Glutathione S-transferase in humans: development and tissue distribution

Pacifici, Gian Maria; Franchi, M; Colizzi, Cesare; Giuliani, L.; Rane, Anders

doi:10.1007/bf00364848

Cited by 60 publications

(23 citation statements)

References 29 publications

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“…The lack of correlation between TMT ac tivity and gestational age suggests that the enzyme develops before the 14th week of gestation, the earliest liver assayed, and it does not undergo modification during the second trimester of gestation. Such a lack of correlation is consistent with previous re sults on acetyltransferase [5], glutathione transferase [6], glucuronyl transferase [14] and sulfotransferase [7], A late perinatal or postnatal development of hepatic TMT activity must occur, the av erage activity in the adult liver being 6 times higher than the fetal one. Placental TMT activity is comparable with that of the fetal liver.…”

Section: Mean ± Sdsupporting

confidence: 75%

Thiol Methyltransferase in Humans: Development and Tissue Distribution

Santerini²,

Giuliani³

et al. 1991

Dev Pharmacol Ther

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Thiol methyltransferase (EC 2.1.1.9, TMT) activity was measured with 2-mercaptoethanol in the microsomal fraction of 12 placenta and 31 fetal and 33 adult liver specimens. TMT activity (nmol/min incubation/mg protein; mean ± SD) was 0.61 ± 0.25 (placenta), 0.74 ± 0.45 (fetal liver), and 4.51 ± 2.29 (adult liver). TMT activity was also measured in extrahepatic tissues and it was about one order of magnitude lower in fetal lungs, kidney and intestine as compared with the fetal liver. A similar distribution pattern was also observed in adult tissues except that in the kidney TMT activity was one third of the hepatic one. Studies of enzyme kinetics showed that fetal and adult hepatic TMT obeyed non-Michaelis-Menten kinetics when 2-mercaptoethanol was the varying substrate. Average values of Km for the higher and lower affinity phases were 0.03 and 14.05 mmol/l, respectively (fetal liver) and 0.005 and 14.57 mmol/l, respectively (adult liver). This paper shows that TMT develops prenatally and its distribution pattern is consistent with that of other microsomal enzymes, being preferentially associated with the liver both in the human fetus and in adult subject.

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Section: Mean ± Sdsupporting

confidence: 75%

Thiol Methyltransferase in Humans: Development and Tissue Distribution

Santerini²,

Giuliani³

et al. 1991

Dev Pharmacol Ther

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“…We have previously described the distribution pattern of sulphotransferases with 2-naphthol as substrate in human tissues [7], Liver and intestine are among the tissues with the highest rate of 2-naphthol sulphotransferase. The hepatic sulphotransferase followed Michaelis-Menten kinetics [8]. In contrast, the intestinal one obeyed a complex kinetic pattern and two phases, one at higher and another at lower affinity for 2-naphthol, were observed [9], The reason of such a different kinetic pattern in the liver and intestinal mucosa was unknown.…”

Section: Introductionmentioning

confidence: 92%

“…The activity of the sulphotransferase for 2-naph thol in the presence of p-nitrophenol or dopamine was measured using [l4C]-2-naphthol as described pre viously [8]. Briefly, the incubation mixture (final vol ume 50 pi) contained 0.25 mol/1 sodium pyrophos phate buffer, pH 5.5, 0.5 mmol/1 [l4C]-2-naphtho!…”

Section: -Naphthol Sulphotransferase Inhibition By P-nitrophenol Andmentioning

confidence: 99%

Differential Distribution of Phenol and Catechol Sulphotransferases in Human Liver and Intestinal Mucosa

Cappiello¹,

Giuliani

Pacifici³

1990

Pharmacology

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Phenol and catechol sulphotransferases were studied with β-nitrophenol and dopamine as substrates in the mucosa of the ileum and colon obtained from 6 subjects and also in the liver from 6 subjects. The ileum and colon were from the same donor. The kinetics of phenol and catechol sulphotransferases were studied in each tissue specimen. The maximum velocity of reaction (V_max) for phenol sulphotransferase (in pmol × min^–1 × mg^–1; mean ± SD) was 165 ± 28 (ileum), 79 ± 42 (colon) and 1,361 ± 370 (liver), whereas V_maxfor catechol sulphotransferase was 489 ± 75 (ileum), 198 ± 93 (colon) and 39 ± 23 (liver). Phenol sulphotransferase is the predominant pathway in the liver, whereas catechol sulphotransferase is the predominant pathway in the intestine. The ileum catalysed the sulphation of p-nitrophenol and dopamine at a higher rate than the colon. The Michaelis-Menten constant (K_m) for phenol sulphotransferase (in μmol/l; mean ± SD) was 0.96 ± 0.11 (ileum), 1.00 ± 0.19 (colon) and 0.84 ± 0.07 (liver), whereas K_m for catechol sulphotransferase was 17.8 ± 2.8 (ileum), 18.2 ± 3.4 (colon) and 21.4 ± 1.2 (liver). K_m values of hepatic phenol or catechol sulphotransferases are not different from those of intestinal enzymes. Previous work has shown that 2-naphthol sulphotransferase obeys non-Michaelis-Menten kinetics in the human intestinal mucosa [Pharmacology, 1988;43:411]. Here, we show that 2-naphthol is sulphated by at least two enzymes in human intestine.

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“…However, on the basis of the available literature it seems that the drugmetabolizing enzymes generally are well ex pressed in the kidney. This is particularly true for conjugating enzymes such as glucuronyl transferase [11,42], acetyltransferasc [11,34], glutathionetransfcrase [11,31], sulphotransferase [11,35], and thiomcthyltransferase and thiopurinemethyltransferase [present work].…”

Section: Discussionmentioning

confidence: 99%

Profile of Drug-Metabolizing Enzymes in the Cortex and Medulla of the Human Kidney

et al. 1989

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The cortex and medulla were isolated from kidneys whose donors (5 men and 1 woman, aged between 44 and 68 years) were undergoing nephrectomy to remove a tumor. Kidneys with normal architecture for at least two thirds of the organ were included in the study. Tissue specimens used in our experiments were free from pathological changes. The activities of the following enzymes of phase INADPH cytochrome c reductase, aminopyrine N-demethylase, ethoxycoumarin O-deethylase, ethoxyresorufin O-deethylase, microsomal and cytosolic epoxide hydrolases, glutathione reductase and glutathione peroxidase, and those of the following enzymes of phase II glutathione transferase, glucuronyl transferase, sulphotransferase, acetyltransferase, thiomethyltransferase, thiopurinemethyltransferase, thioltransferase and glyoxalase were measured. The activity in renal cortex was significantly higher than in medulla for NADPH cytochrome c reductase, cytosolic epoxide hydrolase, glutathione reductase and glutathione peroxidase (phase I enzymes), and glutathione transferase, acetyltransferase, thiomethyltransferase, thiopurinemethyltransferase, thioltransferase and glyoxalase (phase II enzymes). The other enzymes had similar activity in cortex and medulla. The distribution pattern of drug-metabolizing enzymes in the human kidney cannot be considered as a single pattern because of the observed enzyme-dependent differences between cortex and medulla.

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Glutathione S-transferase in humans: development and tissue distribution

Cited by 60 publications

References 29 publications

Thiol Methyltransferase in Humans: Development and Tissue Distribution

Thiol Methyltransferase in Humans: Development and Tissue Distribution

Differential Distribution of Phenol and Catechol Sulphotransferases in Human Liver and Intestinal Mucosa

Profile of Drug-Metabolizing Enzymes in the Cortex and Medulla of the Human Kidney

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