Multiple functions of vitamin A.

Wolf, George

doi:10.1152/physrev.1984.64.3.873

Cited by 337 publications

(171 citation statements)

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“…In the plasma, RBP-retinol is found in complex with TTR. This association is proposed to facilitate RBP release from its site of synthesis in the endoplasmic reticulum and to prevent renal filtration of RBP (20,21). The presence of retinol bound to RBP is essential for the formation of a stable complex with TTR (22).…”

Section: Ttr Binding To Rbp: a Partnership For The Transport Of Retinolmentioning

confidence: 99%

Aboard transthyretin: From transport to cleavage

et al. 2010

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SummaryTransthyretin (TTR) is a plasma and cerebrospinal fluid protein mainly recognized as the transporter of thyroxine (T 4 ) and retinol. Mutated TTR leads to familial amyloid polyneuropathy, a neurodegenerative disorder characterized by TTR amyloid deposition particularly in peripheral nerves. Beside its transport activities, TTR is a cryptic protease and participates in the biology of the nervous system. Several studies have been directed at finding new ligands of TTR to further explore the biology of the protein. From the identified ligands, some were in fact TTR protease substrates. In this review, we will discuss the existent information concerning TTR ligands/substrates. 2010 IUBMB IUBMB Life, 62(6): [429][430][431][432][433][434][435] 2010

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Section: Ttr Binding To Rbp: a Partnership For The Transport Of Retinolmentioning

confidence: 99%

Aboard transthyretin: From transport to cleavage

et al. 2010

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“…Retinoid homeostasis involves balance among multiple retinoids in multiple tissues effected through dietary intake, storage, mobilization, transport, and metabolism (1)(2)(3)(4)(5). Specific binding proteins, enzymes, and receptors control flux through the central pathways of retinoid homeostasis, ultimately to produce retinoic acid, an active form of vitamin A (Figure 1) (6)(7).…”

Section: Introductionmentioning

confidence: 99%

HPLC/UV quantitation of retinal, retinol, and retinyl esters in serum and tissues

Kane

Folias

Napoli

2008

Analytical Biochemistry

154

165

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We report robust HPLC/UV methods for quantifying retinyl esters (RE), retinol (ROL) and retinal (RAL) applicable to diverse biological samples, with lower limits of detection of 0.7 pmol, 0.2 pmol, and 0.2 pmol, respectively, and linear ranges >3 orders of magnitude. These assays function well with small, complex biological samples (10-20 mg tissue). Coefficients of variation range from: intra-day, 5.9-10.0%; inter-day, 5.9-11.0%. Quantification of endogenous RE, ROL, and RAL in mouse serum and tissues (liver, kidney, adipose, muscle, spleen, testis, skin, brain, and brain regions) reveals utility. Ability to discriminate spatial concentrations of ROL and RE is illustrated with C57BL/6 mouse brain loci (hippocampus, cortex, olfactory bulb, thalamus, cerebellum, and striatum.) We also developed a method to distinguish isomeric forms of ROL to investigate precursors of retinoic acid. The ROL isomer assay has limits of detection between 3.5-4.5 pmol and a similar linear range and % CV as the ROL/RE and RAL assays. The assays described here provide for sensitive and rigorous quantification of endogenous RE, ROL, and RAL to elucidate retinoid homeostasis in disease states, such as Alzheimer's disease, type 2 diabetes, obesity, and cancer.

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“…Retinol is the major circulating retinoid in the human body (Ong and Chytil, 1983;Wolf, 1984). All-trans-retinoic acid (all-trans-RA) is an endogenous metabolite of retinol (McCormick and Napoli, 1982) which has proven to be more potent than retinol in a variety of in vivo and in vitro assay systems.…”

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Induction of the oxidative catabolism of retinoic acid in MCF-7 cells

Krekels

Verhoeven²,

Dun³

et al. 1997

Br J Cancer

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Cytochrome P450-dependent oxidation is a pathway for all-trans-retinoic acid (all-trans-RA) catabolism. Induction of this catabolic pathway was studied in MCF-7 breast cancer cells. MCF-7 cells showed low constitutive all-trans-RA catabolism. Concentration-dependent induction was obtained by preincubation of the cells with all-trans-RA (10(-9) to 10(-6) M). Onset of induction was fast, being detectable within 60 min, with maximal induction (45-fold) obtained after 16 h. Enzymatic characterization of induced all-trans-RA catabolism showed an estimated Km value (Michaelis-Menten constant) of 0.33 microM and a Vmax value (maximal velocity of an enzyme-catalysed reaction) of 54.5 fmol polar all-trans-RA metabolites 10(6) cells(-1) h(-1). These kinetic parameters represent the overall formation of polar metabolites from all-trans-RA. Induction of all-trans-RA catabolism was also obtained with other retinoids, CH55 >> 13-cis-RA = all-trans-RA > 9-cis-RA > 4-keto-all-trans-RA > 4-keto-13-cis-RA > retinol. The potency of the retinoids to induce all-trans-RA catabolism was correlated to their retinoic acid receptor affinity (Crettaz et al, 1990; Repa et al, 1990; Sani et al, 1990). Induction of all-trans-RA catabolism was inhibited by actinomycin D. Furthermore, all-trans-RA did not increase cytosolic retinoic acid-binding protein (CRABP) mRNA levels. These data suggest that induction of all-trans-RA catabolism in MCF-7 cells is a retinoic acid receptor-mediated gene transcriptional event. Induced all-trans-RA catabolism was inhibited by various retinoids with decreasing potency in the order: all-trans-RA > 4-keto-all-trans-RA > 13-cis-RA > 9-cis-RA > 4-keto-13-cis-RA > retinol > CH55. The antitumoral compound liarozole-fumarate inhibited all-trans-RA catabolism with a potency similar to that of all-trans-RA. Images Figure 4

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Multiple functions of vitamin A.

Cited by 337 publications

References 0 publications

Aboard transthyretin: From transport to cleavage

Aboard transthyretin: From transport to cleavage

HPLC/UV quantitation of retinal, retinol, and retinyl esters in serum and tissues

Induction of the oxidative catabolism of retinoic acid in MCF-7 cells

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