressure Source: UniProtKB-KW
Renal absorption Source: UniProtKB
Response to hydrogen peroxide Source: BHF-UCL

Cytosol; Hemoglobin complex; Blood microparticle; Extracellular exosome; Extracellular region; Extracellular space; Endocytic vesicle lumen; Ficolin-1-rich granule lumen; Haptoglobin-hemoglobin complex; Tertiary granule lumen

Heinz body anemias (HEIBAN):
Form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency.
Beta-thalassemia (B-THAL):
A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia, while reduced amounts of detectable beta globin causes beta(+)-thalassemia. In the severe forms of beta-thalassemia, the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically, beta-thalassemia is divided into thalassemia major which is transfusion dependent, thalassemia intermedia (of intermediate severity), and thalassemia minor that is asymptomatic.
Sickle cell anemia (SKCA):
Characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues.
Beta-thalassemia, dominant, inclusion body type (B-THALIB):
An autosomal dominant form of beta thalassemia characterized by moderate anemia, lifelong jaundice, cholelithiasis and splenomegaly, marked morphologic changes in the red cells, erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors, and the presence of large inclusion bodies in the normoblasts, both in the marrow and in the peripheral blood after splenectomy.

Glucose reacts non-enzymatically with the N-terminus of the beta chain to form a stable ketoamine linkage. This takes place slowly and continuously throughout the 120-day life span of the red blood cell. The rate of glycation is increased in patients with diabetes mellitus.
S-nitrosylated; a nitric oxide group is first bound to Fe2+ and then transferred to Cys-94 to allow capture of O2.
Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure.