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Proposed nomenclature for human butyrylcholinesterase genetic variants identified by DNA sequencing

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Summary

  1. 1.

    New information identifying nucleotide alterations of human butyrylcholinesterase allows the use of more specific nomenclature for the variants commonly known as atypical, fluoride, silent, and K variant.

  2. 2.

    In addition to suggesting a system of trivial names and abbreviations, we provide a list of formal names that follow the guidelines of the Committee for Human Gene Nomenclature.

  3. 3.

    It is suggested that formal names be included in publications whenever possible.

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References

  • Arpagaus, M., Kott, M., Vatsis, K. P., Bartels, C. F., La Du, B. N., and Lockridge, O. (1990). Structure of the gene for human butyrylcholinesterase. Evidence for a single copy.Biochemistry 29124–131.

    Google Scholar 

  • Bartels, C. F., van der Spek, A., Lockridge, O., and La Du, B. N. (1989). A polymorphism (K variant?) of human serum cholinesterase at nucleotide 1615, coding for Ala/Thr 539.FASEB J. 3:A741.

  • Delbruck, A., and Henkel, E. (1979). A rare genetically determined variant of pseudocholinesterase in two German families with high plasma enzyme activity.Eur. J. Biochem. 9965–69.

    Google Scholar 

  • Eckerson, H. W., Oseroff, A., Lockridge, O., and La Du, B. N. (1983). Immunological comparison of the usual and atypical human serum cholinesterase phenotypes.Biochem. Genet. 2193–108.

    Google Scholar 

  • Eiberg, H., Nielsen, L. S., Klausen, J., Dahlen, M., Kristensen, M., Bisgaard, M. L., Moller, N., and Mohr, J. (1989). Linkage between serum cholinesterase 2 (CHE2) andγ-crystallin gene cluster (CRYG): Assignment to chromosome 2.Clin Genet. 35313–321.

    Google Scholar 

  • Evans, R. T., and Wardell, J. (1984). On the identification and frequency of the J and K cholinesterase phenotypes in a Caucasian population.J. Med. Genet. 2199–102.

    Google Scholar 

  • Garry, P. J., Dietz, A. A., Lubrano, T., Ford, P. C., James, K., and Rubinstein, H. M. (1976). New allele at cholinesterase locus 1.J. Med Genet. 13 38–42.

    Google Scholar 

  • Harris, H., and Whittaker, M. (1961). Differential inhibition of human serum cholinesterase with fluoride. Recognition of two new phenotypes.Nature Lond. 191496–498.

    Google Scholar 

  • Harris, H., Robson, E. B., Glen-Bott, A. M., and Thornton, J. A. (1963). Evidence for non-allelism between genes affecting human serum cholinesterase.Nature 2001185–1187.

    Google Scholar 

  • Kalow, W. (1962).Pharmacogenetics, Heredity and the Response to Drugs. W. B. Saunders, Philadelphia, pp. 69–93.

    Google Scholar 

  • Kalow, W., and Genest, K. (1957). A method for the detection of atypical forms of human cholinesterase; Determination of dibucaine numbers.Can. J. Biochem. Physiol. 35339–346.

    Google Scholar 

  • Kalow, W., and Gunn, D. R. (1959). Some statistical data on atypical cholinesterase of human serum.Ann. Hum. Genet. 23239–250.

    Google Scholar 

  • Kalow, W., and Lindsay, H. A. (1955). A comparison of optical and manometric methods for the assay of human serum cholinesterase.Can. J. Biochem. Physiol. 33568–574.

    Google Scholar 

  • Kalow, W., and Staron, N. (1957). On distribution and inheritance of atypical forms of human serum cholinesterase, as indicated by dibucaine numbers.Can. J. Biochem. Physiol. 351305–1320.

    Google Scholar 

  • Krause, A., Lane, A. B., and Jenkins, T. (1988). A new high activity plasma cholinesterase variant.J. Med. Genet. 25677–681.

    Google Scholar 

  • La Du, B. N., Bartels, C. F., Nogueira, C. P., Hajra, A., Lightstone, H., van der Spek, A., and Lockridge, O. (1990). Phenotypic and molecular biological analysis of human serum cholinesterase variants.Clin. Biochem. 23423–431.

    Google Scholar 

  • Liddell, J., Lehmann, H., and Silk, E. (1962). A “silent” pseudocholinesterase gene.Nature (Lond.)193561–562.

    Google Scholar 

  • Lockridge, O. (1990). Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine.Pharmacol. Ther. 4735–60.

    Google Scholar 

  • Lockridge, O., and La Du, B. N. (1978). Comparison of atypical and usual human serum cholinesterase: Purification, number of active sites, substrate affinity, and turnover number.J. Biol. Chem. 253361–366.

    Google Scholar 

  • Lovrien, E. W., Magenis, R. E., Rivas, M. L., Lamvik, N., Rowe, S., Wood, J., and Hemmerling, J. (1978). Serum cholinesterase (E2) linkage analysis: Possible evidence for localization to chromosome 16.Cytogenet. Cell Genet. 22324–325.

    Google Scholar 

  • Marazita, M. L., Keats, B. J. B., Spence, M. A., Sparkes, R. S., Field, L. L., Sparkes, M. C., and Crist, M. (1989). Mapping studies of the serum cholinesterase-2 locus (CHE2).Hum. Genet. 83139–144.

    Google Scholar 

  • Masson, P. (1989). A naturally-occurring molecular form of human plasma cholinesterase is an albumin conjugate.Biochim. Biophys. Acta 988258–266.

    Google Scholar 

  • Masson, P., Chatonnet, A., and Lockridge, O. (1990). Evidence for a single butyrylcholinesterase gene in individuals carrying the C5 plasma cholinesterase variant (CHE2).FEBS Lett. 262115–118.

    Google Scholar 

  • McGuire, M. C., Nogueira, C. P., Bartels, C. F., Lightstone, H., Hajra, A., van der Spek, A. F. L., Lockridge, O., and La Du, B. N. (1989). Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase.Proc. Natl. Acad. Sci. USA 86953–957.

    Google Scholar 

  • Neitlich, H. W. (1966). Increased plasma cholinesterase activity and succinylcholine resistance: A genetic variant.J. Clin. Invest. 45380–387.

    Google Scholar 

  • Nogueira, C. P., McGuire, M. C., Graeser, C., Bartels, C. F., Arpagaus, M., van der Spek, A. F. L., Lightstone, H., Lockridge, O., and La Du, B. N. (1990). Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117, (GGT→GGAG).Am. J. Hum. Genet. 46934–942.

    Google Scholar 

  • Olson, M., Hood, L., Cantor, C., and Botstein, D. (1989). A common language for physical mapping of the human genome.Science 2451434–1435.

    Google Scholar 

  • Robson, E. B., and Harris, H. (1966). Further data on the incidence and genetics of the serum cholinesterase phenotype C5+.Ann. Hum. Genet. Lond. 29403–408.

    Google Scholar 

  • Robson, E. B., Sutherland, I., and Harris, H. (1966). Evidence for linkage between the transferrin locus (Tf) and the serum cholinesterase locus (El) in man.Ann. Hum. Genet. Lond. 29325–332.

    Google Scholar 

  • Rubinstein, H. M., Dietz, A. A., Hodges, L. K., Lubrano, T., and Czebotar, V. (1970). Silent cholinesterase gene: Variations in the properties of serum enzyme in apparent homozygotes.J. Clin. Invest. 49479–486.

    Google Scholar 

  • Rubinstein, H. M., Dietz, A. A., and Lubrano, T. (1978). E k1 , another quantitative variant at cholinesterase locus 1.J. Med. Genet. 1527–29.

    Google Scholar 

  • Savarese, J. J., Ali, H. H., Basta, S. J., Embree, P. B., Scott, R. P. F., Sunder, N., Weakly, J. N., Wastila, W. B., and El-Sayad, H. A. (1988). The clinical neuromuscular pharmacology of mivacurium chloride (BW B1090U). A short-acting nondepolarizing ester neuromuscular blocking drug.Anesthesiology 68723–732.

    Google Scholar 

  • Scott, E. M., and Powers, R. F. (1974). Properties of the C5 variant form of human serum cholineserase.Am. J. Hum. Genet. 26189–194.

    Google Scholar 

  • Shows, T. B., McAlpine, P. J., Boucheix, C., Collins, F. S., Conneally, P. M., Frezal, J., Gershowitz, H., Goodfellow, P. N., Hall, J. G., Issitt, P., Jones, C. A., Knowles, B. B., Lewis, M., McKusick, V. A., Meisler, M., Morton, N. E., Rubinstein, P., Schanfield, M. S., Schmickel, R. D., Skolnick, M. H., Spence, M. A., Sutherland, G. R., Traver, M., Van Cong, N., and Willard, H. F., (1987). Guidelines for human gene nomenclature. An International System for Human Gene Nomenclature (ISGN, 1987).Cytogenet. Cell Genet. 4611–28.

    Google Scholar 

  • Simpson, N. E., and Elliott, C. R. (1981). Cholinesterase Newfoundland: A new succinylcholine-sensitive variant of cholinesterase at locu 1.Am. J. Hum. Genet. 33366–374.

    Google Scholar 

  • Soreq, H., Zamir, R., Zevin-Sonkin, D., and Zakut, H. (1987). Human cholinesterase genes localized by hybridization to chromosomes 3 and 16.Hum. Genet. 77325–328.

    Google Scholar 

  • Sparkes, R. S., Field, L. L., Sparkes, M. C., Crist, M., Spence, M. A., James, K., and Garry, P. J. (1984). Genetic linkage studies of transferrin, pseudocholinesterase, and chromosome 1 loci.Hum. Hered. 3496–100.

    Google Scholar 

  • Tunek, A., and Svensson, L. A. (1988). Bambuterol, a carbamate ester prodrug of terbutaline, as inhibitor of cholinesterases in human blood.Drug Metab. Dispos. 16759–764.

    Google Scholar 

  • Viby-Mogensen, J. (1983). Cholinesterase and succinylcholine.Danish Med. Bull. 30129–150.

    Google Scholar 

  • Whittaker, M. (1986).Cholinesterase. Monograph in Human Genetics, Vol. 11 Karger, Basel, pp. 1–134.

    Google Scholar 

  • Whittaker, M., and Britten, J. J. (1985). Plasma cholinesterase variants: Family studies of the E k1 gene.Hum. Hered. 35364–368.

    Google Scholar 

  • Whittaker, M., and Britten, J. J. (1987). E h1 , a new allele at cholinesterase locus 1.Hum. Hered. 3754–58.

    Google Scholar 

  • Whittaker, M., and Britten, J. J. (1988). Recognition of two new phenotypes segregating the E k1 allele from plasma cholinesterase.Hum. Hered. 38233–239.

    Google Scholar 

  • Yang, F., Lum, J. B., McGill, J. R., Moore, C. M., Naylor, S. L., Van Bragt, P. H., Baldwin, W. D., and Bowman, B. H. (1984). Human transferrin: cDNA characterization and chromosomal localization.Proc. Natl. Acad. Sci. USA 812752–2756.

    Google Scholar 

  • Yoshida, A., and Motulsky, A. G. (1969). A Pseudocholinesterase variant (E Cynthiana) associated with elevated plasma enzyme activity.Am. J. Hum. Genet. 21486–498.

    Google Scholar 

  • Zakut, H., Zamir, R., Sindel, L., and Soreq, H. (1989). Gene mapping on chorionic villi chromosomes by hybridization in situ: Localization of cholinesterase cDNA binding sites to chromosomes 3q21, 3a26-ter and 16q21.Hum. Reprod. 4941–946.

    Google Scholar 

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Author notes

  1. Martine Arpagaus

    Present address: INRA, Génétique Moléculaire des Invertébrés, 123 Blvd. Francis Meilland, 06606, Antibes Cedex, France

  2. Oksana Lockridge

    Present address: Eppley Institute, University of Nebraska Medical Center, 600 South 42nd Street, 68198-6805, Omaha, Nebraska, USA

Authors and Affiliations

  1. Pharmacology Department, Medical Science I, M6322, University of Michigan Medical School, 48109-0626, Ann Arbor, Michigan, USA

    Bert N. La Du, Cynthia F. Bartels, Christine P. Nogueira, Martine Arpagaus & Oksana Lockridge

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  1. Bert N. La Du
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  2. Cynthia F. Bartels
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  3. Christine P. Nogueira
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  4. Martine Arpagaus
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  5. Oksana Lockridge
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La Du, B.N., Bartels, C.F., Nogueira, C.P. et al. Proposed nomenclature for human butyrylcholinesterase genetic variants identified by DNA sequencing. Cell Mol Neurobiol 11, 79–89 (1991). https://doi.org/10.1007/BF00712801

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  • DOI: https://doi.org/10.1007/BF00712801

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