Glyoxylate cycle in the rat liver: effect of vitamin D
            <sub>3</sub>
            treatment

Davis, Walter L.; Matthews, James L.; Goodman, David B. P.

doi:10.1096/fasebj.3.5.2537775

Cited by 41 publications

(23 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The same authors have demonstrated induction by VD of peroxisomal -oxidation in rat liver (Davis et al 1989).…”

Section: Introductionmentioning

confidence: 78%

“…None was upregulated. This was unexpected since Davis et al (1989) reported an increase in peroxisomal palmitate oxidation in rat liver after VD administration (a single dose of 500 IU). There is, however, no actual contradiction with our mRNA assay; enzyme capacity can be modified by other mechanisms such as mRNA stability or enzyme turnover (Horie & Suga 1989).…”

Section: Discussionmentioning

confidence: 95%

See 1 more Smart Citation

Modulation of the peroxisomal gene expression pattern by dehydroepiandrosterone and vitamin D: therapeutic implications

Depreter

Vandesompele²,

Espeel³

et al. 2002

Journal of Endocrinology

View full text Add to dashboard Cite

Peroxisomes are ubiquitous organelles required for several metabolic functions. Their dysfunction is responsible for a group of human inherited disorders. In the search for endogenous factors regulating the peroxisomal compartment in normal liver, we treated female rats with dehydroepiandrosterone (DHEA) and 25-hydroxycholecalciferol for 1 and 6 days. Relative transcription levels of 39 selected genes were evaluated by real-time quantitative RT-PCR analysis. Catalase (peroxisomal marker)-specific activity was assayed in total liver homogenate and peroxisomes were visualized by catalase localization. DHEA induced peroxisome proliferation and raised catalase specific activity. Expression levels of 16 (of which 11 were peroxisomal) genes were altered. Pex 11, acyl-CoA oxidase, -and -multifunctional enzyme, thiolase 1, phytanoyl-CoA hydroxylase, 70 kDa peroxisomal membrane protein and very long chain acyl-CoA synthetase were upregulated, three others were downregulated. Vitamin D caused downregulation of six genes. Administration of vitamin D to peroxisomal disorder patients may be contraindicated. The adrenocortical hormone DHEA is a potential natural regulator of the peroxisomal compartment. Its therapeutic use in X-linked adrenoleukodystrophy, some other -oxidation defects and classical Refsum should be considered.

show abstract

“…The same authors have demonstrated induction by VD of peroxisomal -oxidation in rat liver (Davis et al 1989).…”

Section: Introductionmentioning

confidence: 78%

Section: Discussionmentioning

confidence: 95%

Modulation of the peroxisomal gene expression pattern by dehydroepiandrosterone and vitamin D: therapeutic implications

Depreter

Vandesompele²,

Espeel³

et al. 2002

Journal of Endocrinology

View full text Add to dashboard Cite

show abstract

“…Recent studies have demonstrated that hepatic tissue has several physiological responses to 1,25(OH)2D3 (16)(17)(18)(19)(20)(21)(22)(23)(24)46) and appears to contain high-affinity receptors for this potent hormone (47). General vitamin D deficiency in the rat has been shown to alter hepatic function as manifested by delayed bromosulfthalein clearance and elevated plasma transaminases (16).…”

Section: Identificationmentioning

confidence: 99%

“…Furthermore, this study also noted liver histology changes consistent with periportal necrosis due to vitamin D deficiency. Hepatic isocitrate lyase and malate synthase are also known to be decreased in vitamin D deficiency (46). In addition to these generalized symptoms of vitamin D deficiency, 1,25(OH)2D3 is known to specifically increase hydroxymethylglutaryl CoA reductase activity (18), decrease liver regeneration time independent of calcium (17), regulate the synthesis of hepatic DNA polymerase a (19,20), increase [3H]thymidine incorporation into hepatic DNA (17), and enable regenerating liver cells to make functional ribonucleotide reductase subunits (21).…”

Section: Identificationmentioning

confidence: 99%

25-Hydroxyvitamin D3-1 alpha-hydroxylase in porcine hepatic tissue: subcellular localization to both mitochondria and microsomes.

Hollis

1990

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

In vitro studies were performed to assess the ability of hepatic homogenates, mitochondria, and microsomes to la-hydroxylate 25-hydroxyvitamin D3 (25(OH)D3]. Addition of 25(OH)D3 to either hepatic mitochondria or microsomes caused a concentration-dependent increase in the production of 1,25-dihydroxyvitamin D3 [1,25(OH) Because of its inability to achieve substrate saturation, meaningful kinetic parameters could not be calculated for the hepatic microsomal la-hydroxylase. These data demonstrate the liver to be an even more dynamic organ than was previously believed with respect to vitamin D metabolism in that the liver has the potential to produce 1,25(OH)2D3 in situ by at least two separate mechanisms.It is well established that various side chain and/or A-ring hydroxylation reactions are essential for the metabolic activation of vitamin D3 (1, 2). Circulating vitamin D3 first undergoes a hepatic conversion to 25-hydroxyvitamin D3 [25(OH)D3] (3). The hydroxylase enzymes responsible for this conversion are known to be cytochrome P-450 mixed-function oxidases that are NADPH dependent and are located in both hepatic mitochondria (4-6) and microsomes (7,8). Final activation of 25(OH)D3 into 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] takes place primarily in the kidney (9). The renal enzyme responsible for this activation, 25(OH)D3 lahydroxylase, is also known to be a cytochrome P450 mixedfunction oxidase that is located solely in the inner mitochondrial membrane (10, 11). In recent years, other tissues have also been shown to be capable of synthesizing 1,25(OH)2D3, including placenta (12), bone cells (13), lymphatic tissue (14), and keratinocytes (15). Compared with the renal 25(OH)D3 la-hydroxylase, very little information is known with respect to the metabolic control of these extrarenal 25(OH)D3 lahydroxylases and essentially no information is available concerning their subcellular distribution.Because of the important role of 1,25(OH)2D3 in various aspects of hepatic function (16-24), the possibility that the liver could synthesize in situ this hormonal form of vitamin D3 was investigated. It is reported here that both hepatic mitochondria and microsomes possess a 25(OH)D3 lahydroxylase in significant amounts. These enzymes differ in some characteristics, but both appear to behave as cytochrome P-450 mixed-function oxidases. MN). Coomassie blue protein assay reagent was purchased from Pierce. Nicotinamide adenine dinucleotide phosphate, isocitrate, N,N'-diphenylethylenediamine (DPED), dithiothreitol, and ethylenediaminetetraacetic acid were purchased from Sigma. All solvents were of HPLC grade and were obtained from Fisher. MATERIALS AND METHODS ReagentsLivers. Livers from 3-month-old castrated male pigs, maintained on stock diet, were obtained at the time of slaughter. The livers were perfused with ice-cold 0.15 M NaCl, minced, and placed in an appropriate volume of ice-cold 50 mM Na2HPO4 (pH 7.4) buffer containing 0.25 M sucrose and 0.5 mM EDTA to provide a 20% (wt/vol) 6009The publication costs of th...

show abstract

“…Vitamin E with its anti-oxidant properties is important for alleviating the effects of cardiac oxidative stress [ 97 , 98 ] by inhibiting lipid peroxidation [ 99 , 100 ], stress signaling pathways [ 101 ] and apoptosis [ 102 , 98 , 101 ]. Regarding vitamin D, although there is not much information about its role in cardiac fatty acid oxidation, it has been associated with increased fatty acid oxidation in other organs such as liver [ 103 ] and bone cartilage [ 104 ]. Thus, vitamin D may have a positive effect on cardiac fatty acid oxidation.…”

Section: Role Of Lipoprotein-carried Vitamins In Cardiac Metabolism Amentioning

confidence: 99%

Lipoproteins: A Source of Cardiac Lipids

Drosatos

Goldberg

2014

Cardiac Energy Metabolism in Health and Disease

View full text Add to dashboard Cite

Lipids are the major substrate for cardiac ATP production and they are derived from adipose tissue or lipoprotein triglycerides. Lipoproteins are synthesized in the liver and they obtain their mature form following interaction with enzymes that are present in the circulation. Lipoprotein-derived fatty acids are released by lipoprotein lipase and are then taken up by cardiomyocytes either passively or via fatty acid receptors, such as CD36. Uptake of remnant lipoproteins via cardiomyocyte lipoprotein receptors is also possible. Besides fatty acids, other hydrophobic molecules such as cholesteryl esters, retinyl esters and vitamins are delivered by lipoproteins to the heart. While lipids are important for normal cardiac function, excessive lipid uptake, also known as lipotoxicity, may lead to cardiac abnormalities. This chapter focuses on the role of lipoproteins in providing fatty acids and other essential lipids to the heart in healthy conditions as well as in cardiac disease.

show abstract

Glyoxylate cycle in the rat liver: effect of vitamin D ₃ treatment

Cited by 41 publications

References 19 publications

Modulation of the peroxisomal gene expression pattern by dehydroepiandrosterone and vitamin D: therapeutic implications

Modulation of the peroxisomal gene expression pattern by dehydroepiandrosterone and vitamin D: therapeutic implications

25-Hydroxyvitamin D3-1 alpha-hydroxylase in porcine hepatic tissue: subcellular localization to both mitochondria and microsomes.

Lipoproteins: A Source of Cardiac Lipids

Contact Info

Product

Resources

About

Glyoxylate cycle in the rat liver: effect of vitamin D 3 treatment

Cited by 41 publications

References 19 publications

Modulation of the peroxisomal gene expression pattern by dehydroepiandrosterone and vitamin D: therapeutic implications

Modulation of the peroxisomal gene expression pattern by dehydroepiandrosterone and vitamin D: therapeutic implications

25-Hydroxyvitamin D3-1 alpha-hydroxylase in porcine hepatic tissue: subcellular localization to both mitochondria and microsomes.

Lipoproteins: A Source of Cardiac Lipids

Contact Info

Product

Resources

About

Glyoxylate cycle in the rat liver: effect of vitamin D ₃ treatment