Abstract
Cholinesterase (EC 3.1.1.8, CHE or BChE) also called butyrylcholinesterase or serum cholinesterase, has evoked the interest of geneticists, biochemists, pharmacologists, and clinicians, particularly hepatologists. Recent molecular biological investigations have thrown light on new facets of this plasma enzyme. Some of them will be reported, and a number of still open questions discussed, preferably under clinical aspects, without claiming comprehensiveness.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Kalow, K. and K. Genest, A method for the detection of atypical forms of human cholinesterase, determination of dibucaine numbers. Can. J. Biochem. 35: 1957; 339–346
Harris, H. and M. Whittaker, Differential inhibition of human serum cholinesterase with fluoride: recognition of two new phenotypes. Nature19I: I961; 496–498
Liddell, J., H. Lehmann and E. Silk, A “silent” pseudocholinesterase gene. Nature 193: 1962; 561–562
Bartels, C.F., F.S. Jensen, O. Lockridge, A.F.L. van der Spek, H.M. Rubinstein, T. Lubrano and B.N. La Du, DNA mutation associated with the human butyrylcholinesterase K-variant and its linkage to the atypical variant mutation and other polymorphic sites. Am. J. Hum. Genet. 50: 1992; 1086–1103
Rubinstein, A.A. Dietz and T. Lubrano, Elk, another quantitative variant at cholinesterase locus 1. J. Med. Genet. 15: 1978; 27–29
Garry, P.J., A.A. Dietz, T. Lubrano, P.C. Ford, K. James and H.M. Rubinstein, J. med. Genet. 13: 1976; 38–42
Whittaker, M. and J.J. Britten, Elh, a new allele at cholinesterase locus 1. Hum. Hered. 37: 1987; 54–58
Schmidt, E., R. Klauke and F.W. Schmidt, Proposed routine method for phenotyping of cholinesterase (CHE) locus El variants with butyrylcholine as substrate at 37°C, Fresenius Z. Anal. Chem. 330: 1988; 364
Lockridge, O. and B. N. La Du, Structure of the human butyrylcholinesterase gene and expression in mammalian cells, in: Cholinesterases, J. Massoulié et al. eds., Am. Chem. Soc. Washington, DC, 1991, 168–171
Arpagaus, M., M. Kott, K.P. Vatsis, C.F. Bartels, B.N. La Du and O. Lockridge, Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry 29: 1990; 124–131
Gaughan, G., H. Park, J. Priddle, I. Craig and S. Craig, Refinement of the localization of human butyrylcholinesterase to chromosome 3g26.1-g26.2 using a PCR-derived probe. Genomics 11: 1991; 455–458
McGuire, M.C., C.P. Nogueira, C.F. Bartels, H. Lightstone, A. Hajra, A.F. van der Spek, O. Lockridge and B.N. La Du, Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. Proc. Nat. Acad. Sci. U.S.A. 86: 1989; 953–957
Nogueira, C.P., C.F. Bartels, M.C. McGuire, S. Adkins, T. Lubrano, H.M. Rubinstein, H. Lightstone, A.F. van der Spek, O. Lockridge and B.N. La Du, Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase. Am. J. Hum. Genet. 51: 1992; 821–828
Jensen, F.S. C.F. Bartels and B.N. La Du, A DNA point mutation associated with the H-variant of human butyrylcholinesterase, in: Cholinesterases, J. Massoulié et al. eds. Am. Chem. Soc. Washington DC, 1991, 189
Whittaker, M. and J.J. Britten, Segregation of the sub(1)(j) gene for plasma cholinesterase in family studies. Hum. Her. 39: 1989; 1–6
Bartels, C.F., K. James, B.N. La Du, DNA mutations associated with the human butyrylcholinesterase J-variant. Am. J. Hum. Genet. 50: 1992; 1104–1114
Evans and J Wardell, On the identification and frequency of the J and K cholinesterase phenotypes in a Caucasian population. J. Med. genet. 21: 1984; 99–102
Bartels, C.F., O. Lockridge and B.N. La Du, DNA coding for the K polymorphism in linkage disequilibrium with atypical human butyrylcholinesterase complicates phenotyping, in: Cholinesterases, J. Massoulié et al. eds.Am. Chem. Soc., Washington, DC, 1991, 191
Szeinberg, A., S. Pipano, M. Assa, J.H. Medalie and H.N. Neufeld, High frequency of atypical pseudocholinesterase gene among Iraqi and Iranian Jews. Clin. Genet. 3: 1972; 123–127
Whittaker, M., Cholinesterase, Karger, Basel, 1986
Arnaud, J., H. Brun, R. Llobera and J. Constans, Serum cholinesterase polymorphism in France: an epidemiological survey of the deficient alleles detected by an automated micro-method. Ann. Hum. Biol. 18: 1991; 1–8
Chautard-Freire-Maia, E.A. S.L. Primo-Parmo, M.A. Canever de Lourenço and L. Culpi, Frequencies of atypical serum cholinesterase among Caucasians and Negroes from Southern Brazil. Hum. Hered. 34: 1984; 388–392
Evans, R.T., A. Walker and K.M. Bowness, Improved accuracy of cholinesterase phenotyping after participation in a proficiency survey. Clin. Chem. 33: 1987; 823–825
Rosalki, S.B., Genetic influences on diagnostic enzymes in plasma. Enzyme 39: 1988; 95–109
Masson, P., A. Chatonnet and O. Lockridge, Evidence for a single butyrylcholinesterase gene in individuals carrying the C5 plasma cholinesterase variant (CHE2). FEBS 262: 1990; 1 15–1 18
Harris, H., D.A. Hopkinson, E.B. Robson and M. Whittaker. Genetical studies on a new variant of serum cholinesterase detected by electrophoresis. Ann. Hum. Genet. 26: 1963; 359–382
Masson, P., Molecular heterogeneity of human plasma cholinesterase, in: Cholinesterases, J. Massoulié et al. eds. Am. Chem. Soc. Washington, DC., 1991, 42–46
Soreq, H., R. Zamir, D. Zevin-Sonkin and H. Zakut, Human cholinesterase genes localized by hybridization to chromosomes 3 and 16. Hum. genet. 77: 1987; 325–328
Marazita, M.L., B.J.B. Keats, M.A. Spence, R.S. Sparkes, L.L. Field, M.C. Sparkes and M. Crist, Mapping studies of the serum cholinesterase-2-locus (CHE2). Hum. Genet. 83: 1989; 139–144
Eiberg, H., L.S. Nielsen, J. Klausen, M. Dahlen, M. Kristensen, M.L. Bisgaard, N. Moller and J. Mohr, Linkage between serum cholinesterase 2 (CHE2) and gamma-crystalline gene cluster (CRYG): assignment to chromosome 2. Clin. Genet. 35: 1989, 313–321
Gueirrero, J.F., S.E. Santos and G.F. Aguiar, Serum cholinesterase polymorphism (CHEZ and CHE2 loci) among several Indian groups from Amazon region of Brazil, and segregation of the C5 variant in families. Gene Geography 3: 1989; I I - 20
Steegmüller, H., On the geographical distribution of pseudocholinesterase variants. Humangenetik 26: 1975; 167–185
Oimomi, M., J. Ohkawa, S. Saeki and S. Baba, A familial study of C5+cholinesterase and its frequency in the normal population. Gastroent. japon. 23: 1988; 680–683
Schmidt, E., F.W. Schmidt, A. Delbrück and E. Henkel, Variants of cholinesterase. Adv. Clin. Enzymol. 2: 1982; 55–66
Lockridge, O., H.W. Eckerson and B. N. La Du, Interchain disulphide bonds and subunit organization in human serum cholinesterase. J. biol. Chem. 254: 1979; 8324–8330
Fishman, J.B. and R.E. Fine, A trans Golgi-derived exocytic coated vesicle can contain both newly synthesized cholinesterase and internalized transferrin. Cell 48: 1987; 157–164
Ostergaard, D., J. Viby-Mogensen, H.K. Hand and L.T. Skovogaard, Half-life of plasma cholinesterase. Acta Anaesthesiol. Scand. 32: 1988; 266–269
Neitlich, H.W., Increased plasma cholinesterase activity and succinylcholine resistance: a genetic variant. J. clin. Invest. 45: 1966; 380–387
Yoshida, A. and A.G. Motulski, A pseudocholinesterase variant (E Cynthiana) associated with elevated plasma enzyme activity. Am. J. Hum. genet. 21: 1969; 486–498
Delbrück, A. and E. Henkel, A rare genetically determined variant of pseudocholinesterase in two German families with high plasma enzyme activity. Eur. J. Biochem. 99: I979; 65–69
Brock, A., Additional electrophoretic components of cholinesterase in plasma: a phenomenon of no importance to the total plasma cholinesterase activity. J. Clin. Chem.Clin. Biochem. 27: 1989; 429–431
Lockridge, O., C.F. Bartels, T.A. Vaughan, C.K. Wong, S.E. Norton and L.L. Johnson, Complete amino acid sequence of human serum cholinesterase. J. biol. Chem. 262: 1987; 549–557
Yamato, K., I. Huang, H. Muensch, A. Yoshida, H.-W. Goedde and D.P. Agarwal, Amino acid sequence of the active site of human pseudocholinesterase. Biochem. Genet. 21: 1983; 135–145
Arpagaus, M., A. Chatonnet, P. Masson, M. Newton, T.A. Vaughan, C.F. Bartels, C.P. Nogueira, B.N. La Du and O. Lockridge, Use of the polymerase chain reaction for homology probing of butyrylcholinesterases from several vertebrates. J. biol. Chem. 266: 1991; 6966–6974
Neville, L.F., A. Gnatt, R. Padan, B. Seidman and H. Soreq, Anionic site interactions in human butyrylcholinesterase disrupted bytwo single point mutations. J. biol. Chem. 265: 1990; 20735–20738
Chatonnet, A. and O. Lockridge, Comparison of butyrylcholinesterase and actylcholinesterase. Biochem. J. 260: 1989; 625–634
Lockridge, O. and B.N. La Du, Comparison of atypical and usual human serum cholinesterase. J. biol. Chem. 253: 1978; 361–366
Augustinsson, K.B., Cholinesterases: a study in comparative enzymology. Acta Physiol. Scand. 15:1948, Suppl. 52; 1–182
Schmidt, E., F.W. Schmidt, Sex differences of plasma cholinesterases in the rat. Enzyme 23: 1978; 52–55
Wright, P.G., V. de Vos, E. Marcus, M. Ganhao and J. Hattingh, Species variation in plasma cholinesterase activity. Comp. Biochem. Physiol. 70: 1981; 289–291
Kutty, K.M., Biochemical functions of cholinesterase. Clin. Biochem. 13: 1980; 239–243
Lockridge, O., Substance P hydrolysis by human serum cholinesterase. J. Neurochem. 39: 1982; 106–110
Myers. C., O. Lockridge, B.N. La Du, Hydrolysis of methylprednisolone acetate by human serum cholinesterase. Drug Metab. Dispos. 10: 1982; 279–280
Rao, R.V., A.S. Balasubramanian, The peptidase activity of human serum butyrylcholinesterase:studies using monoclonal antibodies and characterization of the peptidase.J. prot. chem. 12: 1993; 103–110
Ram, Z., M. Molcho, Y.L. Danon, S. Almong, J. Baniel, A. Karni and J. Shemer, The effect of pyridostigmine on respiratory function in healthy and asthmatic volunteers. Israel J. med. Sci. 27: 1991; 664–668
Gordon, C.J. and L. Fogelson, Relationship between serum cholinesterase activity and the change in body temperature and motor activity in the rat. A dose-response study of diisopropyi iiiuorophosphate. Neurotox. Teratol. 15: 1993; 21–25
Layer, P.G., Expression and possible functions of cholinesterases during chicken neurogenesis, in: Cholinesterases, J. Massoulié et al. eds. Am. Chem. Soc., Washington, DC, 1991. 350–357
Massoulié, J., S. Bon and M. Vigny, The polymorphism of cholinesterase in vertebrates. Neurochem. int. 2: 1980; 161–184
Ehrlich, G., E. Viegas-Péquinot, D. Ginzberg, L. Sindel, H. Soreq and H. Zakut, Mapping the human acetylcholinesterase gene to chromosome 7q22 by fluorescent in situ hybridization coupled with selective PCR amplification from a somatic hybrid cell panel and chromosome-sorted DNA libraries. Genomics 13: 1992; 1192–1197
Getman, D.K., J.H. Eubanks, S. Camp, G.A. Evans and P. Taylor, The human gene encoding acetylcholinesterases located on the long arm of chromosome 7. Am. J. Hum. Genet. 51: 1992; 170–177
Sorensen, K., U. Brodbeck, A.G. Rasmussen and B. Norgaard-Pedersen, Normal human serum contains two forms of acetylcholinesterase. Clin. Chim. Acta 158: 1986; 1–6
Edwards, J.A. and S. Brimijoin, Divergent regulation of acetylcholinesterase and butyrylcholinesterase in tissues of the rat. J. Neurochem. 38: 1982; 1393–1403
Lapidot-Lifson, Y., C.A. Prody, D. Ginzberg, D. Meytes, H. Zakut and H. Soreq, Coamplification of human acetylcholinesterase and butyrylcholinesterase genes in blood cells: correlation with various leukemias and abnormal megakaryocytopoiesis. Proc. Nat. Acad. Sci. U.S.A. 86: 1989; 4715–4719
Soreq, H., Y. Lapidot-Lifson and H. Zakut, A role for cholinesterase in tumorigenesis? Cancer Cells 3: 1991; 511–516
Birkhauser, H. and E.A. Zeller, Cholinesterase und Sexualhormone. Helv.chim.Acta 23: 1940; 1460–1464
Everett, H.W. and C.H. Sawyer, Effects of castration and treatment with sex steroids on synthesis of serum cholinesterase in rat. Endocrinology 39: 1946; 323–343
Illsley, N.P. and C.A. Lamartinière, Endocrine regulation of rat serum cholinesterase activity. Endocrinology 108: 1981; 1737–1743
Lamartinière, C.A.,Growth hormone modulates serum cholinesterase. Endocrinology 118: 1986; 1252 1254
Kambam, J.R., R.J. Naukam, W. Parris, J.J. Franks, S.M. Perry, B.V.R. Sastry and B.E. Smith, Effects of progesterone, estriol, and prostaglandin on pseudocholinesterase activity. Anesthesiology 71:1989; A 883
Sidell, F.R. and A. Kaminskis, Influence of age, sex and oral contraceptives on human blood cholinesterase activity. Clin. Chem. 21: 1975; 1393–1395
Blaauwen, D.H. den, W.A. Poppe and W. Tritschler, Cholinesterase (EC 3.1. 1.8) mit Butyryl-thiocholinjodid als Substrat: Referenzwerte in Abhängigkeit von Alter und Geschlecht unter Berücksichtigung hormoneller Einflüsse und Schwangerschaft. J. Clin. Chem. Clin. Biochem. 21: 1983; 381–386
Lepage, L., Cholinesterase, in: Interpretation of Clinical Laboratory Tests. G. Siest, J. Henny, F. Schiele and D.S. Young, eds. Biochemical Publications, Forster City, Ca, U.S.A., 1985, 209–219
Pritchard, J.A., Plasma cholinesterase activity in normal pregnancy and in eclamptogenic toxemias. Am. J. Obstet. Gynecol. 70: 1955; 1083–1086
Foldes, F.F., T. Arai, H.H. Gentsch and Y. Zarda, The influence of glucocorticoids on plasma cholinesterase. Proc. Soc. exp. Biol. 146: 1974; 918–920
Bradamante, V. and E. Kunec-Vaji“c, Effect ofglucocorticoids on plasma cholinesterase in the rat. Biomed. Biochim. Acta 46: 1987; 439–443
Bradamante, V., E. Kunec-Vaji“c, M. Lisic, I. Dobric and I. Beus, Plasma cholinesterase activity in patients during therapy with dexamethasone or prednisone. Eur. J. clin. Pharmacol. 36: 1989; 253–257
Tiefenbach, B., L. Jordanov and G. Henninghausen, The glucocorticoid-induced inhibition of cholinesterase activity and the importance for drug interactions. Arch. Pharmacol. 345:1992; Suppl. 1, R101
Seto, Y. and T. Shinohara, Structure-activity relationship of reversible cholinesterase inhibitors including paraquat. Arch. Toxicol. 62: 1988; 37–40
Hansen, W.E. and K. Nehammer, Inhibition of cholinesterase by oxmetidine. Gastroenterology 86: 1984; 1107
Buccafusco, J.J. and M.D. Smith, In vivo and in vitro cholinesterase inhibitor property of the antitumor agent caracemide. Res. Comm. Chem. Pathol. Pharmacol. 67: 1990; 219–227
Aden-Abdi, Y., T. Villen, O. Ericsson, L.L. Gustaysson and M.L. Dahl-Puustinen, Metrifonate in healthy volunteers: interrelationship between pharmacokinetic properties, cholinesterase inhibition and side-effects.
Bull. WHO 68: 1990; 731–736
Bang, U., J. Viby-Mogensen and J.E. Wiren, The effect of bambuterol on plasma cholinesterase activity and suxamethonium-induced neuromuscular blockade in subjects heterozygous for abnormal plasma cholinesterase. Acta Anaesthesiol. Scand. 34: 1990; 600–604
Sharma, M. and L.-A. Svensson, Bambuterol, a selective inhibitor of human plasma butyrylcholinesterase, in: Cholinesterases, J. Massoulié et al. eds., Am. Chem. Soc. Washington, DC, U.S.A., 1991, 345
Berman, H.A. and K. Leonard, Interaction of tetrahydroaminoacridine with acetylcholinesterase and butyrylcholinesterase. Mol. Pharmacol. 41: 1992; 412–418
Laine-Cessac, P., A. Turcant, A. Premel-Cabic, J. Boyer and P. Allain, Inhibition of cholinesterases by histamine 2 receptor antagonist drugs. Res. Comm. Chem. Path. Pharm. 79: 1993; 185–193
Kao, Y.J., J. Tellez and D.R. Turner, Dose-dependent effect of metoclopramide on cholinesterases and suxamethonium metabolism. Br. J. Anaesth. 65: 1990; 220–224
Whittaker, M., J.J. Britten, R.J. Wicks, Inhibition of the plasma cholinesterase variants by propranolol. Br. J. Anaesth. 53: 1981; 511–516
Holmes, J.H., P. Kaufer and H. Zwarenstein, Effect of benzodiazepine derivatives on human blood cholinesterase in vitro. Res. Comm. Chem. Path. Pharm. 21: 1978; 367–370
Hoffman, R.S., G.C. Henry, M.A. Howland, R.S. Weisman, L. Weil and L..R. Goldfrank, Association between life-threatening cocaine toxicity and plasma cholinesterase activity. Ann. Emerg. Med. 21: 1992; 247–253
Lander, F., E. Pike, K. Hinke, A. Brock and J.B. Nielsen, Anti-cholinesterase agents uptake during cultivation of greenhouse flowers. Arch. Envir. Contam. Toxicol. 22: 1992; 159–162
Filimore, C.M. and J.E. Lessenger, A cholinesterase testing program for pesticide applicators. J. occup. Med. 35: 1993; 61–70
Wu, Y.Q., J.D. Wang, J.S. Cheng, S.C. Chung and S.Y. Hwang, Occupational risk of decreased plasma cholinesterase among pesticide production workers in Taiwan. Am. J. Industr. Med. 16: 1989; 659–666
Kamal, A.A., N.T. Elgarthy, F. Maklady, M.A. Mostafa and A. Massoud, Serum cholinesterase and liver function among a group of organophosphorus pesticides sprayers in Egypt. J. toxicol. clin. exper. 10: 1990; 427–435
Faustini, A., F. Arpala, P. Pagliarella, F. Forastiere, P. Papini and C.A. Perucci, Monitoraggio delle colinesterasi in lavoratori agricoli e commercianti esposito ad esteri fosforici e carbammati. Med. Lavoro 83: 1992; 135–145
Rama, D.B. and K. Jaga, Pesticide exposure and cholinesterase levels among farm workers in the Republic of South Africa. Sci. Total Envir. 122: 1992; 315–319
Lander, F., A. Brock, E. Pike, K. Hinke, Chronic subclinical intake of dietary anticholinesterase agents during the spraying season. Food Chem. Toxicol. 30: 1992; 37–40
Brock, A. and V. Brock, Plasma cholinesterase activity in a healthy population group with no occupational exposure to known cholinesterase inhibitors: relative influence of some factors related to normal inter-and intra-individual variations. Scand. J. Clin. Lab. Invest. 50: 1990; 401–408
Prody, C.A., P. Dreyfus, R. Zamir, H. Zakut and H. Soreq, De novo amplification within a “silent” human cholinesterase gene in a family subjected to prolonged exposure to organophosphorous insecticides. Proc. Nat. Acad. Sci. US.A. 86: 1989; 690–694
Soreq, H. and H. Zakut, Amplification of butyrylcholinesterase and acetylcholinesterase genes in normal and tumor tissues: putative relationship to organophosphorous poisoning. Pharma. Res. 7: 1990; 1–7
Panteghini, M. and R. Bonora, Evaluation of a new continuous colorimetric method for determination of serum pseudocholinesterase catalytic activity and its application to a centrifugal fast analyser. J. Clin. Chem. Clin. Biochem. 22: 1984; 671–676
Rostron, P. and T. Higgins, Serum pseudocholinesterase and dibucaine numbers as measured with the Technicon RA-1000 analyzer. Clin. Chem. 34: 1988; 1924–1925
Hasselberg, S., L. Mauck and D Nealon, Development of a Kodak Ektachem thin-film assay for serum cholinesterase. Clin. Chem. 35: 1989; 1120
Takeuchi, T., Y. Kabasawa, R. Horikawa and T. Tanimura. Mechanized assay of serum cholinesterase by specific colorimetric detection of released acid. Clin. Chim. Acta 205: 1992; 117–126
Krull, N.B., J. Kropf and A.M. Gressner, Influence of reagent composition of atypical pseudocholinesterase activity measurement: comparison of a manual and an automated method and implications for routine. Eur. J. Clin. Chem. Clin. Biochem. 30: 1992; 545–546
Thomsen, T., H. Kewitz and O. Pleul. Estimation of cholinesterase activity (EC 3.1.1.7; 3.1.1.8) in undiluted plasma and erythrocytes as a tool for measuring in vivo effects of reversible inhibitors. J. Clin. Chem. Clin. Biochem. 26: 1988; 469–475
Vorschlag zum Arzneibuch der DDR, 2. Ausg., Bestimmung der Aktivität der Cholinesterase in Serum. Zbl. Pharm. 119: 1980; 1293–1297
Alcini, D., M. Maroni, A. Colombi, D. Xaiz and V. Foa, Evaluation of a standardized European method for the determination of cholinesterase activity in plasma and erythrocytes. Med. Lavoro 79: 1988; 42–53
Deutsche Gesellschaft far Klinische Chemie, Proposal for standard methods for the determination of enzyme catalytic concentrations in serum and plasma at 37°C, II. Cholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) Eur. J. Clin. Chem. Clin. Biochem. 30: 1992; 163–170
Rama, D.B.K. and M. Deneys, Quality control of red blood cell cholinesterase estimations. South Mr. Med. J. 81: 1992; 530
Whittaker, M., J.W. Jones and J. Braven, Immunological studies of plasma cholinesterase during pregnancy and the puerperium. Clin. Chim. Acta 199: 1991; 223–230
Lepage, L. F. Schiele, R. Gueguen and G. Siest, Total cholinesterase in plasma: Biological variations and reference limits. Clin. Chem. 31: 1985; 546–550
Brock, A., Immunoreactive plasma cholinesterase (EC 3.1.1.8) substance concentration compared with cholinesterase activity concentration and albumin: Inter-and intra-individual variations in a healthy population group. J. Clin. Chem. Clin. Biochem. 28: 1990; 851–856
Pourrat, O., R. Robert, J.P. Neau, P. Deleplanque and D. Alcalay, Crises cholinergiques chez un myasthenique traité par échanges plasmatiques et anticholinesterasiques. Aim. Med. Int. 139: 1988; 51–52
Evans, R.T. and A. Robinson, The combined effects of pregnancy and repeated plasma exchange on serum cholinesterase activity. Acta anaesthesiol. Scand. 28: 1984; 44–46
Schuh, F.T., Pseudocholinesterase activity of human whole blood, bank blood and blood protein solutions. Anaesthesist 24: 1975; 103–106
Huizenga, J.R., K. van der Belt and C.H. Gips, The effect of storage at different temperatures on cholinesterase activity in human serum. J. Clin. Chem. Clin. Biochem. 23: 1985; 283–285
Balland, M., M. Vincent-Viry and J. Henny, Effect of long-term storage on human plasma cholinesterase activity. Clin. Chim. Acta 211: 1992; 129–131
Braun, B.-E., R. Goes, M. Tryba, D. Huppe, H.-D. Kuntz and M. Krieg, Anstieg der CholinesteraseAktivitat bei Patienten mit dekompensierter Leberzirrhose nach Gabe von gerinnungsaktivem Frischplasma (FFP). Lab. med. 15: 1991; 485–489
Lovely, M.J., S.K. Patteson, F.J. Beuerlein and J.T. Chesney, Perioperative blood transfusion may conceal atypical pseudocholinesterase. Anest. Analg. 70: 1990; 326–327
Puche, E., E. Gomez-Valverde, M- Garcia-Morillas, F. Jorde F. Fajardo and J.M. Garcia Gil, Postoperative decline in plasma aspirin-esterase and cholinesterase activity in surgical patients. Acta anaesthesiol. Scand. 37: 1993; 20–22
Burnett, W. and Y. Conen: Liver function after surgery: A study of 50 cases with particular reference to serum cholinesterase. Br. J. Anaesth. 27: 1955; 66–71
Ryan, D.W., Postoperative serum cholinesterase activity following successful renal transplantation. Br. J. Anaesth. 51: 1979; 881–884
Waterlow, J., Liver cholinesterase in malnourished infants. Lancet 1: 1950; 908–909
Barclay, G.P.T., Pseudocholinesterase activity as a guide to prognosis in malnutrition. Am. J. Clin. Path. 59: 1973; 712–716
Venkataraman, B.V., J. Thangam, P.S. Shetty and P.M. Stephen, Cholinesterase in starvation. Ind. J. Physiol. Pharmacol. 26: 1982; 137–140
Foldes, F.F., Enzymes in Anesthesiology. Springer, New York, 1978, 107–131
Jenike, M.A., M. Albert, L. Baer and J. Gunther, Oral physostigmine treatment for primary dementia: a double-blind placebo-controlled inpatient trial. J. Geriat. Psychiat. Neurol. 3: 1990; 13–16
Volger, B.W., Alternatives in the treatment of memory loss in patients with Alzheimer’s disease. Clin. Pharm. 10: 1991; 447–456
Davis, K.L., L.J. Thai, E.R. Gamzu, C.S. Davis, R.F. Woolson, S.I. Gracon, D.A. Drachman, L.S. Schneider, P.J. Whitehouse, T.m. Hoover and the Tacrine Collaborative Study Group, A double-blind, placebo-controlled multicenter study of tacrine for Alzheimer’s disease. New Engl. J. Med. 327: 1992; 1253–1259
Mesulam, M.M. and C Goula, Shifting patterns of cortical cholinesterase in Alzheimer’s disease: implications for treatment, diagnosis, and pathogenesis. Adv. Neurol. 51: 1990; 235–240
Arendt, T., M.K. Brueckner, M. Lange and V. Bigl, Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer’s disease resemble embryonic development: a study of molecular forms. Neurochem. Int. 21: 1992; 381–396
Wright, C.I., C. Guela and M.M. Mesulam, Protease inhibitors and indoleamines selectively inhibit cholinesterases in the histopathologic structures of Alzheimer disease. Proc. Nat. Acad. Sci. U.S.A. 90: 1993; 683–686
Atack, J.R., C. May, J.A. Kaye, A.D. Kay and S.I. Rapoport, Cerebrospinal fluid cholinesterases in aging and in dementia of the Alzheimer type. Ann. Neurol. 23: 1988; 161–167
Sirvioe, J. and P.J. Riekkinen, Brain and cerebrospinal fluid cholinesterases in Alzheimer’s disease, Parkinson’s disease and aging A critical review of clinical and experimental studies. J. Neur.Transmiss. 4: 1992; 337–358
Bonham, J.R., G. Dale, D.J. Scott and J. Waggett, Diagnostic value of acetylcholinesterase/butyrylcholinesterase ratio in Hirschsprung’s disease. Am. J. Clin. Path. 90: 1988; 520–521
Rasmussen Loft, A.G., Determination of amniotic fluid acetylcholinesterase activity in the antenatal diagnosis of foetal malformations: The first ten years. J. Clin. Chem. Clin. Biochem. 28: 1990; 893–911
Kutty, K.M., R. Jain, S.N. Huang and K. Kean, Serum pseudocholinesterase:high density lipoprotein cholesterol ratio as an index of risk for cardiovascular disease. Clin. Chim. Acta 115: 1981; 55–61
enschläger, G., M. Schrappe-Bächer, M. Steffen, B. Bürger and B. Allolio, Erhebung des Ernährungszustandes–ein Bestandteil der klinischen Routine-Diagnostik: Cholinesterase-Aktivität als Ernährungsindikator. Klirr. Wschr. 67: 1989; 1101–1107
Novacek, G., H. Vogelsang, B. Schmidt and H. Lochs, Are single measurements of pseudocholinesterase and albumin markers for inflammatory activity or nutritional status in Crohn’s disease? Wien. Klirr. Wschr. 105: 1993; 111–115
Wellmann, W., R. Kubale, T.G.A. Nyman, J. Oestmann, E. Schmidt and F.W. Schmidt, Enzyme screening in inflammatory bowel disease: A preliminary report, in: Progress in Clinical Enzymology. D.M. Goldberg, M. Werner, eds. Masson, New York, 1980, 145–149
Tromm, A., D. Huppe, I. Thau, U. Schwegler, H.D. Kuntz, M. Krieg and B. May, Die Serumcholinesterase als Aktivitätsparameter bei chronisch entzündlichen Darmerkrankungen. Z. Gastroenterol. 30: 1992; 449–453
Schmidt, E. and F.W. Schmidt, Mitreaktionen der Leber bei systemischen Erkrankungen unter besonderer Berücksichtigung der Infektionen, in: Die Leber bei extrahepatischen Erkrankungen und Stoffwechselleiden. W. Tittor, G. Schwalbach, eds. Demeter, Gräfelfing 1984, 41–76
Guder, W.G., Anwendung von Bewertungsverfahren: Modell Lebererkrankungen, in: Validität klinisch-chemischer Befunde, H. Lang, W. Rick, H. Büttner, eds., Springer, Berlin, 1980, 84–91
Schmidt, E. and F.W. Schmidt, Strategie-Probleme bei der Diagnostik von Lebererkrankungen, in: Strategien für den Einsatz klinisch-chemischer Untersuchungen, H. Lang, W. Rick, H. Büttner, eds. Springer, Berlin, 1982, 152–169
Lautz, H.U., E. Schmidt, F.W. Schmidt and M. Barthels, Korrelationen zwischen Einschränkung der Sekretionsleistung der Leber und dem Austritt von Zellenzymen. Z. Gastroenterol. 171979;99–105
Schmidt, E. and F.W. Schmidt, Enzyme diagnosis in diseases of the liver and the biliary system. Adv. Clin. Enzymol. 1: 1979; 239–292
Tinè, F. and L. Pagliaro, Cirrhosis and its recognition in asymptomatic subjects with aminotransferase elevation. Hepatology 11: 1990; 516–517
Nomura, F., K. Olmishi, H. Koen, Y. Hiyama, T. Nakayama, Y. Itoh, K. Shirai, Y. Saitoh and K. Okuda, Serum cholinesterase in patients with fatty liver. J. Clin. Gastroenterol. 8: 1986; 599–602
Hada, T., T. Ohue, H. Imanishi, H. Nakaoka, M. Fujikura, T. Yamamoto, Y. Amuro and K. Higashino, Alteration of serum cholinesterase isozyme in patients with liver cirrhosis. Clin. Chim. Acta 178: 1988; 111–112
Schmidt, E. and F.W. Schmidt, Enzyme patterns in liver failure, in: Artificial Liver Support. G. Brunner, F.W. Schmidt, eds. Springer, Berlin, 1987, 8–17
Burghardt, M., A. Henze, U. Russmann, J. Lobers, E. Schmidt, F.W. Schmidt, On the prognosis of liver cirrhosis, in: Experimental and Clinical Hepatology. C.E. Broelsch, O. Zelder, eds. MTP Press, Lancaster, 1986, 80–88
Schmidt, E., F.W. Schmidt S. Ohlendorf, R. Raupach, T. Wittig, C.E. Broelsch and R. Pichlmayr, Enzyme patterns in serum after liver transplantation, in: A. Burlina, L. Galzigna, eds. Clinical Enzymology Symposia 5. Piccin, Padua, 1986, 143–156
Irrgang, B., N. Adam, A. Schwab and F. Przybylski, Computer-supported decision making in liver diagnosis based on a graphical presentation of laboratory data. J. Clin. Chem. Clin. Biochem. 28: 1990; 733
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer Science+Business Media New York
About this chapter
Cite this chapter
Ellen, Schmidt, F.W. (1994). Serum Cholinesterase: Genetics, Enzymology, Diagnostic Use and the Association with Clinical Disorders. In: Mackness, M.I., Clerc, M. (eds) Esterases, Lipases, and Phospholipases. NATO ASI Series, vol 266. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0993-0_2
Download citation
DOI: https://doi.org/10.1007/978-1-4899-0993-0_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-0995-4
Online ISBN: 978-1-4899-0993-0
eBook Packages: Springer Book Archive