Cytoglobin

Mammalian protein found in Homo sapiens From Wikipedia, the free encyclopedia

Cytoglobin is the protein product of CYGB, a human and mammalian gene.[5]

Quick facts CYGB, Available structures ...
CYGB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCYGB, HGB, STAP, cytoglobin
External IDsOMIM: 608759; MGI: 2149481; HomoloGene: 12706; GeneCards: CYGB; OMA:CYGB - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_134268

NM_030206

RefSeq (protein)

NP_599030

NP_084482

Location (UCSC)Chr 17: 76.53 – 76.55 MbChr 11: 116.54 – 116.55 Mb
PubMed search[3][4]
Wikidata
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Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. It was discovered in 2001[6] in hepatic stellate cells during liver fibrosis. Thus, it was originally called "stellate cell activated protein" or STAP.[7] It received its current name in 2002.[8] It is thought to help in the distribution and storage of oxygen as well as protect against hypoxia by scavenging reactive oxygen species . The predicted function of cytoglobin is the facilitation of oxygen among tissues that don't express myoglobin.[9]

Function

Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin that may facilitate diffusion of oxygen through tissues, scavenge nitric oxide or reactive oxygen species, or serve a protective function during oxidative stress.[5][10]

Structure

Cytoglobin has 30-40% sequence homology with myoglobin, and has a similar oxygen binding affinity. One of the major differences is the presence of a 20 amino acids extension at both the n and c terminus.[11]

Cytoglobin is a hexacoordinate heme protein. The heme iron in coordinated with histidine residues on both sides, HisF8 and HisE7. The HisE7 is considered to be an "endogenous ligand." In order for oxygen or another gaseous ligand to bind, the HisE7 must dissociate from the iron, making the binding kinetics relatively slow.[12]

Diagram of how the heme group in cytoglobin interacts with the surrounding amino acids of the globin protein. Normally, the iron is coordinated with histidine residues on both sides. The HisE7 must be dissociated in order for oxygen to bind.

In an oxidizing environment, a disulfide bond between Cys38 and Cys83 of the protein forms and causes a conformational change to move HisE7 out of the way, allowing oxygen to bind. Thus, oxygen binding is dependent on the redox state of the tissue.[11]

Applications

CYGB expression can be used as a specific marker with which hepatic stellate cells can be distinguished from portal myofibroblasts in the damaged human liver.[13]

References

Further reading

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