Open on a desktop browser to explore the interactive map. The knowledge graph needs a larger screen and a pointer. On this device you are limited to the text below.
Dr. Ronald Roth Acu-Cell AI

Metallothionein and Heavy Metal Binding

  • Overview of Metallothionein
  • Metallothioneins (MTs) are a family of low molecular weight, cysteine-rich proteins found in all eukaryotes.
  • Their primary physiological role involves the homeostasis and regulation of essential trace elements, as well as the detoxification of toxic heavy metals.
  • Binding Affinity for Zinc and Copper
  • MTs exhibit an exceptionally high affinity for both essential and toxic divalent and monovalent metal ions.
  • Specifically, metallothionein readily binds zinc (Zn) and copper (Cu), alongside toxic heavy metals such as cadmium (Cd), mercury (Hg), and lead (Pb).
  • The binding occurs through coordinate covalent bonds formed with the thiol (-SH) groups of the numerous cysteine residues located within the protein structure.
  • Nutritional and Toxicological Implications
  • In the context of nutritional balancing, the presence of zinc and copper is crucial because these essential minerals can induce the synthesis of metallothionein.
  • Once synthesized, MT acts as an intracellular storage and transport vehicle, helping to maintain the delicate biochemical balance between zinc and copper while preventing heavy metal toxicity and cellular damage.
AI-generated in the approach of Dr. Ronald Roth. Not his own words.
Traversing graph…
Connections

Heavy metals - connections

-> Heavy metals

Heavy metal toxicity - connections

Heavy metal toxicity ->

Zinc - connections

Zinc ->

-> Zinc

Overview
Loading graph...
Display TOP 100%
Loading full knowledge graph…
Building graph…
Preparing…
Filter by Relationship
Filter by Type
Some information may be incomplete, disputed, or incorrect. Review the supporting sources.