Effects of high-fat diet and fasting on levels of acyl-coenzyme a binding protein in liver, kidney, and heart of rat

Bhuiyan, Jalaluddin; Pritchard, P H; Pande, Shri V.; Seccombe, David W.

doi:10.1016/0026-0495(95)90013-6

Cited by 42 publications

(36 citation statements)

References 23 publications

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“…Previously, an increased concentration of ACBP was reported in the heart and in liver of the fat-fed insulinresistant rat (11), but this is the first study in skeletal muscles. Other proteins involved in transport and metabolism of FFA have, however, been studied in insulinresistant muscles.…”

Section: Discussionmentioning

confidence: 85%

“…Other proteins, like sterol carrier protein 2 and cytosolic fatty acid binding protein (FABP c ), are also able to bind acyl-CoA, but with much lower affinity (10). The effects of acyl-CoA on protein regulation depend on its free concentration, and addition of ACBP inhibits the acyl-CoA action (11,12). The acyl-CoA/ACBP ratio, rather than the total concentration of acyl-CoA, seems therefore to determine the biological (regulatory) effect of acyl-CoA (10).…”

mentioning

confidence: 99%

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Acyl-CoA Binding Protein Expression Is Fiber Type- Specific and Elevated in Muscles From the Obese Insulin-Resistant Zucker Rat

et al. 2002

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Accumulation of acyl-CoA is hypothesized to be involved in development of insulin resistance. Acyl-CoA binds to acyl-CoA binding protein (ACBP) with high affinity, and therefore knowledge about ACBP concentration is important for interpreting acyl-CoA data. In the present study, we used a sandwich enzyme-linked immunosorbent assay to quantify ACBP concentration in different muscle fiber types. Furthermore, ACBP concentration was compared in muscles from lean and obese Zucker rats. Expression of ACBP was highest in the slow-twitch oxidative soleus muscle and lowest in the fast-twitch glycolytic white gastrocnemius (0.46 ؎ 0.02 and 0.16 ؎ 0.005 g/mg protein, respectively). Expression of ACBP was soleus > red gastrocnemius > extensor digitorum longus > white gastrocnemius. Similar fiber type differences were found for carnitine palmitoyl transferase (CPT)-1, and a correlation was observed between ACBP and CPT-1. Muscles from obese Zucker rats had twice the triglyceride content, had approximately twice the long-chain acyl CoA content, and were severely insulin resistant. ACBP concentration was ϳ30% higher in all muscles from obese rats. Activities of CPT-1 and 3-hydroxy-acyl-CoA dehydrogenase were increased in muscles from obese rats, whereas citrate synthase activity was similar. In conclusion, ACBP expression is fiber type-specific with the highest concentration in oxidative muscles and the lowest in glycolytic muscles. The 90% increase in the concentration of acyl-CoA in obese Zucker muscle compared with only a 30% increase in the concentration of ACBP supports the hypothesis that an increased concentration of free acyl-CoA is involved in the development of insulin resistance. Diabetes 51:449 -454, 2002

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Section: Discussionmentioning

confidence: 85%

mentioning

confidence: 99%

Acyl-CoA Binding Protein Expression Is Fiber Type- Specific and Elevated in Muscles From the Obese Insulin-Resistant Zucker Rat

et al. 2002

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“…Previous results showing that ACBP is induced in hepatocytes in response to peroxisome proliferators (11,43) and that the acbp promoter is activated by PPAR␣ in transient transfections (10) have suggested that ACBP is a PPAR␣ target gene. However, other reports claiming a down-regulation of ACBP expression by fasting (11,12) suggest that ACBP does not behave as a typical PPAR␣ target gene. We have reinvestigated the effect of fasting and have shown that ACBP mRNA expression is indeed modestly down-regulated by fasting for 24 h and up-regulated again following refeeding with a carbohydrate-rich diet for 24 h. In contrast, the PPAR␣ target gene ACO is significantly induced by fasting.…”

Section: Discussionmentioning

confidence: 88%

“…dents-Previous semi-quantitative studies have shown that rats that have been fasted have a decreased expression level of ACBP mRNA and protein in the liver (12) and that feeding a high fat diet increases hepatic ACBP mRNA (11), indicating that ACBP expression is metabolically regulated. To establish further how fasting and feeding regulated ACBP expression, we performed a fasting/refeeding experiment with mice.…”

Section: Acbp Expression Is Regulated By Fasting/refeeding In Ro-mentioning

confidence: 99%

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The Gene Encoding Acyl-CoA-binding Protein Is Subject to Metabolic Regulation by Both Sterol Regulatory Element-binding Protein and Peroxisome Proliferator-activated Receptor α in Hepatocytes

Sandberg

Bloksgaard

Durán-Sandoval

et al. 2005

Journal of Biological Chemistry

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The acyl-CoA-binding protein (ACBP) is a 10-kDa intracellular lipid-binding protein that transports acylCoA esters. The protein is expressed in most cell types at low levels; however, expression is particularly high in cells with a high turnover of fatty acids. Here we confirm a previous observation that ACBP expression in rodent liver is down-regulated by fasting, and we show that insulin but not glucose is the inducer of ACBP expression in primary rat hepatocytes. In keeping with the regulation by insulin, we show that ACBP is a sterol regulatory element-binding protein 1c (SREBP-1c) target gene in hepatocytes. Members of the SREBP family activate the rat ACBP gene through binding sites for SREBP and the auxiliary factors Sp1 and nuclear factor Y in the proximal promoter. In addition, we show that ACBP is a peroxisome proliferator-activated receptor (PPAR) ␣ target gene in cultured hepatocytes and is induced in the liver by fibrates in a PPAR␣-dependent manner. Thus, ACBP is a dual PPAR␣ and SREBP-1c target gene in hepatocytes. Fasting leads to reduced activity of SREBP but increased activity of PPAR␣ in hepatocytes, and in keeping with ACBP being a dual target gene, we show that ACBP expression is significantly lower in livers from PPAR␣ knock-out mice than in livers from wild type mice. In conclusion, expression of ACBP in rodent hepatocytes is subject to dual metabolic regulation by PPAR␣ and SREBP-1c, which may reflect the need for ACBP during lipogenic as well as lipo-oxidative conditions.

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Triglyceride Metabolism in the Liver

Auger

Cohen

2017

Comprehensive Physiology

518

508

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Triglyceride molecules represent the major form of storage and transport of fatty acids within cells and in the plasma. The liver is the central organ for fatty acid metabolism. Fatty acids accrue in liver by hepatocellular uptake from the plasma and by de novo biosynthesis. Fatty acids are eliminated by oxidation within the cell or by secretion into the plasma within triglyceride-rich very low-density lipoproteins. Notwithstanding high fluxes through these pathways, under normal circumstances the liver stores only small amounts of fatty acids as triglycerides. In the setting of overnutrition and obesity, hepatic fatty acid metabolism is altered, commonly leading to the accumulation of triglycerides within hepatocytes, and to a clinical condition known as nonalcoholic fatty liver disease (NAFLD). In this review, we describe the current understanding of fatty acid and triglyceride metabolism in the liver and its regulation in health and disease, identifying potential directions for future research. Advances in understanding the molecular mechanisms underlying the hepatic fat accumulation are critical to the development of targeted therapies for NAFLD. © 2018 American Physiological Society. Compr Physiol 8:1-22, 2018.

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Effects of high-fat diet and fasting on levels of acyl-coenzyme a binding protein in liver, kidney, and heart of rat

Cited by 42 publications

References 23 publications

Acyl-CoA Binding Protein Expression Is Fiber Type- Specific and Elevated in Muscles From the Obese Insulin-Resistant Zucker Rat

Acyl-CoA Binding Protein Expression Is Fiber Type- Specific and Elevated in Muscles From the Obese Insulin-Resistant Zucker Rat

The Gene Encoding Acyl-CoA-binding Protein Is Subject to Metabolic Regulation by Both Sterol Regulatory Element-binding Protein and Peroxisome Proliferator-activated Receptor α in Hepatocytes

Triglyceride Metabolism in the Liver

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