Human liver and plasma aspirin esterase

Williams, Faith M.; Mutch, Elaine; Nicholson, E.; Wynne, Hilary; Wright, Peter V.; Lambert, Denis; Rawlins, M. D.

doi:10.1111/j.2042-7158.1989.tb06487.x

Cited by 37 publications

(25 citation statements)

References 13 publications

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“…The variability in GB hydrolase activity of human plasma was smaller than those in butyrylcholinesterase activity (2.0-fold) (Table 1), aspirin hydrolase activity (2.2-fold), 14) and fluazifop-butyl hydrolase activity (approximately 4-fold), 11) although the variation in plasma GB hydrolase activity was larger than that in plasma nafamostat hydrolase activity (1.2-fold). 10) Interindividual difference in erythrocyte activity of the GB hydrolysis was slightly smaller than those in acetylcholinesterase activity (1.3-fold) ( Table 1) and nafamostat hydrolase activity (1.4-fold) reported previously.…”

Section: Discussionmentioning

confidence: 93%

Butyrylcholinesterase and Erythrocyte Sulfhydryl-dependent Enzyme Hydrolyze Gabexate in Human Blood

Yamaori

Kushihara

Fujiyama

et al. 2007

JOURNAL OF HEALTH SCIENCE

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Gabexate (GB), a serine protease inhibitor that is widely used for the treatment of acute pancreatitis and disseminated intravascular coagulation, has been reported to be partly hydrolyzed by human serum albumin. However, other enzymes responsible for GB hydrolysis in human blood remain unclear. In this study, we examined in vitro metabolism of GB with human blood samples. The hydrolytic activities of the plasma and erythrocytes at 100 µM of GB were 167 ± 26 and 151 ± 9 nmol/min/ml blood fraction (mean ± S.D., n = 8), respectively. Kinetic analysis indicated that V max and K m values were 1.75 µmol/min/ml blood fraction and 529 µM for the plasma and 10.6 µmol/min/ml blood fraction and 7360 µM for the erythrocytes, respectively. The activity of human plasma was inhibited by ethopropazine, a butyrylcholinesterase inhibitor (27% inhibition at 100 µM). Furthermore, the plasma activity was inhibited by 5,5 -dithiobis(2-nitrobenzoic acid) (DTNB) (40% inhibition at 5000 µM), suggesting the involvement of albumin in the plasma GB hydrolysis. The erythrocyte activity was also decreased by DTNB (56% inhibition at 5000 µM), implying that this activity was dependent on the presence of sulfhydryl group(s), while little or no inhibition of the activity was seen with phenylmethylsulfonyl fluoride, diisopropyl fluorophosphate, and BW284C51. Butyrylcholinesterase from human serum showed GB hydrolytic activity with V max of 363 nmol/min/mg protein and K m of 263 µM. These results suggest that, in addition to albumin, butyrylcholinesterase and erythrocyte sulfhydryl-dependent enzyme are responsible for GB hydrolysis in human blood.

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Section: Discussionmentioning

confidence: 93%

Butyrylcholinesterase and Erythrocyte Sulfhydryl-dependent Enzyme Hydrolyze Gabexate in Human Blood

Yamaori

Kushihara

Fujiyama

et al. 2007

JOURNAL OF HEALTH SCIENCE

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“…[53] Human plasma contains cholinesterase but little carboxylesterase in contrast to rat plasma, which has high carboxylesterase levels. [54] Human-plasma hydrolysis of mebeverine was completely inhibited with physostigmine but only partially inhibited in rat plasma. [36] For BISGMA, the presence of the tetrahydroxy metabolite ( Figure 2) was determined to be below the limit of quantitation of 25 ng Á mL À1 indicating stability in fresh human plasma.…”

Section: Aqueous Chemical Stabilitymentioning

confidence: 99%

In-Vitro Stability, Metabolism, and Transport of Dental Monomers Made from Bisphenol A and Bisphenol F

et al. 2002

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“…Various specific hydrolases play a role in this hydrolysis in different tissues. For example, human CES 1 and 2 are the major contributors to this activity in the liver and intestine, respectively (Inoue et al, 1980;Heymann and Mentlein, 1988;Williams et al, 1989;Tang et al, 2006). In plasma, aspirin is rapidly hydrolyzed (Rowland et al, 1972) by BChE (Hofstee, 1951;Morgan and Truitt, 1965), PON (Santanam and Parthasarathy, 2007;Jaichander et al, 2008), and albumin (Morikawa et al, 1979;Yang et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…After oral administration in humans, aspirin undergoes hydrolysis in the intestine, liver, and plasma (Rowland et al, 1972;Williams et al, 1989). Various specific hydrolases play a role in this hydrolysis in different tissues.…”

Section: Introductionmentioning

confidence: 99%

Aspirin Hydrolysis in Human and Experimental Animal Plasma and the Effect of Metal Cations on Hydrolase Activities

Bahar

Imai

2013

Drug Metab Dispos

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The hydrolyzing properties of plasma esterases for aspirin were investigated in human plasma and plasma from experimental animals. The observed rates of aspirin hydrolysis were in the following order: rabbit > human > monkey > rat > mouse > dog > minipig. In human, monkey, and dog plasma, aspirin was hydrolyzed by their major hydrolases, paraoxonase (PON), butyrylcholinesterase (BChE), and albumin. In rabbit, mouse, and rat plasma, carboxylesterase (CES) was determined to be the enzyme responsible for aspirin hydrolysis, and in mouse and rat plasma, especially the latter, hydrolase activity was increased by the addition of ethopropazine, a specific inhibitor of BChE. Interestingly, divalent cations affected the plasma activity by enhancing or inhibiting the hydrolase activity of plasma BChE. The addition of 2 mM calcium increased the hydrolysis of aspirin in human, monkey, and dog plasma by 2.7-, 1.9-, and 2.3-fold, respectively. Magnesium showed a similar but lesser effect. Increasing concentrations of calcium and magnesium resulted in a two-phase stimulatory effect on aspirin hydrolysis in human plasma. In contrast, the addition of zinc had an inhibitory effect on plasma BChE activity. It is postulated that calcium and magnesium bind to BChE and thereby change the conformation of the enzyme to a more appropriate position for aspirin hydrolysis.

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Human liver and plasma aspirin esterase

Cited by 37 publications

References 13 publications

Butyrylcholinesterase and Erythrocyte Sulfhydryl-dependent Enzyme Hydrolyze Gabexate in Human Blood

Butyrylcholinesterase and Erythrocyte Sulfhydryl-dependent Enzyme Hydrolyze Gabexate in Human Blood

In-Vitro Stability, Metabolism, and Transport of Dental Monomers Made from Bisphenol A and Bisphenol F

Aspirin Hydrolysis in Human and Experimental Animal Plasma and the Effect of Metal Cations on Hydrolase Activities

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