Butyrylcholinesterase

Butyrylcholinesterase, also known as BCHE, is a human gene. Butyrylcholinesterase is also called serum cholinesterase. It is very similar to the neuronal acetylcholinesterase. Butyrylcholine is a synthetic compound and does not occur in the body naturally. It is used as a tool to distinguish between acetyl- and butyrylcholinesterase.

PBB_Summary
section_title =
summary_text = Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage. [cite web | title = Entrez Gene: BCHE butyrylcholinesterase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=590| accessdate = ]

Medical Applications

Butyrylcholinesterase is believed to play a role in the body's ability to metabolize the drug cocaine. In 2008 an experimental new drug was discovered for the potential treatment of cocaine abuse and overdose based on the BChE structure. It was shown to remove cocaine from the body 2000 times as fast as the natural form of BChE. Studies in rats have shown that the drug prevented convulsions and death when administered cocaine overdoses. [http://www.sciencedaily.com/releases/2008/09/080915164427.htm]

ee also

Cholinesterase enzyme

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lockridge O |title=Structure of human serum cholinesterase. |journal=Bioessays |volume=9 |issue= 4 |pages= 125–8 |year= 1989 |pmid= 3067729 |doi= 10.1002/bies.950090406
*cite journal | author=Allderdice PW, Gardner HA, Galutira D, "et al." |title=The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26. |journal=Genomics |volume=11 |issue= 2 |pages= 452–4 |year= 1992 |pmid= 1769657 |doi=
*cite journal | author=Gaughan G, Park H, Priddle J, "et al." |title=Refinement of the localization of human butyrylcholinesterase to chromosome 3q26.1-q26.2 using a PCR-derived probe. |journal=Genomics |volume=11 |issue= 2 |pages= 455–8 |year= 1992 |pmid= 1769658 |doi=
*cite journal | author=Arpagaus M, Kott M, Vatsis KP, "et al." |title=Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. |journal=Biochemistry |volume=29 |issue= 1 |pages= 124–31 |year= 1990 |pmid= 2322535 |doi=
*cite journal | author=Nogueira CP, McGuire MC, Graeser C, "et al." |title=Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117 (GGT----GGAG). |journal=Am. J. Hum. Genet. |volume=46 |issue= 5 |pages= 934–42 |year= 1990 |pmid= 2339692 |doi=
*cite journal | author=McGuire MC, Nogueira CP, Bartels CF, "et al." |title=Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 953–7 |year= 1989 |pmid= 2915989 |doi=
*cite journal | author=Prody CA, Zevin-Sonkin D, Gnatt A, "et al." |title=Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 11 |pages= 3555–9 |year= 1987 |pmid= 3035536 |doi=
*cite journal | author=Lockridge O, Adkins S, La Du BN |title=Location of disulfide bonds within the sequence of human serum cholinesterase. |journal=J. Biol. Chem. |volume=262 |issue= 27 |pages= 12945–52 |year= 1987 |pmid= 3115973 |doi=
*cite journal | author=McTiernan C, Adkins S, Chatonnet A, "et al." |title=Brain cDNA clone for human cholinesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 19 |pages= 6682–6 |year= 1987 |pmid= 3477799 |doi=
*cite journal | author=Lockridge O, Bartels CF, Vaughan TA, "et al." |title=Complete amino acid sequence of human serum cholinesterase. |journal=J. Biol. Chem. |volume=262 |issue= 2 |pages= 549–57 |year= 1987 |pmid= 3542989 |doi=
*cite journal | author=Jbilo O, Toutant JP, Vatsis KP, "et al." |title=Promoter and transcription start site of human and rabbit butyrylcholinesterase genes. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20829–37 |year= 1994 |pmid= 8063698 |doi=
*cite journal | author=Mattes C, Bradley R, Slaughter E, Browne S |title=Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters. |journal=Life Sci. |volume=58 |issue= 13 |pages= PL257–61 |year= 1996 |pmid= 8622553 |doi=
*cite journal | author=Iida S, Kinoshita M, Fujii H, "et al." |title=Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. |journal=Hum. Mutat. |volume=6 |issue= 4 |pages= 349–51 |year= 1996 |pmid= 8680411 |doi= 10.1002/humu.1380060411
*cite journal | author=Kamendulis LM, Brzezinski MR, Pindel EV, "et al." |title=Metabolism of cocaine and heroin is catalyzed by the same human liver carboxylesterases. |journal=J. Pharmacol. Exp. Ther. |volume=279 |issue= 2 |pages= 713–7 |year= 1996 |pmid= 8930175 |doi=
*cite journal | author=Hidaka K, Iuchi I, Tomita M, "et al." |title=Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency. |journal=Ann. Hum. Genet. |volume=61 |issue= Pt 6 |pages= 491–6 |year= 1998 |pmid= 9543549 |doi= 10.1046/j.1469-1809.1997.6160491.x
*cite journal | author=Browne SP, Slaughter EA, Couch RA, "et al." |title=The influence of plasma butyrylcholinesterase concentration on the in vitro hydrolysis of cocaine in human plasma. |journal=Biopharmaceutics & drug disposition |volume=19 |issue= 5 |pages= 309–14 |year= 1998 |pmid= 9673783 |doi=
*cite journal | author=Altamirano CV, Lockridge O |title=Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers. |journal=Biochemistry |volume=38 |issue= 40 |pages= 13414–22 |year= 1999 |pmid= 10529218 |doi=
*cite journal | author=Darvesh S, Kumar R, Roberts S, "et al." |title=Butyrylcholinesterase-Mediated enhancement of the enzymatic activity of trypsin. |journal=Cell. Mol. Neurobiol. |volume=21 |issue= 3 |pages= 285–96 |year= 2002 |pmid= 11569538 |doi=
*cite journal | author=Barta C, Sasvari-Szekely M, Devai A, "et al." |title=Analysis of mutations in the plasma cholinesterase gene of patients with a history of prolonged neuromuscular block during anesthesia. |journal=Mol. Genet. Metab. |volume=74 |issue= 4 |pages= 484–8 |year= 2002 |pmid= 11749053 |doi= 10.1006/mgme.2001.3251

External links

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