<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <id type="integer">644</id>
  <title>T3D0643</title>
  <common-name>Beryllium copper</common-name>
  <description>Beryllium copper is a metal alloy of beryllium and copper. It is used in springs, load cells, batteries, electrical connectors, tools and intruments. Beryllium is a lightweight alkaline earth metal with the atomic number 4. It is a relatively rare element found naturally only combined with other elements in minerals. Copper is a chemical element with the symbol Cu and atomic number 29. Copper is an essential elements in plants and animals as it is required for the normal functioning of more than 30 enzymes. It occurs naturally throughout the environment in rocks, soil, water, and air. (L277, L278, L24, L26)</description>
  <cas>11133-98-5</cas>
  <pubchem-id>21871507</pubchem-id>
  <chemical-formula>BeCu</chemical-formula>
  <weight></weight>
  <appearance>No data.</appearance>
  <melting-point></melting-point>
  <boiling-point></boiling-point>
  <density></density>
  <solubility></solubility>
  <specific-gravity></specific-gravity>
  <flash-point></flash-point>
  <vapour-pressure></vapour-pressure>
  <route-of-exposure>Oral (L277) ; inhalation (L277) ; dermal (L277)</route-of-exposure>
  <target></target>
  <mechanism-of-toxicity>Once in the body, beryllium acts as a hapten and interacts with human leucocyte antigen (HLA) DP presenting cells in the lungs, becoming physically associated with a major histocompatability (MHC) class II molecule. This MHC class II-beryllium-peptide complex is recognized by the T lymphocyte receptor, triggering CD4+ T lymphocyte activation and proliferation. The resulting inflammatory response is a cell-mediated process orchestrated by cytokines and results in the formation of (usually pulmonary) granulomas. Beryllium's toxicity may be controlled by the iron-storage protein ferritin, which sequesters beryllium by binding it and preventing it from interacting with other enzymes. Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. Copper-induced emesis results from stimulation of the vagus nerve. (L277, T49, A174, L280, L25, A37, A91)</mechanism-of-toxicity>
  <metabolism>Beryllium is absorbed mainly through the lungs, where it enters the bloodstream and is transported throughout the body by binding to prealbumins and gamma-globulins. Beryllium accumulates in lung tissue and the skeleton. It is excreted mainly in the urine. Copper is mainly absorbed through the gastrointestinal tract, but it can also be inhalated and absorbed dermally. It passes through the basolateral membrane, possibly via regulatory copper transporters, and is transported to the liver and kidney bound to serum albumin. The liver is the critical organ for copper homoeostasis. In the liver and other tissues, copper is stored bound to metallothionein, amino acids, and in association with copper-dependent enzymes, then partitioned for excretion through the bile or incorporation into intra- and extracellular proteins. The transport of copper to the peripheral tissues is accomplished through the plasma attached to serum albumin, ceruloplasmin or low-molecular-weight complexes. Copper may induce the production of metallothionein and ceruloplasmin. The membrane-bound copper transporting adenosine triphosphatase (Cu-ATPase) transports copper ions into and out of cells. Physiologically normal levels of copper in the body are held constant by alterations in the rate and amount of copper absorption, compartmental distribution, and excretion. (L277, L279, L25)</metabolism>
  <toxicity nil="true"/>
  <lethaldose>10 to 20 grams for an adult human (copper salts). (T17)</lethaldose>
  <carcinogenicity>1, carcinogenic to humans. (L135)</carcinogenicity>
  <use-source>Beryllium copper is used in springs, load cells, batteries, electrical connectors, tools and intruments. (L26)</use-source>
  <min-risk-level>Chronic Oral: 0.002 mg/kg/day (Beryllium) (L134)
Acute Oral: 0.01 mg/kg/day (Copper) (L134) 
Intermediate Oral: 0.01 mg/kg/day (Copper) (L134)</min-risk-level>
  <health-effects>Acute inhalation of a high level of beryllium can result in a pneumonia-like condition called acute beryllium disease. Chronic inhalation of beryllium can cause an inflammatory reaction in the respiratory system called chronic beryllium disease. Chronic beryllium disease may result in anorexia and weight loss, as well as right side heart enlargement and heart disease in advanced cases. Chronic exposure can also increase the risk of lung cancer. Skin contact with beryllium results in contact dermatitus. People must absorb small amounts of copper every day because copper is essential for good health, however, high levels of copper can be harmful. Very-high doses of copper can cause damage to your liver and kidneys, and can even cause death. Copper may induce allergic responses in sensitive individuals. (L278, L279, L24, L25)</health-effects>
  <symptoms>Chronic beryllium disease causes fatigue, weakness, difficulty breathing, and a persistent dry cough. Breathing high levels of copper can cause irritation of the nose and throat. Ingesting high levels of copper can cause nausea, vomiting, diarrhea, headache, dizziness, and respiratory difficulty. (L278, L279, L24, L25)</symptoms>
  <treatment>Chronic beryllium disease is treated with immunosuppressive medicines, usually of the glucocorticoid class. (L24)</treatment>
  <created-at type="dateTime">2009-03-21T00:59:05Z</created-at>
  <updated-at type="dateTime">2014-12-24T20:22:28Z</updated-at>
  <interacting-proteins>Transthyretin (P02766) Ferritin light chain (P02792) Ferritin heavy chain (P02794) Ferritin, mitochondrial (Q8N4E7) Ferritin heavy polypeptide-like 17 (Q9BXU8) Putative ferritin heavy polypeptide-like 19 (P0C7X4)High affinity copper uptake protein 1 (O15431) Probable low affinity copper uptake protein 2 (O15432) Serum albumin (P02768) Ceruloplasmin (P00450) Copper-transporting ATPase 1 (Q04656) Copper-transporting ATPase 2 (P35670) Copper transport protein ATOX1 (O00244) Copper chaperone for superoxide dismutase (O14618) Cytochrome c oxidase copper chaperone (Q14061) Metallothionein-2 (P02795) Metallothionein-1G (P13640) Metallothionein-1H (P80294) Metallothionein-3 (P25713) Metallothionein-1F (P04733) Metallothionein-1E (P04732) Metallothionein-1X (P80297) Metallothionein-1A (P04731) Metallothionein-1B (P07438) Metallothionein-1M (Q8N339) Metallothionein-4 (P47944) Metallothionein-1L (Q93083)(L25, L277, A176)</interacting-proteins>
  <wikipedia nil="true"/>
  <uniprot-id nil="true"/>
  <kegg-compound-id></kegg-compound-id>
  <omim-id></omim-id>
  <chebi-id></chebi-id>
  <biocyc-id></biocyc-id>
  <ctd-id nil="true"/>
  <stitch-id>Beryllium copper</stitch-id>
  <drugbank-id nil="true"/>
  <pdb-id nil="true"/>
  <actor-id nil="true"/>
  <organism nil="true"/>
  <export type="boolean">true</export>
  <metabolizing-proteins nil="true"/>
  <transporting-proteins>Transthyretin (P02766) 
Ferritin light chain (P02792) 
Ferritin heavy chain (P02794) 
Ferritin, mitochondrial (Q8N4E7) 
Ferritin heavy polypeptide-like 17 (Q9BXU8) 
Putative ferritin heavy polypeptide-like 19 (P0C7X4)
High affinity copper uptake protein 1 (O15431) 
Probable low affinity copper uptake protein 2 (O15432) 
Serum albumin (P02768) 
Ceruloplasmin (P00450) 
Copper-transporting ATPase 1 (Q04656) 
Copper-transporting ATPase 2 (P35670) 
Copper transport protein ATOX1 (O00244) 
Copper chaperone for superoxide dismutase (O14618) 
Cytochrome c oxidase copper chaperone (Q14061) 
Metallothionein-2 (P02795) 
Metallothionein-1G (P13640) 
Metallothionein-1H (P80294) 
Metallothionein-3 (P25713) 
Metallothionein-1F (P04733) 
Metallothionein-1E (P04732) 
Metallothionein-1X (P80297) 
Metallothionein-1A (P04731) 
Metallothionein-1B (P07438) 
Metallothionein-1M (Q8N339) 
Metallothionein-4 (P47944) 
Metallothionein-1L (Q93083)
(L25, L277, A176)</transporting-proteins>
  <moldb-smiles>[Be].[Cu]</moldb-smiles>
  <moldb-formula>BeCu</moldb-formula>
  <moldb-inchi>InChI=1S/Be.Cu</moldb-inchi>
  <moldb-inchikey>InChIKey=DMFGNRRURHSENX-UHFFFAOYSA-N</moldb-inchikey>
  <moldb-average-mass type="decimal">72.558</moldb-average-mass>
  <moldb-mono-mass type="decimal">71.941783214</moldb-mono-mass>
  <origin>Exogenous</origin>
  <state>Solid</state>
  <logp nil="true"/>
  <hmdb-id nil="true"/>
  <chembl-id nil="true"/>
  <chemspider-id nil="true"/>
  <structure-image-file-name nil="true"/>
  <structure-image-content-type nil="true"/>
  <structure-image-file-size type="integer" nil="true"/>
  <structure-image-updated-at type="dateTime" nil="true"/>
  <biodb-id nil="true"/>
  <synthesis-reference></synthesis-reference>
  <structure-image-caption nil="true"/>
</compound>
