Metallothionein, an explanation
Function
Metallothionein proteins participate in the uptake, transport, and regulation of zinc in a biological system. The zinc binding sites are typically cysteine-rich, and often bind three or four zinc ions. In some proteins, histidine also participates in zinc binding. By binding and releasing zinc, metallothioneins (MTs) regulate its level within the body. Zinc, in turn, is a key element for the activation and binding of certain transcription factors through its participation in (aptly-named) zinc fingers. Metallothionein also carries zinc ions (signals) from one part of the cell to another. When zinc enters a cell, it can be picked up by thionein (which thus becomes "metallothionein") and carried to another part of the cell where it is released to another organelle or protein. In this way the thionein-metallothionein becomes a key component of the zinc signaling system in cells. This system is particularly important in the brain, where zinc signaling is prominent both between and within nerve cells. It also seems to be important for the regulation of the tumor suppressor protein p53.
Metallothionein (MT) detoxifies mercury and heavy metals by binding to the metal before it can cause harm. It forms subcellular inclusions or crystals which act jointly to consolidate and enclose excess metals. These inclusions then accumulate within tissues or skeletal structure over time.
Metallothionein proteins participate in the uptake, transport, and regulation of zinc in a biological system. The zinc binding sites are typically cysteine-rich, and often bind three or four zinc ions. In some proteins, histidine also participates in zinc binding. By binding and releasing zinc, metallothioneins (MTs) regulate its level within the body. Zinc, in turn, is a key element for the activation and binding of certain transcription factors through its participation in (aptly-named) zinc fingers. Metallothionein also carries zinc ions (signals) from one part of the cell to another. When zinc enters a cell, it can be picked up by thionein (which thus becomes "metallothionein") and carried to another part of the cell where it is released to another organelle or protein. In this way the thionein-metallothionein becomes a key component of the zinc signaling system in cells. This system is particularly important in the brain, where zinc signaling is prominent both between and within nerve cells. It also seems to be important for the regulation of the tumor suppressor protein p53.
Metallothionein (MT) detoxifies mercury and heavy metals by binding to the metal before it can cause harm. It forms subcellular inclusions or crystals which act jointly to consolidate and enclose excess metals. These inclusions then accumulate within tissues or skeletal structure over time.