hemopexin
Sign in to saveAlso known as HPX, epididymis secretory sperm binding protein, beta-1B-glycoprotein
Hemopexin (or haemopexin; Hpx; Hx), also known as beta-1B-glycoprotein, is a glycoprotein that in humans is encoded by the HPX gene and belongs to the hemopexin family of proteins. Hemopexin is the plasma protein with the highest binding affinity for heme.
Protein · UniProt
Hemopexin
- Gene
- HPX
- Organism
- Homo sapiens (Human)
- Length
- 462 aa
- Molecular mass
- 51,676 Da
- Evidence
- 1: Evidence at protein level
Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation
Swiss-Prot (reviewed) · via UniProt
Clinical Trials
3 registered- COMPLETEDHpx•apoB Product as a Biomarker for Coronary Artery DiseaseShiyan City Renmin Hospital · NCT07126132
- PHASE2RECRUITINGSafety, Efficacy, and Pharmacokinetics of CSL889 in Adults and Adolescents With Sickle Cell Disease During Vaso-Occlusive CrisisCSL Behring · NCT06699849
- NACOMPLETEDThe Effect of Alpha-tocopherol in Hemolysis and Oxidative Stress Marker on the Red Cell Membrane Beta-thalassemia MajorIndonesia University · NCT03948737
Wikidata facts
Show 2 more facts
- exact match
- purl.uniprot.org/uniprot/P02790
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- Hemopexin
via Wikidata · CC0
~7 min read
Article
10 sectionsContents
- Cloning, expression, and discovery
- Mapping of hemopexin gene
- Differential transcriptional pattern of hemopexin gene
- Function
- Clinical significance
- Relation to haptoglobin
- See also
- References
- Further reading
- External links
Hemopexin (or haemopexin; Hpx; Hx), also known as beta-1B-glycoprotein, is a glycoprotein that in humans is encoded by the HPX gene and belongs to the hemopexin family of proteins. Hemopexin is the plasma protein with the highest binding affinity for heme.
Hemoglobin itself circulating alone in the blood plasma (called free hemoglobin, as opposed to the hemoglobin situated in and circulating with the red blood cell.) will soon be oxidized into met-hemoglobin which then further disassociates into free heme along with globin chain. The free heme will then be oxidized into free met-heme and sooner or later the hemopexin will come to bind free met-heme together, forming a complex of met-heme and hemopexin, continuing their journey in the circulation until reaching a receptor, such as LRP1, on hepatocytes or macrophages within the spleen, liver and bone marrow.