Vitamin A Acid from Retinene

Barua, R. K.; Barua, A. B.

doi:10.1042/bj0920021c

Cited by 15 publications

(4 citation statements)

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“…1 H nuclear magnetic resonance (NMR) data of the purified acycloretinal were consistent with the values reported (36,37). Acycloretinoic acid (3,7,11,15-tetramethyl-2,4,6,8,10,14-hexadecahexaenoic acid) was prepared from the purified acycloretinal with Tollens reagent by the method of Barua and Barua (38). It was further purified on a TSK-Gel Silica 60 column, 4.6 × 250 mm with hexane/ethyl acetate (92:8, vol/vol) containing 0.1% acetic acid as a mobile phase.…”

Section: Methodsmentioning

confidence: 77%

Formation of cleavage products by autoxidation of lycopene

Kim

Nara

Kobayashi

et al. 2001

Lipids

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The cleavage products formed by autoxidation of lycopene were evaluated in order to elucidate possible oxidation products of lycopene in biological tissues. Lycopene solubilized at 50 microM in toluene, aqueous Tween 40, or liposomal suspension was oxidized by incubating at 37 degrees C for 72 h. Among a number of oxidation products formed, eight products in the carbonyl compound fraction were identified as 3,7,11 -trimethyl-2,4,6,10-dodecatetraen-1-al, 6,10,14-trimethyl-3,5,7,9,13-pentadecapentaen-2-one, acycloretinal, apo-14'-lycopenal, apo-12'-lycopenal, apo-10'-lycopenal, apo-8'-lycopenal, and apo-6'-lycopenal. These correspond to a series of products formed by cleavage in the respective 11 conjugated double bonds of lycopene. The maximal formation of acycloretinal was 135 nM in toluene, 49 nM in aqueous Tween 40, and 64 nM in liposomal suspension. Acycloretinoic acid was also formed by autoxidation of lycopene, although its formation was lower in the aqueous media than in toluene. The pig liver homogenate had the ability to convert acycloretinal to acycloretinoic acid, comparable to the conversion of all-transretinal to all-trans-retinoic acid. These results suggest that lycopene might be cleaved to a series of apolycopenals and short-chain carbonyl compounds under the oxidative conditions in biological tissues and that acycloretinal is further enzymatically converted to acycloretinoic acid.

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Section: Methodsmentioning

confidence: 77%

Formation of cleavage products by autoxidation of lycopene

Kim

Nara

Kobayashi

et al. 2001

Lipids

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“…The 9-cw-RA was either a gift from Hoffman-La Roche (Nutley, NJ) or synthesized as described below. The 9-cisand 9,13-di-cw-RA were prepared by oxidation of 9-cw-retinal (Sigma Chemical Co., St. Louis, MO) with Tollens reagent (Barua & Barua, 1964). The Tollens reagent was prepared immediately prior to use by combining equal volumes of 10% w/w AgNOs and 10% w/w NaOH.…”

Section: Methodsmentioning

confidence: 99%

Identification of 9-cis,13-cis-Retinoic Acid as a Major Circulating Retinoid in Plasma

Horst¹,

Reinhardt²,

Goff³

et al. 1995

Biochemistry

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In the course of measuring the concentrations of retinoic acids (RA) in bovine plasma, a major peak was observed which comigrated with 9-cis-RA on normal-phase high-performance liquid chromatography. Rechromatography of this retinoic on reverse-phase high-performance liquid chromatography showed that it was distinct from 9-cis-,13-cis-, and all-trans-RA, but comigrated with 9-cis,13-cis-retinoic acid (9,13-di-cis-RA). This retinoid was identified as 9,13-di-cis-RA based on its chemical, spectral, and chromatographic properties. Plasma concentrations of 9,13-di-cis-RA increased from < or = 0.5 ng/mL at birth to 5-6 ng/mL by 48 h of age in the calf. The 9,13-di-cis-RA was also a major circulating product of 9-cis-RA dosed intramuscularly to rats; conversely, intravenous administration of 9,13-di-cis-RA produced circulating 9-cis-RA in the rat. 9,13-Di-cis-RA had little or no affinity for cellular retinoic acid binding protein types I and II. This study establishes 9,13-di-cis-RA as a naturally-occurring retinoid under physiological conditions, shows that it undergoes interconversion with 9-cis-RA, and emphasizes a need for careful chromatography to resolve 9-cis-RA and 9,13-di-cis-RA. This is consistent with in vivo 13-cis isomerization operating to modify the concentration and perhaps the activity of 9-cis-RA in vivo.

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“…3-OH-atRA was synthesized by oxidation of 3-OH-retinal with Tollens' reagent (Barua and Barua, 1964). The Tollens' reagent was freshly prepared before use by mixing equal volumes of 10% w/w AgNO 3 and 10% w/w NaOH.…”

Section: Methodsmentioning

confidence: 99%

Substrate Specificity and Ligand Interactions of CYP26A1, the Human Liver Retinoic Acid Hydroxylase

Thatcher¹,

Buttrick²,

Shaffer³

et al. 2011

Mol Pharmacol

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All-trans-retinoic acid (atRA) is the active metabolite of vitamin A. atRA is also used as a drug, and synthetic atRA analogs and inhibitors of retinoic acid (RA) metabolism have been developed. The hepatic clearance of atRA is mediated primarily by CYP26A1, but design of CYP26A1 inhibitors is hindered by lack of information on CYP26A1 structure and structure-activity relationships of its ligands. The aim of this study was to identify the primary metabolites of atRA formed by CYP26A1 and to characterize the ligand selectivity and ligand interactions of CYP26A1. On the basis of high-resolution tandem mass spectrometry data, four metabolites formed from atRA by CYP26A1 were identified as 4-OH-RA, 4-oxo-RA, 16-OH-RA and 18-OH-RA. 9-cis-RA and 13-cis-RA were also substrates of CYP26A1. Forty-two compounds with diverse structural properties were tested for CYP26A1 inhibition using 9-cis-RA as a probe, and IC 50 values for 10 inhibitors were determined. The imidazole-and triazole-containing inhibitors [S- (5,6,7,8-tetrahydro-5,5,8,8-tetramethyl-2-naphthalenyl)-1-propenyl]benzoic acid and the peroxisome proliferator-activated receptor ligands rosiglitazone and pioglitazone inhibited CYP26A1 with IC 50 values of 3.7, 4.2, and 8.6 M, respectively. These data demonstrate that CYP26A1 has high ligand selectivity but accepts structurally related nuclear receptor agonists as inhibitors.

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Vitamin A Acid from Retinene

Cited by 15 publications

References 0 publications

Formation of cleavage products by autoxidation of lycopene

Formation of cleavage products by autoxidation of lycopene

Identification of 9-cis,13-cis-Retinoic Acid as a Major Circulating Retinoid in Plasma

Substrate Specificity and Ligand Interactions of CYP26A1, the Human Liver Retinoic Acid Hydroxylase

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