Effect of hypolipidemic drugs, nafenopin and clofibrate, on the concentration of ligandin and Z protein in rat liver

Fleischner, G; Meijer, Dirk K. F.; Levine, Walter G.; Gatmaitan, Zenaida; Gluck, Robert; Arias, Irwin M.

doi:10.1016/0006-291x(75)90182-5

Cited by 57 publications

(7 citation statements)

References 18 publications

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“…Interesting to note and as formulated above, the activity of the cytosolic glutathione Stransferase is not impaired along with CLA intake (Table 3). This phase-II detoxifying enzyme has a critical role in cellular protection, and its activity might be induced during a chemical stress or by chemoprotective agents (43), or declined with peroxisome proliferator molecules (40)(41)(42). Therefore, in addition to the two phase-I enzymes presently studied (CYP4A1 and CYP2E1), the CLA diets caused no impairment of this glutathione-dependent detoxication activity either (phase II enzyme).…”

Section: Discussionmentioning

confidence: 86%

“…For instance, the peroxisomal ACO activity and the microsomal CYP4A1 activity remained unchanged (Table 3). Additionally, in peroxisome proliferation, the mitochondrion CPT-I activity is also often increased (35,39), and the cytosolic glutathione S-transferase activity is decreased (40)(41)(42). These activities were not modified after dietary intake of any of the CLA isomers (Table 3).…”

Section: Discussionmentioning

confidence: 91%

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Effects of conjugated linoleic acid isomers on lipid‐metabolizing enzymes in male rats

Martin

Grégoire

Siess³

et al. 2000

Lipids

105

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Male weanling Wistar rats (n = 15), weighing 200-220 g, were allocated for 6 wk to diets containing 1% (by weight) of conjugated linoleic acid (CLA), either as the 9c,11 t-isomer, the 10t,12c-isomer, or as a mixture containing 45% of each of these isomers. The five rats of the control group received 1% of oleic acid instead. Selected enzyme activities were determined in different tissues after cellular subfractionation. None of the CLA-diet induced a hepatic peroxisome-proliferation response, as evidenced by a lack of change in the activity of some characteristic enzymes [i.e., acyl-CoA oxidase, CYP4A1, but also carnitine palmitoyltransferase-I (CPT-I)] or enzyme affected by peroxisome-proliferators (glutathione S-transferase). In addition to the liver, the activity of the rate-limiting beta-oxidation enzyme in mitochondria, CPT-I, did not change either in skeletal muscle or in heart. Conversely, its activity increased more than 30% in the control value in epididymal adipose tissue of the animals fed the CLA-diets containing the 10t,12c-isomer. Conversely, the activity of phosphatidate phosphohydrolase, a rate-limiting enzyme in glycerolipid neosynthesis, remained unchanged in adipose tissue. Kinetic studies conducted on hepatic CPT-I and peroxisomal acyl-CoA oxidase with CoA derivatives predicted a different channeling of CLA isomers through the mitochondrial or the peroxisomal oxidation pathways. In conclusion, the 10t,12c-CLA isomer seems to be more efficiently utilized by the cells than its 9c,11t homolog, though the Wistar rat species appeared to be poorly responsive to CLA diets for the effects measured.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 91%

Effects of conjugated linoleic acid isomers on lipid‐metabolizing enzymes in male rats

Martin

Grégoire

Siess³

et al. 2000

Lipids

105

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“…[CoA] [6,8], [carnitine] [9,10] and the fatty-acid-binding Z-protein are increased [28][29][30]. Fibrate drugs may cause Table 5.…”

Section: Relation Between Mitochondrial and Peroxisomal /1-oxidationmentioning

confidence: 99%

Effects of ciprofibrate and 2-[5-(4-chlorophenyl)pentyl]oxirane-2-carboxylate (POCA) on the distribution of carnitine and CoA and their acyl-esters and on enzyme activities in rats. Relation between hepatic carnitine concentration and carnitine acetyltransferase activity

Bhuiyan

Bartlett

Sherratt

et al. 1988

Biochemical Journal

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The effects of feeding the peroxisome proliferators ciprofibrate (a hypolipidaemic analogue of clofibrate) or POCA (2-[5-(4-chlorophenyl)pentyl]oxirane-2-carboxylate) (an inhibitor of CPT I) to rats for 5 days on the distribution of carnitine and acylcarnitine esters between liver, plasma and muscle and on hepatic CoA concentrations (free and acylated) and activities of carnitine acetyltransferase and acyl-CoA hydrolases were determined. Ciprofibrate and POCA increased hepatic [total CoA] by 2 and 2.5 times respectively, and [total carnitine] by 4.4 and 1.9 times respectively, but decreased plasma [carnitine] by 36-46%. POCA had no effect on either urinary excretion of acylcarnitine esters or [acylcarnitine] in skeletal muscle. By contrast, ciprofibrate decreased [acylcarnitine] and [total carnitine] in muscle. In liver, ciprofibrate increased the [carnitine]/[CoA] ratio and caused a larger increase in [acylcarnitine] (7-fold) than in [carnitine] (4-fold), thereby increasing the [short-chain acylcarnitine]/[carnitine] ratio. POCA did not affect the [carnitine]/[CoA] and the [short-chain acylcarnitine]/[carnitine] ratios, but it decreased the [long-chain acylcarnitine]/[carnitine] ratio. Ciprofibrate and POCA increased the activities of acyl-CoA hydrolases, and carnitine acetyltransferase activity was increased 28-fold and 6-fold by ciprofibrate and POCA respectively. In cultures of hepatocytes, ciprofibrate caused similar changes in enzyme activity to those observed in vivo, although [carnitine] decreased with time. The results suggest that: (1) the reactions catalysed by the short-chain carnitine acyltransferases, but not by the carnitine palmitoyltransferases, are near equilibrium in liver both before and after modification of metabolism by administration of ciprofibrate or POCA; (2) the increase in hepatic [carnitine] after ciprofibrate or POCA feeding can be explained by redistribution of carnitine between tissues; (3) the activity of carnitine acetyltransferase and [total carnitine] in liver are closely related.

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“…Although its precise function in vivo has not yet been defined, it may be involved in the intracellular transport and compartmentation of long chain fatty acids, or it may protect specific enzymes against inhibition by long chain acyl-CoA esters Grinstead et al, 1983). Support for the first of these hypotheses comes from the observation that hepatic FABP concentration is altered by conditions that affect the uptake and utilization of free fatty acids (Fleischner et al, 1975;Ockner et al, 1979;Renaud et al, 1978).…”

Section: Introductionmentioning

confidence: 99%

Studies on fatty acid-binding proteins. The detection and quantification of the protein from rat liver by using a fluorescent fatty acid analogue

Wilkinson¹,

Wilton²

1986

Biochemical Journal

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Fatty acid-binding protein from rat liver is shown to bind the fluorescent fatty acid probe dansyl undecanoic acid. Binding is accompanied by a shift in the fluorescence emission maximum from 550 nm to 500 nm and a 60-fold fluorescence enhancement at 500 nm. These spectral properties have allowed the use of this probe to detect and quantify microgram amounts of liver fatty acid-binding protein during purification procedures. In conjunction with h.p.l.c. the method allows the rapid estimation of liver fatty acid-binding protein in biological samples. The validity of the method is demonstrated by measuring the concentration of fatty acid-binding protein in livers from control and hypolipidaemic-drug-treated rats. The dramatic diurnal rhythm previously reported for this protein [Dempsey (1984) Curr. Top. Cell. Regul. 24, 63-86] was not observed with this method.

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Effect of hypolipidemic drugs, nafenopin and clofibrate, on the concentration of ligandin and Z protein in rat liver

Cited by 57 publications

References 18 publications

Effects of conjugated linoleic acid isomers on lipid‐metabolizing enzymes in male rats

Effects of conjugated linoleic acid isomers on lipid‐metabolizing enzymes in male rats

Effects of ciprofibrate and 2-[5-(4-chlorophenyl)pentyl]oxirane-2-carboxylate (POCA) on the distribution of carnitine and CoA and their acyl-esters and on enzyme activities in rats. Relation between hepatic carnitine concentration and carnitine acetyltransferase activity

Studies on fatty acid-binding proteins. The detection and quantification of the protein from rat liver by using a fluorescent fatty acid analogue

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