Target type: biologicalprocess
Any process involved in the maintenance of an internal steady state of copper ions within an organism or cell. [GOC:ai, GOC:jid, GOC:mah]
Copper ion homeostasis is a tightly regulated process that ensures adequate levels of copper are available for essential biological functions while preventing toxic accumulation. It involves a complex interplay of proteins that facilitate copper absorption, distribution, storage, and excretion.
**Absorption:** Copper enters the body primarily through dietary intake. In the small intestine, copper is absorbed by a specialized transporter called Ctr1. Ctr1 facilitates the uptake of copper ions across the intestinal epithelial cells and into the bloodstream.
**Distribution:** Once in the bloodstream, copper binds to ceruloplasmin, a major copper-carrying protein. Ceruloplasmin delivers copper to various tissues and organs, including the liver, brain, and skeletal muscle. Copper is also transported by albumin and transcuprein, which play a role in copper distribution and detoxification.
**Storage:** The liver is the primary storage site for copper. Copper is stored in the liver as metallothionein, a small protein that binds to heavy metals, including copper. Metallothionein protects the liver from copper toxicity and acts as a reservoir for copper release when needed.
**Excretion:** The primary route of copper excretion is through bile. Copper is excreted in the bile as a complex with glutathione and other ligands. The bile is then transported to the small intestine, where a small amount of copper may be reabsorbed, while the majority is excreted in the feces.
**Regulation:** Copper homeostasis is tightly regulated at multiple levels. The amount of copper absorbed from the diet is regulated by the expression and activity of Ctr1. The liver also plays a critical role in maintaining copper balance. When copper levels are high, the liver reduces copper absorption and increases copper excretion. Conversely, when copper levels are low, the liver increases copper absorption and decreases copper excretion.
**Biological Functions:** Copper is an essential cofactor for numerous enzymes involved in a wide range of biological processes, including:
* **Cellular Respiration:** Copper is required for the function of cytochrome c oxidase, a key enzyme in the electron transport chain, which is essential for ATP production.
* **Neurotransmission:** Copper is involved in the production of dopamine and norepinephrine, neurotransmitters that play crucial roles in mood, motivation, and attention.
* **Iron Metabolism:** Copper is required for the activity of ceruloplasmin, an enzyme that oxidizes ferrous iron (Fe2+) to ferric iron (Fe3+). This conversion is essential for iron absorption and transport.
* **Connective Tissue Formation:** Copper is essential for the activity of lysyl oxidase, an enzyme involved in the cross-linking of collagen and elastin, proteins that provide structure and strength to connective tissues.
* **Antioxidant Defense:** Copper is a cofactor for superoxide dismutase, an enzyme that protects cells from damage caused by reactive oxygen species.
**Consequences of Dysregulation:**
* **Copper Deficiency:** Copper deficiency can lead to anemia, bone abnormalities, neurological disorders, and impaired immune function.
* **Copper Toxicity:** Excessive copper accumulation can lead to liver damage, Wilson's disease (a genetic disorder characterized by copper accumulation in the liver, brain, and other organs), and other health problems.
**Conclusion:** Copper ion homeostasis is a critical process that ensures the proper functioning of essential biological processes while preventing copper toxicity. The intricate network of proteins involved in copper absorption, distribution, storage, and excretion maintains copper balance within a narrow range, ensuring optimal health.'
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Protein | Definition | Taxonomy |
---|---|---|
E3 ubiquitin-protein ligase XIAP | A baculoviral IAP repeat-containing protein 4 that is encoded in the genome of human. [PRO:CNA, UniProtKB:P98170] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
embelin | embelin : A member of the class of dihydroxy-1,4-benzoquinones that is 2,5-dihydroxy-1,4-benzoquinone which is substituted by an undecyl group at position 3. Isolated from Lysimachia punctata and Embelia ribes, it exhibits antimicrobial, antineoplastic and inhibitory activity towards hepatitis C protease. embelin: from Embelia fruit (Myrsinaceae) | dihydroxy-1,4-benzoquinones | antimicrobial agent; antineoplastic agent; hepatitis C protease inhibitor; plant metabolite |
phenylalanine | L-phenylalanine : The L-enantiomer of phenylalanine. phenylalanine : An aromatic amino acid that is alanine in which one of the methyl hydrogens is substituted by a phenyl group. Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE. | amino acid zwitterion; erythrose 4-phosphate/phosphoenolpyruvate family amino acid; L-alpha-amino acid; phenylalanine; proteinogenic amino acid | algal metabolite; EC 3.1.3.1 (alkaline phosphatase) inhibitor; Escherichia coli metabolite; human xenobiotic metabolite; micronutrient; mouse metabolite; nutraceutical; plant metabolite; Saccharomyces cerevisiae metabolite |
kaempferol | 7-hydroxyflavonol; flavonols; tetrahydroxyflavone | antibacterial agent; geroprotector; human blood serum metabolite; human urinary metabolite; human xenobiotic metabolite; plant metabolite | |
kaempferol 3-o-rhamnoside | afzelin : A glycosyloxyflavone that is kaempferol attached to an alpha-L-rhamnosyl residue at position 3 via a glycosidic linkage. kaempferol 3-O-rhamnoside: from apple (Malus domestica) leaves; structure in first source | glycosyloxyflavone; monosaccharide derivative; trihydroxyflavone | anti-inflammatory agent; antibacterial agent; plant metabolite |
lbw242 | LBW242: proapoptotic IAP inhibitor; low MW Smac (Second mitochondria-derived activator of caspases) mimetic; structure in first source | ||
sm 164 | SM 164: a bivalent Smac mimetic with antineoplastic activity; structure in first source | benzenes; organic heterobicyclic compound; secondary carboxamide; triazoles | antineoplastic agent; apoptosis inducer; radiosensitizing agent |
lcl161 | 1,3-thiazoles; aromatic ketone; L-alanine derivative; monofluorobenzenes; N-acylpyrrolidine | antineoplastic agent; apoptosis inducer | |
at 406 | |||
gdc-0152 | GDC-0152: structure in first source | ||
birinapant | birinapant: a Smac mimetic with antineoplastic activity | dipeptide | |
nvp-cgm097 | NVP-CGM097: an MDM2 and HDM2 inhibitor; structure in first source | ||
2-carboxyarabinitol 1-phosphate |