Recombinant Mouse Long-chain-fatty-acid--CoA ligase 1 (Acsl1)
Description
Introduction to Recombinant Mouse Long-chain-fatty-acid--CoA ligase 1
Recombinant Mouse Long-chain-fatty-acid--CoA ligase 1 (Acsl1) is a bioengineered form of the naturally occurring enzyme that catalyzes the ATP-dependent activation of long-chain fatty acids. As a member of the ligase enzyme family (EC 6.2.1.3), Acsl1 plays a fundamental role in fatty acid metabolism by converting free fatty acids into their biologically active acyl-CoA derivatives . This activation represents an essential first step before fatty acids can participate in various metabolic pathways, including β-oxidation, phospholipid synthesis, and triacylglycerol formation. The recombinant version allows researchers to study the specific properties and functions of this enzyme in controlled laboratory conditions, providing valuable insights into its role in both normal physiology and disease states.
Molecular Properties
| Characteristic | Information |
|---|---|
| Enzyme Classification | EC 6.2.1.3 |
| Alternative Names | Acyl-CoA synthetase long-chain family member 1, FACL2 |
| Human Gene Location | Chromosome 4 q35 |
| Reaction Catalyzed | Long-chain fatty acid + ATP + CoA → Acyl-CoA + AMP + PPi |
| Subcellular Localization | Endoplasmic reticulum, outer mitochondrial membrane |
| Structure | Contains N-terminal transmembrane domain |
| Major Function | Catalyzes the pre-step reaction for β-oxidation of fatty acids |
The molecular structure of Acsl1 features a single N-terminal transmembrane domain that anchors it to either the endoplasmic reticulum or the outer mitochondrial membrane (OMM) . This strategic positioning is crucial for directing activated fatty acids toward specific metabolic pathways within the cell.
Enzymatic Activity
The primary function of Acsl1 is to catalyze the formation of fatty acyl-CoA through a two-step process that proceeds through an adenylated intermediate . This activation requires the energy from ATP hydrolysis, specifically using 2 "ATP equivalents" because the pyrophosphate (PPi) released is subsequently cleaved into 2 molecules of inorganic phosphate .
The general reaction catalyzed by Acsl1 can be represented as:
Long-chain fatty acid + ATP + CoA → Acyl-CoA + AMP + PPi
This activation is essential before fatty acids can participate in various metabolic pathways, particularly β-oxidation in mitochondria and peroxisomes.
Reaction Mechanism
Acsl1 operates through what is known as a "bi uni uni bi ping-pong" mechanism . This enzymatic terminology describes the precise sequence of substrate binding and product release:
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Two substrates (ATP and long-chain fatty acid) simultaneously enter the enzyme's active site
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The negatively charged oxygen on the fatty acid attacks the alpha phosphate on ATP, forming an ATP-long chain fatty acid intermediate
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Pyrophosphate (PPi) leaves, resulting in an AMP-long chain fatty acid molecule within the enzyme's active site
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Coenzyme A enters the enzyme and forms another intermediate consisting of AMP-long chain fatty acid-Coenzyme A
This sophisticated mechanism ensures the efficient transfer of energy from ATP to create the thioester bond in the resulting acyl-CoA product, preparing the fatty acid for subsequent metabolic reactions.
Direction of Fatty Acid Trafficking
Research with tissue-specific knockouts indicates that Acsl1 plays a critical role in directing fatty acids into the mitochondria for β-oxidation, particularly in adipose tissue . This channeling function represents a form of metabolic partitioning, where Acsl1 helps determine whether fatty acids are directed toward energy production through oxidation or storage in the form of complex lipids.
Impact on Fatty Acid Oxidation
Studies with Acsl1-deficient mouse models have demonstrated that this enzyme is essential for normal fatty acid oxidation in adipose tissue. In Acsl1 knockout adipocytes, the rate of [14C]oleate incorporation into CO2 and acid-soluble metabolites (products of fatty acid oxidation) was 50-90% lower than in control adipocytes . This dramatic reduction indicates that Acsl1 plays a non-redundant role in channeling fatty acids into the oxidative pathway.
Relationship to Triacylglycerol Synthesis
Interestingly, despite contributing 80% of total ACSL activity in adipose tissue, Acsl1 appears to be largely dispensable for triacylglycerol (TAG) synthesis. Studies show that adipocytes from Acsl1 knockout mice incorporated [14C]oleate into TAG and phospholipids at rates similar to control cells . This finding suggests that other ACSL isoforms can effectively compensate for the lack of Acsl1 in anabolic pathways, or that the remaining ACSL activity is sufficient for this purpose.
Metabolic Phenotype
Studies using recombinant mouse models have provided valuable insights into the function of Acsl1 in vivo. Contrary to initial expectations, mice lacking Acsl1 in adipose tissue (Acsl1 A−/−) did not exhibit lipodystrophy. Instead, these mice displayed:
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30% greater fat mass when fed a low-fat diet compared to control mice
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Approximately 40% larger gonadal fat depot weights when fed standard or low-fat diets
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Normal weight gain when fed a high-fat diet
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17% lower plasma triacylglycerol concentrations
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Similar plasma glucose, fatty acid, cholesterol, and insulin concentrations compared to wild-type mice
| Parameter | Wild-type Mice | Acsl1 A−/− Mice | % Difference |
|---|---|---|---|
| Fat Mass (Low-fat diet) | Baseline | 30% increase | +30% |
| Gonadal Fat Depot Weight | Baseline | 40% increase | +40% |
| Plasma TAG Concentration | Baseline | 17% decrease | -17% |
| FA Oxidation Rate in Adipocytes | Baseline | 50-90% decrease | -50 to -90% |
| TAG/PL Synthesis Rate | Baseline | No significant change | 0% |
This metabolic profile suggests that the increased adiposity in Acsl1 A−/− mice likely results from reduced fatty acid oxidation in adipose tissue rather than increased triglyceride synthesis or impaired lipolysis.
Thermogenesis and Cold Response
One of the most striking phenotypes of Acsl1 A−/− mice was their marked cold intolerance . These mice were unable to maintain normal body temperature when exposed to cold environments. Additionally, β3-adrenergic agonists, which normally stimulate thermogenesis, did not increase oxygen consumption in Acsl1 A−/− mice despite normal adrenergic signaling in brown adipose tissue .
In brown adipocytes from Acsl1 A−/− mice, glycerol release after adrenergic stimulation was reduced by approximately 50% compared to control cells . These findings indicate that while lipolysis itself might not be severely impaired, the utilization of freed fatty acids for thermogenesis was compromised, likely due to impaired fatty acid oxidation.
Impact on Adipose Tissue Composition
Despite the loss of 80% of ACSL activity in adipose tissue, several aspects of adipocyte morphology and function remained normal in Acsl1 A−/− mice:
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Adipocyte size and histology were similar to control mice
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Glycerol phosphate acyltransferase (GPAT) specific activity was unaffected
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AMP-activated protein kinase (AMPK) phosphorylation remained normal
Protein Interactions and Subcellular Localization
The specific subcellular localization and protein interactions of Acsl1 are crucial determinants of its metabolic functions. In liver, proteomics analyses have identified physical interactions between Acsl1, voltage-dependent anion channel (VDAC), and carnitine palmitoyltransferase-1 (CPT-1) in the outer mitochondrial membrane . This association may explain why Acsl1 deficiency impairs fatty acid oxidation, as it could be part of a protein complex that channels activated fatty acids directly to the mitochondrial transport machinery.
Several factors may contribute to the ability of Acsl1 to direct fatty acids toward synthetic pathways versus mitochondrial oxidation:
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Subcellular location - Acsl1 is anchored to either the ER or outer mitochondrial membrane
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Post-translational modifications - Phosphorylation and acetylation of specific amino acid residues may regulate its activity
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Protein-protein interactions - Specific interactions with other metabolic enzymes may influence substrate channeling
Researchers have employed techniques such as BioID proximity biotinylation to identify proteins that physically interact with Acsl1, providing insights into its functional networks and metabolic roles .
Role in Inflammatory Conditions
Research has revealed connections between Acsl1 and inflammatory processes. The enzyme is induced by lipopolysaccharide and inflammatory cytokines including IFN-gamma and TNF-alpha, and its increased expression is associated with the inflammatory activation of macrophages .
Acsl1 promotes membrane phospholipid turnover in activated macrophages, which might contribute to its inflammatory effects . This connection to membrane remodeling during inflammation highlights a function beyond basic fatty acid metabolism and suggests it may play a role in mediating cellular responses during inflammatory conditions.
Connection to Autoimmune Disorders
Studies have shown that Acsl1 expression is increased in both human systemic lupus erythematosus and murine models of lupus . Specifically, ACSL1 mRNA expression was significantly elevated in peripheral blood mononuclear cells of patients with lupus compared to matched controls, as well as in splenocytes obtained from the TLR7 transgenic mouse model of lupus .
Further investigation revealed that Acsl1 mRNA is induced 3-4 fold by type 1 interferon in thioglycollate-elicited macrophages and 6-7 fold in bone marrow-derived macrophages . This induction occurred concomitantly with increases in well-known interferon-stimulated genes, suggesting that Acsl1 may be part of the interferon signature characteristic of lupus and potentially other autoimmune disorders.
Research Applications and Future Directions
Recombinant mouse Acsl1 has proven invaluable for investigating the specific functions of this enzyme in lipid metabolism. The development of recombinant forms and tissue-specific knockout models has allowed researchers to:
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Elucidate the specific role of Acsl1 in directing fatty acids toward mitochondrial oxidation
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Demonstrate that other ACSL isoforms can compensate for Acsl1 in triacylglycerol synthesis
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Identify novel connections between Acsl1 and inflammatory processes
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Characterize the metabolic phenotype resulting from Acsl1 deficiency
Future research directions might include:
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More detailed characterization of the protein complexes involving Acsl1
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Investigation of the specific post-translational modifications that regulate its activity
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Exploration of its potential as a therapeutic target in metabolic or inflammatory diseases
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Further studies on its role in different tissues and cell types
Product Specs
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Target Background
- ACSL1-mediated metabolic trapping of exogenous LCFA accelerates LCFA uptake rates, albeit to a lesser extent in females. This distinctly affects LCFA trafficking to acyl intermediates but not triglyceride storage or mitochondrial oxidation. Notably, this process is influenced by female sex hormones. PMID: 26995156
- Research findings, including data from cell lines derived from knockout mice, suggest a significant role of long-chain fatty acid incorporation, partly mediated by ACSL1, in supplying octanoic acid for ghrelin acylation/lipoylation in ghrelin-producing cells. PMID: 26991015
- Acyl-CoA synthetase 1 deficiency alters cardiolipin species and impairs mitochondrial function. PMID: 26136511
- ACSL1 serves as a programmable mediator of insulin sensitivity and cellular lipid content. PMID: 25915184
- Long-chain acyl-CoA synthetase isoform 1 (ACSL1) deficiency in the heart activates mTORC1, inhibiting autophagy and increasing the number of damaged mitochondria. PMID: 26220174
- Acsl1(M-/-) mice exhibit increased insulin sensitivity. During an overnight fast, their respiratory exchange ratio is elevated, indicating greater glucose utilization. Notably, Acsl1(M-/-) mice exhibit reduced endurance during exercise, running only 48% as far as control mice. PMID: 25071025
- Research findings indicate that Acsl1-deficiency leads to diastolic dysfunction. Furthermore, mTOR activation is linked to the development of cardiac hypertrophy in Acsl1(H-/-) mice. PMID: 24631848
- Data suggest that ACSL1 expression levels and triglyceride levels are significantly increased in hepatitis B virus X protein (HBx)-induced liver cancer tissues from HBx transgenic mice models. PMID: 24462768
- Understanding the role of ACSL1 in monocytes/macrophages in inflammation and diabetes-accelerated atherosclerosis holds promise for developing new treatments to combat diabetic vascular disease. PMID: 23153419
- Acyl-CoA synthetase 1 is induced by Gram-negative bacteria and lipopolysaccharide. It is essential for phospholipid turnover in stimulated macrophages. PMID: 23426369
- Endothelial ACSL1 is not required for the inflammatory and apoptotic effects of a saturated fatty acid-rich environment. PMID: 23241406
- The reduced ABCA1 and cholesterol efflux in macrophages exposed to conditions of diabetes and elevated fatty load might be, at least partially, mediated by ACSL1. PMID: 22020260
- Acsl1 knockdown stimulated the expression of lipogenic genes. PMID: 22445754
- ACSL1 plays a crucial role in promoting the inflammatory phenotype of macrophages associated with type 1 diabetes. PMID: 22308341
- Acsl1 is essential for heart fatty acid oxidation. Heart-specific Acsl1 deficiency causes cardiac hypertrophy. PMID: 21245374
- Acsl1(A-/-) adipocytes exhibit normal [(14)C]oleate incorporation into glycerolipids. However, fatty acid oxidation rates are significantly reduced (50%-90%) compared to control adipocytes and mitochondria. PMID: 20620995
- O-GlcNAc disrupts a known interaction between Sp1 and sterol regulatory element binding protein 2 (SREBP2), inhibiting the expression of the gene encoding acetyl-CoA synthetase 1, which is involved in lipid synthesis. PMID: 20138838
- Normoleptinemic control ACS-transgenic mice develop severe dilated cardiomyopathy with thickened left ventricular walls and profound impairment of systolic function on echocardiogram. PMID: 15347805
- Research findings suggest that a constitutive interaction between FATP1 and ACSL1 contributes to the efficient cellular uptake of LCFAs in adipocytes through vectorial acylation. PMID: 16357361
- The primary role of ACSL1 in adipocytes is not in controlling lipid influx, as previously believed, but rather in lipid efflux and fatty acid-induced insulin resistance. PMID: 19429676
- ACSL1 acts as a cancer survival factor; its inhibition enhances the efficacy of etoposide. PMID: 19459852
- Research findings describe a knock-out model of acyl-CoA synthetase-1 (ACSL1) and its effects on liver and whole body metabolism. PMID: 19648649
Q&A
What is the fundamental role of ACSL1 in lipid metabolism?
ACSL1 catalyzes the conversion of long-chain fatty acids into acyl-CoA esters, a critical step enabling fatty acids to enter multiple metabolic pathways. This enzyme demonstrates high affinity for long-chain fatty acids with 16 to 20 carbon atoms, particularly palmitoleate, oleate, and linoleate . The activation of fatty acids by ACSL1 is essential for:
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Lipid biosynthesis pathways
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Fatty acid degradation via β-oxidation
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Energy production
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Cellular membrane maintenance
ACSL1's ability to channel fatty acids into different metabolic pathways depends on tissue type, metabolic state, and subcellular localization .
How is ACSL1 distributed across mouse tissues?
ACSL1 shows tissue-specific distribution patterns with significant expression in metabolically active tissues:
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Highest expression in heart, liver, and adipose tissue
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Moderate expression in mammary tissue (with implications for milk production)
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Present in skeletal muscle where it regulates fatty acid partitioning
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Expressed in renal tissue with potential implications in fibrotic pathways
ACSL1 is the most prevalent acyl-CoA synthetase in these primary tissues, highlighting its central role in tissue-specific lipid metabolism .
What are the structural characteristics of recombinant mouse ACSL1?
Recombinant full-length mouse ACSL1 has the following properties:
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Consists of 699 amino acids
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Can be expressed with N-terminal tags (commonly His-tag) to facilitate purification
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Full amino acid sequence available (MEVHELFRYFRMPELIDIRQYVRTLPTNTLMGFGAFAALTTFWYATRPKALKPPCDLSMQSVEIAGTTDGIRRSAVLEDDKLLVYY...)
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Functions as a homodimer based on bacterial ACSL1 crystal structure evidence
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Contains domains for ATP binding, fatty acid binding, and CoA binding
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Best expressed and stored in Tris/PBS-based buffer with 6% Trehalose at pH 8.0
How does ACSL1 overexpression affect lipid metabolism in different tissues?
ACSL1 overexpression produces tissue-specific effects on lipid metabolism:
These tissue-specific effects demonstrate the multi-faceted role of ACSL1 in directing fatty acid metabolism based on cellular context .
What protein interactions govern ACSL1's role in fatty acid metabolism?
BioID proteomic analysis identified distinct protein interaction networks:
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98 proteins specifically interact with ACSL1 at the endoplasmic reticulum (ER)
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55 proteins interact with ACSL1 at the outer mitochondrial membrane (OMM)
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43 proteins interact with ACSL1 at both subcellular locations
Key interaction partners include:
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Peroxisomal proteins (ACBD5, VAPB)
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Lipid droplet proteins
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Tethering and vesicle proteins
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Other ACSL isoforms (ACSL5, ACSL6)
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Ceramide synthase isoforms 2 and 5
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Fatty aldehyde dehydrogenase (ALDH3A2)
These interactions create a complex network that determines ACSL1's role in directing fatty acids to specific metabolic fates .
How does ACSL1 influence triglyceride synthesis and storage?
ACSL1 plays a critical role in triglyceride metabolism, though its effects vary by experimental system:
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In cardiac tissue: Overexpression increases triglyceride content 12-fold
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In adipocytes: Expression increases 4-fold during differentiation, promoting triglyceride synthesis
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In mammary epithelial cells: Knockdown significantly reduces lipid droplet formation (measured by BODIPY staining)
Research demonstrates that:
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ACSL1 knockdown in mammary epithelial cells significantly reduces triglyceride concentration
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ACSL1 overexpression increases triglyceride synthesis
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These effects are accompanied by changes in expression of lipogenic genes
The data suggests ACSL1 is a potential target for modulating triglyceride storage in various tissues .
What is ACSL1's role in diabetic kidney disease pathogenesis?
ACSL1 has emerged as a potential target for treating renal fibrosis in diabetic kidney disease:
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Proteomics analysis identified ACSL1 as differentially expressed in diabetic nephropathy
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ACSL1 expression in urine of diabetic nephropathy patients was verified by Western blot and ELISA
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Studies using db/db mice (model for diabetic nephropathy) confirmed association between renal fibrosis and ACSL1 expression
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Knocking down ACSL1 in cell experiments demonstrated a relationship between ACSL1 and renal fibrosis
This suggests ACSL1 may be a novel therapeutic target for preventing or treating diabetic kidney disease progression .
How does ACSL1 influence cardiac function under pathological stress?
Cardiac ACSL1 overexpression provides protection against transverse aortic constriction (TAC)-induced dysfunction:
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Mitigates TAC-induced cardiac hypertrophy (26% vs. 46% increase in heart weight in ACSL1 mice vs. controls)
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Preserves ejection fraction (65.8±7.5% in ACSL1 TAC vs. 45.9±7.3% in control TAC)
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Improves diastolic function (E/E' ratio)
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Accelerates LCFA uptake, preventing C16 acyl-CoA loss post-TAC
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Alters ceramide profiles: decreases cardiotoxic C16/C24/C24:1 ceramides while increasing cardioprotective C20/C22 ceramides
These findings suggest that ACSL1-mediated changes in cardiac lipid metabolism may be protective during pathological stress .
What are optimal conditions for expressing and storing recombinant mouse ACSL1?
Based on established protocols for recombinant ACSL1 expression:
Expression System:
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E. coli expression system with N-terminal His-tag for purification
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Full-length protein (amino acids 1-699) can be successfully expressed
Storage Conditions:
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Store lyophilized powder at -20°C/-80°C
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Reconstitute in deionized sterile water to 0.1-1.0 mg/mL
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Add 5-50% glycerol (final concentration) for long-term storage
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Default recommended glycerol concentration is 50%
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Store working aliquots at 4°C for up to one week
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Avoid repeated freeze-thaw cycles
Buffer Composition:
What techniques are effective for manipulating ACSL1 expression in experimental models?
Several techniques have proven successful for altering ACSL1 expression:
For Knockdown Studies:
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siRNA transfection: shACSL1-297 (sequence: GGGCATACAGGTGTCCAATAA) has been validated
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Transfection using FuGENE or similar reagents
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Efficiency verification by qRT-PCR (90% reduction in mRNA) and Western blot (51% reduction in protein)
For Overexpression Studies:
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pcDNA3.1-ACSL1 plasmid transfection
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Adenovirus-mediated overexpression for in vivo studies
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Tissue-specific promoters (e.g., MHC promoter for cardiac-specific expression)
Animal Models:
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Tissue-specific ACSL1 knockout mice (e.g., Acsl1L−/− for liver-specific knockout)
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Tissue-specific ACSL1 overexpression mice (e.g., MHC-ACSL1 for cardiac-specific overexpression)
How can researchers assess ACSL1's impact on cellular lipid metabolism?
Multiple complementary approaches can be used:
Lipid Droplet Visualization:
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BODIPY staining (green) with DAPI nuclear counterstain (blue)
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Quantification of fluorescent signal density
Triglyceride Analysis:
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Triglyceride concentration measurement in cell lysates
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Normalization to control samples
Gene Expression Analysis:
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qRT-PCR for lipid metabolism-related genes
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GAPDH as internal control
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Focus on genes involved in lipogenesis and fatty acid oxidation
Functional Assays:
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Fatty acid uptake measurement using isotope-labeled fatty acids
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β-oxidation assays
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Acyl-CoA measurements by LC-MS/MS
What methods can detect ACSL1 protein-protein interactions?
BioID has proven effective for identifying ACSL1 protein interactors:
BioID Technique Implementation:
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Generate fusion protein of ACSL1 with E. coli biotin ligase (BirA*)
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Target the fusion protein to specific subcellular locations (ER or OMM)
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The biotin ligase biotinylates proteins in close proximity to ACSL1
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Isolate biotinylated proteins using streptavidin
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Identify interacting proteins through mass spectrometry
This approach has successfully identified distinct sets of ACSL1-interacting proteins at the ER versus the OMM, providing insights into the protein networks that control fatty acid metabolism .
Other validated methods include:
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Co-immunoprecipitation followed by Western blotting
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Proximity ligation assays
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FRET/BRET for dynamic interaction studies
How can researchers investigate ACSL1's role in disease models?
Researchers have employed several disease models to study ACSL1:
Diabetic Nephropathy Model:
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db/db mice (Lep db/Lep db on C57BLKS/J background)
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Age: 7-24 weeks
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Parameters measured: renal function, ACSL1 expression in kidney tissues, fibrotic markers
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Techniques: Periodic acid-Schiff (PAS) staining, Masson staining, immunostaining
Cardiac Stress Model:
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Transverse aortic constriction (TAC) in ACSL1-overexpressing mice
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Serial echocardiography for 14 weeks
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Isolated heart perfusion with 13C-labeled fatty acids
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Dynamic-mode 13C nuclear magnetic resonance and mass spectrometry analysis
Cellular Models:
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MAC-T mammary epithelial cells with ACSL1 knockdown or overexpression
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Measurements: cell viability, proliferation, apoptosis, lipid metabolism
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Techniques: CCK-8 assays, flow cytometry, BODIPY staining, ELISA for milk proteins
These models have provided valuable insights into ACSL1's role in disease pathogenesis and potential therapeutic applications.
How do ACSL1 genetic variants influence metabolic disease risk?
Genetic association studies have revealed connections between ACSL1 variants and metabolic traits:
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SNPs within the ACSL1 gene region have been associated with fasting glucose levels and type 2 diabetes in large-scale consortia studies (MAGIC, DIAGRAM)
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Specific ACSL1 variants may function as expression quantitative trait loci (eQTLs), affecting ACSL1 expression levels
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The MuTHER consortium data has been used to investigate if ACSL1 SNPs are associated with ACSL1 expression levels in multiple tissues
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CARDIoGRAMplusC4D consortium studies have examined associations between ACSL1 variants and cardiovascular disease risk
These genetic associations suggest ACSL1 may be an important contributor to metabolic disease pathogenesis, though more research is needed to establish causality and mechanisms.
What is the relationship between ACSL1 and immune function?
Emerging research reveals ACSL1's role in immune responses:
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ACSL1 can inhibit viral replication (demonstrated with ALV-J virus) through IFN-I signaling and PI3K/Akt pathway
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ACSL1 overexpression in macrophages increases levels of pro-inflammatory cytokines IL-1β and IL-18
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ACSL1 enhances production of nitric oxide (NO) and inducible nitric oxide synthase (iNOS)
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ACSL1 knockdown affects ATP levels and mitochondrial membrane potential (JC1) in macrophages
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ACSL1 can trigger apoptosis through the PI3K/Akt signaling pathway
These findings suggest ACSL1 may be a previously unrecognized regulator of inflammation and immune responses, opening new avenues for research into metabolic inflammation.
How do ACSL1 transcript variants differ in their metabolic functions?
ACSL1 exhibits transcript diversity with functional implications:
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The ACSL1 gene contains multiple promoters, resulting in multiple transcripts with distinct functions
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Alternative polyadenylation (APA) can produce transcripts with varying 3'UTR lengths or transcripts encoding different proteins
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Different ACSL1 transcripts may be responsible for various roles in triglyceride synthesis
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Transcript variants show tissue-specific expression patterns
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The subcellular targeting of ACSL1 protein isoforms may be affected by transcript variation
Understanding the functional differences between ACSL1 transcript variants could provide insights into tissue-specific roles of ACSL1 in lipid metabolism and disease.
