Protein mediated fatty acid uptake: Synergy between CD36/FAT-facilitated transport and acyl-CoA synthetase-driven metabolism

Schneider, Hannah; Staudacher, Sarah; Poppelreuther, Margarete; Stremmel, Wolfgang; Ehehalt, Robert; Füllekrug, Joachim

doi:10.1016/j.abb.2014.01.025

Cited by 36 publications

(30 citation statements)

References 54 publications

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“…Since CD36 and FATP1 were unchanged, ACSL1 appears to function cooperatively with CD36 and FATP1 to facilitate LCFA uptake. This observation is consistent with a previous in vitro study showing ACSL1 and CD36 synergy in oleate uptake [12]. Our study suggests a previously unknown cooperative regulation of LCFA uptake between membrane transport protein FATP6 and intracellular acyl chain activation mediated by changes in gene expression.…”

Section: Discussionsupporting

confidence: 94%

Acyl CoA synthetase-1 links facilitated long chain fatty acid uptake to intracellular metabolic trafficking differently in hearts of male versus female mice

Goldenberg

Wang

Lewandowski

2016

Journal of Molecular and Cellular Cardiology

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Rationale Acyl CoA synthetase-1 (ACSL1) is localized at intracellular membranes, notably the mitochondrial membrane. ACSL1 and female sex are suggested to indirectly facilitate lipid availability to the heart and other organs. However, such mechanisms in intact, functioning myocardium remain unexplored, and roles of ACSL1 and sex in the uptake and trafficking of fats are poorly understood. Objective To determine the potential for ACSL1 and sex-dependent differences in metabolic trapping and trafficking effects of long-chain fatty acids (LCFA) within cardiomyocytes of intact hearts. Methods and Results 13C NMR of intact, beating mouse hearts, supplied 13C palmitate, revealed 44% faster trans-sarcolemmal uptake of LCFA in male hearts overexpressing ACSL1 (MHC-ACSL1) than in non-transgenic (NTG) males (P<0.05). Acyl CoA content was elevated by ACSL1 overexpression, 404% in males and 164% in female, relative to NTG. Despite similar ACSL1 content, NTG females displayed faster LCFA uptake kinetics compared to NTG males, which was reversed by ovariectomy. NTG female LCFA uptake rates were similar to those in ACSL1 males and ACSL1 females. ACSL1 and female sex hormones both accelerated LCFA uptake without affecting triglyceride content or turnover. ACSL1 hearts contained elevated ceramide, particularly C22 ceramide in both sexes and specifically, C24 in males. ACSL1 also induced lower content of fatty acid transporter-6 (FATP6) indicating cooperative regulation with ACSL1. Surprisingly, ACSL1 overexpression did not increase mitochondrial oxidation of exogenous palmitate, which actually dropped in female ACSL1 hearts. Conclusions ACSL1-mediated metabolic trapping of exogenous LCFA accelerates LCFA uptake rates, albeit to a lesser extent in females, which distinctly affects LCFA trafficking to acyl intermediates but not triglyceride storage or mitochondrial oxidation and is affected by female sex hormones.

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Section: Discussionsupporting

confidence: 94%

Acyl CoA synthetase-1 links facilitated long chain fatty acid uptake to intracellular metabolic trafficking differently in hearts of male versus female mice

Goldenberg

Wang

Lewandowski

2016

Journal of Molecular and Cellular Cardiology

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“…FATP1, 2 and 4 each is expressed~50% of FATP5 in mouse livers [41]. These intracellular FATPs may regulate the uptake via metabolic trapping of fatty acids into neutral lipids, sphingolipids and phospholipids [10], a process recently shown to take place in a concert manner with CD36 [25,55]. Based on our model FATP4 cells, we surmised that other ER-localizing FATPs [25,55], and ACS [43,44] may contribute to apoptosis and steatosis in vivo in a PPARγ and CD36-dependent manner.…”

Section: Discussionmentioning

confidence: 86%

Palmitate activation by fatty acid transport protein 4 as a model system for hepatocellular apoptosis and steatosis

Seeßle¹,

Liebisch

Schmitz

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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“…Some transporters may cooperate concertedly in fatty acids uptake, such as FABPpm and CD36 in heart and muscle (Chabowski et al, 2007), CD36 and ACSL1 in MDCK cell (Schneider et al, 2014), and ACSL1 and FATP1 in adipocytes (Richards et al, 2006). Both FATP1 and FATP4 belong to the FATP family, and their amino acid identity is 60.3% (Herrmann et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Lower Expression of SLC27A1 Enhances Intramuscular Fat Deposition in Chicken via Down-Regulated Fatty Acid Oxidation Mediated by CPT1A

Qiu

Xie

et al. 2017

Front. Physiol.

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Intramuscular fat (IMF) is recognized as the predominant factor affecting meat quality due to its positive correlation with tenderness, juiciness, and flavor. Chicken IMF deposition depends on the balance among lipid synthesis, transport, uptake, and subsequent metabolism, involving a lot of genes and pathways, however, its precise molecular mechanisms remain poorly understood. In the present study, the breast muscle tissue of female Wenchang chickens (WC) (higher IMF content, 1.24 in D120 and 1.62 in D180) and female White Recessive Rock chickens (WRR; lower IMF content, 0.53 in D120 and 0.90 in D180) were subjected to RNA-sequencing (RNA-seq) analysis. Results showed that many genes related to lipid catabolism, such as SLC27A1, LPL, ABCA1, and CPT1A were down-regulated in WC chickens, and these genes were involved in the PPAR signaling pathway and formed an IPA® network related to lipid metabolism. Furthermore, SLC27A1 was more down-regulated in WRR.D180.B than in WRR.D120.B. Decreased cellular triglyceride (TG) and up-regulated CPT1A were observed in the SLC27A1 overexpression QM-7 cells, and increased cellular triglyceride (TG) and down-regulated CPT1A were observed in the SLC27A1 knockdown QM-7 cells. These results suggest that lower lipid catabolism exists in WC chickens but not in WRR chickens, and lower expression of SLC27A1 facilitate IMF deposition in chicken via down-regulated fatty acid oxidation mediated by CPT1A. These findings indicate that reduced lipid catabolism, rather than increased lipid anabolism, contributes to chicken IMF deposition.

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Protein mediated fatty acid uptake: Synergy between CD36/FAT-facilitated transport and acyl-CoA synthetase-driven metabolism

Cited by 36 publications

References 54 publications

Acyl CoA synthetase-1 links facilitated long chain fatty acid uptake to intracellular metabolic trafficking differently in hearts of male versus female mice

Acyl CoA synthetase-1 links facilitated long chain fatty acid uptake to intracellular metabolic trafficking differently in hearts of male versus female mice

Palmitate activation by fatty acid transport protein 4 as a model system for hepatocellular apoptosis and steatosis

Lower Expression of SLC27A1 Enhances Intramuscular Fat Deposition in Chicken via Down-Regulated Fatty Acid Oxidation Mediated by CPT1A

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