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Cytoglobin is the protein product of CYGB, a and .

Cytoglobin is a molecule ubiquitously expressed in all tissues and most notably utilized in . It was discovered in 2001 in hepatic during . Thus, it was originally called "stellate cell activated protein" or STAP. It received its current name in 2002. 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.


Function
Cytoglobin is a ubiquitously expressed that may facilitate diffusion of oxygen through tissues, scavenge or reactive oxygen species, or serve a protective function during .


Structure
Cytoglobin has 30-40% sequence homology with , 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.

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. In an oxidizing environment, a 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 state of the tissue.


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


Further reading

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