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Haptoglobin information


HP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHP, BP, HP2ALPHA2, HPA1S, haptoglobin
External IDsOMIM: 140100; MGI: 96211; HomoloGene: 121756; GeneCards: HP; OMA:HP - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001126102
NM_005143
NM_001318138

NM_017370
NM_001329965

RefSeq (protein)

NP_001119574
NP_001305067
NP_005134

NP_001316894
NP_059066

Location (UCSC)Chr 16: 72.05 – 72.06 MbChr 8: 110.3 – 110.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
A model of α,β-hemoglobin/haptoglobin hexamer complex. There are 2 α,β-hemoglobin dimers depicted: one space filling model (yellow/orange), and one ribbon model (purple/blue). Each is bound by a haptoglobin molecule (both haptoglobin molecules are shown in pink, with one as a space filling model and one as a ribbon model).

Haptoglobin (abbreviated as Hp) is the protein that in humans is encoded by the HP gene.[5][6] In blood plasma, haptoglobin binds with high affinity to free hemoglobin[7] released from erythrocytes, and thereby inhibits its deleterious oxidative activity. Compared to Hp, hemopexin binds to free heme.[8] The haptoglobin-hemoglobin complex will then be removed by the reticuloendothelial system (mostly the spleen).

In clinical settings, the haptoglobin assay is used to screen for and monitor intravascular hemolytic anemia. In intravascular hemolysis, free hemoglobin will be released into circulation and hence haptoglobin will bind the hemoglobin. This causes a decline in haptoglobin levels.

The protein was discovered as a "plasma substance" in 1938 by French biochemists Max-Fernand Jayle and Michel Polonovski.[9][10]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000257017 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031722 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Dobryszycka W (September 1997). "Biological functions of haptoglobin--new pieces to an old puzzle". European Journal of Clinical Chemistry and Clinical Biochemistry. 35 (9): 647–654. PMID 9352226.
  6. ^ Wassell J (2000). "Haptoglobin: function and polymorphism". Clinical Laboratory. 46 (11–12): 547–552. PMID 11109501.
  7. ^ Schaer DJ, Vinchi F, Ingoglia G, Tolosano E, Buehler PW (28 October 2014). "Haptoglobin, hemopexin, and related defense pathways-basic science, clinical perspectives, and drug development". Frontiers in Physiology. 5. Frontiers Media SA: 415. doi:10.3389/fphys.2014.00415. PMC 4211382. PMID 25389409.
  8. ^ Cite error: The named reference eClinpath was invoked but never defined (see the help page).
  9. ^ Shih AW, McFarlane A, Verhovsek M (April 2014). "Haptoglobin testing in hemolysis: measurement and interpretation". American Journal of Hematology. 89 (4): 443–447. doi:10.1002/ajh.23623. PMID 24809098.
  10. ^ "Haptoglobins". New England Journal of Medicine. 266 (11): 569–570. 15 March 1962. doi:10.1056/NEJM196203152661115. ISSN 0028-4793.

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the physiologic range of haptoglobin, the potential deleterious effects of free hemoglobin are prevented because haptoglobin will bind to "free hemoglobin"...

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hemoglobin is released and binds with haptoglobin. This causes haptoglobin levels to decrease. Once haptoglobin is saturated, free hemoglobin readily...

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Hemopexin

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detoxification. Hemopexin is different from haptoglobin, the latter always binds to free hemoglobin. (See Haptoglobin § Differentiation with hemopexin) Takahashi...

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Serum protein electrophoresis

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alpha-2 macroglobulin (AMG or A2M) and haptoglobin. There are typically low levels in haemolytic anaemia (haptoglobin is a suicide molecule which binds with...

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CD163

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affinity scavenger receptor for the hemoglobin-haptoglobin complex and in the absence of haptoglobin - with lower affinity - for hemoglobin alone. It...

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Free hemoglobin can bind to haptoglobin, and the complex is cleared from the circulation; thus, a decrease in haptoglobin can support a diagnosis of hemolytic...

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trypanosome haptoglobin-hemoglobin receptor (TbHpHbR). TLF-2 enters trypanosomes independently of TbHpHbR. TLF-1 uptake increases when haptoglobin level is...

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into the bloodstream in excess of the binding capacity of haptoglobin. The function of haptoglobin is to bind to circulating hemoglobin, thereby reducing...

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Alpha-1-fetoprotein alpha2-macroglobulin Gamma globulins Beta-2 microglobulin Haptoglobin Human Serum Albumin Ceruloplasmin Complement component 3 Complement component...

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Hemolysis

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production of bilirubin and depletion of plasma proteins, such as albumin, haptoglobin, and hemopexin, which may lead to jaundice. It may also lead to increased...

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Rhabdomyolysis

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accumulation of myoglobin in the kidney tubules. Normally, the blood protein haptoglobin binds circulating myoglobin and other heme-containing substances, but...

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Hereditary spherocytosis

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processed in the liver. Haptoglobin (free): Decreased (normal range: 41–165 mg/dL). This is caused by hemoglobin binding to haptoglobin, thus making it no...

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hemolysis; including elevated lactate dehydrogenase (LDH), decreased haptoglobin and elevated unconjugated bilirubin. Reticulocytosis, or an increase...

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