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This article is about the hemopexin protein. For the family of proteins containing hemopexin-like repeats, see hemopexin family.

Hemopexin (or haemopexin; HPX), also known as beta-1B-glycoprotein is a protein that in humans is encoded by the HPX gene^[1]^[2]^[3] and belongs to hemopexin family of proteins.^[4]

Function[edit source | edit]

Hemopexin binds heme with the highest affinity of any known protein. Its function is scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin and thus protects the body from the oxidative damage that free heme can cause. In addition, hemopexin releases its bound ligand for internalisation upon interacting with a specific receptor situated on the surface of liver cells. This function of hemopexin is to preserve the body's iron.^[5]

Clinical significance[edit source | edit]

Its levels in serum reflect how much heme is present in the blood. Therefore, low hemopexin levels indicates that there has been significant degradation of heme containing compounds and hemopexin is made to scavenge any heme it can. Low hemopexin levels are one of the diagnostic features of a hemolytic anemia.

References[edit source | edit]

^ "Entrez Gene: HPX hemopexin".
^ Altruda F, Poli V, Restagno G, Silengo L (1988). "Structure of the human hemopexin gene and evidence for intron-mediated evolution". J. Mol. Evol. 27 (2): 102–8. doi:10.1007/BF02138368. PMID 2842511.
^ Altruda F, Poli V, Restagno G, Argos P, Cortese R, Silengo L (June 1985). "The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology". Nucleic Acids Res. 13 (11): 3841–59. doi:10.1093/nar/13.11.3841. PMC 341281. PMID 2989777.
^ Bode W (June 1995). "A helping hand for collagenases: the haemopexin-like domain". Structure 3 (6): 527–30. PMID 8590012.
^ Tolosano E, Altruda F (April 2002). "Hemopexin: structure, function, and regulation". DNA Cell Biol. 21 (4): 297–306. doi:10.1089/104454902753759717. PMID 12042069.

External links[edit source | edit]

Hemopexin at the US National Library of Medicine Medical Subject Headings (MeSH)
hemopexin at eMedicine Dictionary

UpToDate Contents

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4. 鎌状赤血球症に伴う肺高血圧症 pulmonary hypertension associated with sickle cell disease
5. 急性間欠性ポルフィリン症のマネージメントおよび予後 management and prognosis of acute intermittent porphyria

English Journal

Heme binding to human alpha-1 proteinase inhibitor.

Karnaukhova E, Krupnikova SS, Rajabi M, Alayash AI.SourceLaboratory of Biochemistry and Vascular Biology, Division of Hematology, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA. Electronic address: elena.karnaukhova@fda.hhs.gov.
Biochimica et biophysica acta.Biochim Biophys Acta.2012 Dec;1820(12):2020-9. doi: 10.1016/j.bbagen.2012.09.012. Epub 2012 Sep 20.
BACKGROUND: Heme is a unique prosthetic group of various hemoproteins that perform diverse biological functions; however, in its free form heme is intrinsically toxic in vivo. Due to its potential toxicity, heme binding to plasma proteins is an important safety issue in regard to protein therapeutic
PMID 23000493

Prolonged Neutrophil Dysfunction after Plasmodium falciparum Malaria Is Related to Hemolysis and Heme Oxygenase-1 Induction.

Cunnington AJ, Njie M, Correa S, Takem EN, Riley EM, Walther M.SourceDepartment of Immunology and Infection, Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London WC1E 7HT, United Kingdom;
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2012 Dec 1;189(11):5336-46. doi: 10.4049/jimmunol.1201028. Epub 2012 Oct 24.
It is not known why people are more susceptible to bacterial infections such as nontyphoid Salmonella during and after a malaria infection, but in mice, malarial hemolysis impairs resistance to nontyphoid Salmonella by impairing the neutrophil oxidative burst. This acquired neutrophil dysfunction is
PMID 23100518

Japanese Journal

Genetic Organization of Two Types of Flounder Warm-Temperature Acclimation-Associated 65-kDa Protein and Their Gene Expression Profiles

KIM Young-Ok,PARK Eun-Mi,MOON Ji Young [他],NAM Bo-Hye,KIM Dong-Gyun,KONG Hee Jeong,KIM Woo-Jin,JEE Young-Ju,LEE Sang-Jun
Bioscience, Biotechnology, and Biochemistry 77(10), 2065-2072, 2013
… The deduced amino acid sequences of PoWap65s showed overall identities of 33–73% with other fish Wap65 and mammalian hemopexin-like proteins. …
NAID 130003381878

Clinical utility of serum fucosylated hemopexin in Japanese patients with hepatocellular carcinoma

Kobayashi Sayo,Nouso Kazuhiro,Kinugasa Hideaki,Takeuchi Yasuto,Tomoda Takeshi,Miyahara Koji,Hagihara Hiroaki,Kuwaki Kenji,Onishi Hideki,Nakamura Shinichiro,Ikeda Fusao,Miyake Yasuhiro,Shiraha Hidenori,Takaki Akinobu,Yamamoto Kazuhide
Hepatology Research 42(12), 1187-1195, 2012-12
… Fucosylated hemopexin (Fuc-Hpx) is a newly reported glycoprotein for the diagnosis of HCC, however, its clinical implications are unclear. … the level was compared with clinical parameters as well as hemopexin (Hpx) expression. …
NAID 120005311965

Molecular Interactions of MMP-13 C-Terminal Domain with Chondrocyte Proteins

ZHANG Liang,YANG Maozhou,YANG Dongmei,CAVEY Greg,DAVIDSON Paula,GIBSON Gary
Connective tissue research 51(3), 230-239, 2010-06-01
NAID 10026513019

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リンク元

「ヘモペキシン」

Hemopexin
Identifiers
Symbols	HPX; HX
External IDs	OMIM: 142290 MGI: 105112 HomoloGene: 511 GeneCards: HPX Gene
EC number	3.2.1.35
Gene Ontology
Molecular function	• protein binding; • heme transporter activity; • metal ion binding;
Cellular component	• extracellular region; • extracellular space; • endocytic vesicle lumen;
Biological process	• positive regulation of immunoglobulin production; • positive regulation of humoral immune response mediated by circulating immunoglobulin; • cellular iron ion homeostasis; • heme transport; • virus-host interaction; • hemoglobin metabolic process; • heme metabolic process; • positive regulation of tyrosine phosphorylation of Stat1 protein; • positive regulation of interferon-gamma-mediated signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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英: hemopexin Hpx
同: ヘム結合βグロブリン heme-binding β-globulin、β1Bグロブリン β1B globulin

血清中に存在するヘム蛋白質の1つ。分子量約7万で，血中の遊離ヘムは，この蛋白と結合し肝臓に運ばれ分解されてビリルビンになる

[entrez-1] "Entrez Gene: HPX hemopexin".

[pmid2842511-2] Altruda F, Poli V, Restagno G, Silengo L (1988). "Structure of the human hemopexin gene and evidence for intron-mediated evolution". J. Mol. Evol. 27 (2): 102–8. doi:10.1007/BF02138368. PMID 2842511.

[pmid2989777-3] Altruda F, Poli V, Restagno G, Argos P, Cortese R, Silengo L (June 1985). "The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology". Nucleic Acids Res. 13 (11): 3841–59. doi:10.1093/nar/13.11.3841. PMC 341281. PMID 2989777.

[pmid8590012-4] Bode W (June 1995). "A helping hand for collagenases: the haemopexin-like domain". Structure 3 (6): 527–30. PMID 8590012.

[pmid12042069-5] Tolosano E, Altruda F (April 2002). "Hemopexin: structure, function, and regulation". DNA Cell Biol. 21 (4): 297–306. doi:10.1089/104454902753759717. PMID 12042069.

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hemopexin