Esterification and hydrolysis of vitamin A in the liver of brook trout (Salvelinus fontinalis) and the influence of a coplanar polychlorinated biphenyl

Ndayibagira, Aristocle; Spear, Philip A.

doi:10.1016/s0742-8413(98)10129-9

Cited by 15 publications

(14 citation statements)

References 41 publications

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“…The concentration of liver DRP/O was significantly decreased in this study (Table 1), which concurs with our previous results of diminished retinoid stores in fish populations inhabiting contaminated environments [16, 18–20]. The brook trout investigated in this study also served to establish the effects of TCBP on enzymes regulating retinoid storage [23]. Retinyl ester hydrolase activity (bile salt independent and optimum in an acid medium with a pH of 4.2) was strongly inhibited by TCBP, even at the lowest dose level of 0.1 μg/g [23].…”

Section: Discussionsupporting

confidence: 92%

“…The brook trout investigated in this study also served to establish the effects of TCBP on enzymes regulating retinoid storage [23]. Retinyl ester hydrolase activity (bile salt independent and optimum in an acid medium with a pH of 4.2) was strongly inhibited by TCBP, even at the lowest dose level of 0.1 μg/g [23]. In mammals, this retinyl ester hydrolase activity is associated with absorption of retinyl esters from chylomicrons in the liver [41]; therefore, its inhibition may interfere with the ability to store retinoids.…”

Section: Discussionmentioning

confidence: 99%

“…As our previous investigation with rainbow trout involved a single TCBP dose [17], a logarithmic range of TCBP doses is explored and the two salmonid species compared in this study. In addition, the effects of TCBP on the retinoid storage enzymes retinyl ester hydrolase and lecithin:retinol acyltrans‐ferase in previous experiment were reported separately [23] but are discussed here in the context of their effects on the RA metabolic pathway.…”

Section: Introductionmentioning

confidence: 99%

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Dose‐dependent stimulation of hepatic retinoic acid hydroxylation/oxidation and glucuronidation in brook trout, Salvelinus fontinalis, after exposure to 3,3′,4,4′‐tetrachlorobiphenyl

Boyer

Ndayibagira

Spear

2000

Enviro Toxic and Chemistry

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Abstract-Extremely low stores of vitamin A have been reported in fish and birds inhabiting regions contaminated by coplanar polychlorinated biphenyls (PCBs) and other organochlorines, suggesting many possible effects on retinoid biochemical pathways. Metabolic imbalances associated with biologically active retinoids (e.g., retinoic acid) could be associated with teratogenesis, edema, growth inhibition, reproductive impairment, immunosuppression, and susceptibility to cancer. Sexually mature brook trout were injected intraperitoneally with the coplanar PCB 3,3Ј,4,4Ј-tetrachlorobiphenyl (TCBP) and again 4 weeks later. At 8 weeks, retinoic acid metabolism was measured in liver microsomes. To our knowledge, retinoic acid conjugation by UDP-glucuronyltransferase is described here for the first time in fish. A substantial rate of glucuronidation was detected in the microsomes from control brook trout, which tended to increase over the dose range of TCBP. Glucuronidation was significantly greater in fish receiving the 10 g/ g body weight dose level. Metabolism through the cytochrome P450 system was also dose-dependent, resulting in significantly greater production of 4-hydroxyretinoic acid at the 10 g/g dose level. In contrast, subsequent oxidation to 4-oxo-retinoic acid was greatest at the 1 g/g dose level and did not increase further at higher doses. Liver stores of dehydroretinyl palmitate/oleate were significantly decreased at the 5 and 10 g/g dose levels.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Dose‐dependent stimulation of hepatic retinoic acid hydroxylation/oxidation and glucuronidation in brook trout, Salvelinus fontinalis, after exposure to 3,3′,4,4′‐tetrachlorobiphenyl

Boyer

Ndayibagira

Spear

2000

Enviro Toxic and Chemistry

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“…It was reported that lethitin retinol acyltransferase (LRAT), which is known to be the major enzyme esterifying retinol to retinyl esters in the liver, is stimulated by RA in mammals 47 . Recently, LRAT activity was also reported in fish, such as brook trout Salvelinus fontinalis 48 . Sequence analysis reveals that there is a 70% homologous gene sequence between mouse LRAT and the fugu genome.…”

Section: Discussionmentioning

confidence: 99%

Changes of retinoid contents in larval Japanese flounder Paralichthys olivaceus and Artemia nauplii enriched with a large dose of all-trans retinoic acid

2004

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The present study examined the changes of retinoid content in larval Japanese flounder Paralichthys olivaceus and Artemia nauplii. Artemia nauplii were enriched with 100 mg alltrans retinoic acid (atRA) for 6 h in a 10-L culture tank and then starved for the next 24 h. Flounder larvae at the G stage were fed Artemia nauplii enriched with atRA and then starved for the next 24 h. They were sampled at − 6 h (before enrichment), and at 0, 6, 9, 18 and 24 h after enrichment for analysis of three isomers of retinoic acid (atRA, 9 cis -and 13 cis retinoic acid), retinol, retinal, and retinyl palimitate. atRA was rapidly accumulated in Artemia without isomerization. Peaks of atRA and retinyl palmitate levels were observed at 6 and 18 h in Artemia , suggesting that Artemia excrete RA metabolites and re-uptake in the tank without water exchange. atRA levels in flounder reached a maximum level at 3 h after feeding and decrease to 50% of the maximum level within 18 h, suggesting that flounder larvae can rapidly excrete dietary atRA.

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“…The activity of enzymes that esterify retinol and hydrolyse retinyl esters such as retinyl ester hydrolase (REH), acyl-CoA:retinol acyltransferase (ARAT) and lecithin:retinol acyltransferase (LRAT) were also shown to be modulated by PCBs and TCDD in fish and laboratory animals ( Fig. 1, points 3, 4 and 8) (Chen et al, 1992;Nilsson et al, 1996;Ndayibagira and Spear, 1999;Nilsson et al, 2000). In addition, some hydroxylated PCB metabolites (HO-PCBs) can interact with transthyretin (TTR), as reported in vivo and in vitro in humans and rats.…”

Section: Introductionmentioning

confidence: 99%

Effects of polychlorobiphenyls, polybromodiphenylethers, organochlorine pesticides and their metabolites on vitamin A status in lactating grey seals

Berghe

Weijs

Habran

et al. 2013

Environmental Research

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a b s t r a c tPolychlorobiphenyls (PCBs), polybromodiphenylethers (PBDEs) and organochlorine pesticides (OCPs), such as dichlorodiphenyltrichloroethane (DDT) and hexachlorobenzene (HCB), are considered as endocrine disruptors in laboratory and wild animals. This study investigated whether these compounds and their hydroxylated metabolites (HO-PCBs and HO-PBDEs) may affect the homoeostasis of vitamin A, a dietary hormone, in the blubber and serum of twenty lactating grey seals sampled at early and late lactation on the Isle of May, Scotland. The effect of naturally produced compounds such as the methoxylated (MeO)-PBDEs was also examined. Vitamin A levels in inner blubber (37 7 9 mg/g wet weight (ww) and 92 7 32 mg/g ww at early and late lactation, respectively) and serum (408 7 143 and 390 7 98 ng/ml at early and late lactation, respectively) appeared to be positively related to SPCBs, SPBDEs and several individual PCB and PBDE congeners in inner blubber and serum. These findings may suggest enhanced mobilisation of hepatic retinoid stores and redistribution in the blubber, a storage site for vitamin A in marine mammals. We have also reported that serum concentrations of SHO-PCBs and 4-OH-CB107 tended to increase with circulating vitamin A levels. Although the direction of the relationships may sometimes differ from those reported in the literature, our results are in agreement with previous findings highlighting a disruption of vitamin A homoeostasis in the blubber and bloodstream following exposure to environmental pollutants. The fact that vitamin A and PCBs appeared to share common mechanisms of mobilisation and transfer during lactation in grey seals (Debier et al., 2004;Vanden Berghe et al., 2010) may also play a role in the different relationships observed between vitamin A and lipophilic pollutants.

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Esterification and hydrolysis of vitamin A in the liver of brook trout (Salvelinus fontinalis) and the influence of a coplanar polychlorinated biphenyl

Cited by 15 publications

References 41 publications

Dose‐dependent stimulation of hepatic retinoic acid hydroxylation/oxidation and glucuronidation in brook trout, Salvelinus fontinalis, after exposure to 3,3′,4,4′‐tetrachlorobiphenyl

Dose‐dependent stimulation of hepatic retinoic acid hydroxylation/oxidation and glucuronidation in brook trout, Salvelinus fontinalis, after exposure to 3,3′,4,4′‐tetrachlorobiphenyl

Changes of retinoid contents in larval Japanese flounder Paralichthys olivaceus and Artemia nauplii enriched with a large dose of all-trans retinoic acid

Effects of polychlorobiphenyls, polybromodiphenylethers, organochlorine pesticides and their metabolites on vitamin A status in lactating grey seals

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