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Lipoprotein Lipase

Lipoprotein Lipase: An Enzyme Essential for Lipid Metabolism.
Lipoprotein lipase (LPL) is a key enzyme involved in the hydrolysis of triglycerides in lipoproteins, enabling the uptake and utilization of fatty acids by tissues.
It plays a crucial role in regulating blood lipid levels and energy homeostasis.
LPL deficiency can lead to hypertriglyceridemia and other metabolic disorders.
Reserach on LPL is crucial for understanding lipid metabolism and developing therapies for related conditions.
PubCompare.ai's platform streamlines LPL resarch by providing AI-driven access to the latest protocols, pre-prints, and patents, facilitating the identification of optimal experimental approaches.

Most cited protocols related to «Lipoprotein Lipase»

1
Quantifying Triglycerides in Insect Metabolics
Cited 17 times

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Publication 2014
Adult Biological Assay Carbohydrates Colorimetry Diacylglycerol Fatty Acids Fractionation, Chemical Glycerin Insecta Lipids Lipoprotein Lipase Patient Discharge Pigmentation Proteins Thin Layer Chromatography Triglycerides
2
Quantifying HIV-1 DNA in Purified Lymphoid Cells
Cited 15 times
Lysed extracts from purified LPLs (CD45+ cells), bulk LPs and PBMCs from the same participants were simultaneously obtained and used to measure cell-associated HIV-1 DNA by ddPCR. A total of 2–3 μl of cell lysates were mixed with ddPCR supermix and primers/probes (FAM/HEX-ZEN-Iowa BlackFQ double-quenched probes, Integrated DNA Technologies) in a total volume of 20 μl to generate droplets, according to manufacturer’s recommendations. We managed to circumvent potential primer mismatch in individuals’ viral sequence by using two different primers/probe sets annealing to the 5’LTR and GAG conserved regions of HIV-1 genome [21 (link)–23 (link)] (Table 1). Here, ddPCR Supermix for Residual DNA quantification was used (186–4037, Bio-Rad). Annealing/extension step was set at 57°C to quantify vDNA using the C1000 Touch™ Thermal Cycler (Bio-Rad) and subsequently analyzed using a QX100™ droplet reader (Bio-Rad) and the QuantaSoft v.1.6 software (Bio-Rad).
PBMCs, bulk LPs and LPLs samples were quantified in duplicate or triplicate, respectively. PBMCs from HIV-negative donors were used as negative controls and assayed in each plate to set the positive/negative threshold for ddPCR analysis, and the number of those negative control wells was the same than replicas for each sample. The RPP30 cellular gene was quantified in parallel to normalize sample input (Table 1) [24 (link)].
Morón-López S., Puertas M.C., Gálvez C., Navarro J., Carrasco A., Esteve M., Manyé J., Crespo M., Salgado M, & Martinez-Picado J. (2017). Sensitive quantification of the HIV-1 reservoir in gut-associated lymphoid tissue. PLoS ONE, 12(4), e0175899.
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Publication 2017
Cells Dietary Fiber Donors Genes Genome HIV-1 Lipoprotein Lipase Oligonucleotide Primers Touch
3
Intestinal Epithelial and Lamina Propria Isolation
Cited 13 times
Intestinal samples (6–10 cm long pieces of jejunum and colon) were collected in 50 ml tubes with ice-cold calcium and magnesium free HBSS (Fisher Scientific) and immediately transported to the laboratory. Fat, blood vessels, and mesenteric lymph nodes were trimmed. Mucus and gross debris were quickly removed by covering the specimen with dry paper towels. Specimens were further washed twice in cold PBS (pH 7.4). Intestinal samples were cut into small pieces (approximately 0.5–1 cm2).
All isolation protocols were performed on tissues from necropsied animals to maintain consistency of protocols compared to biopsy protocols where techniques may result in different proportions of ECs in samples. In brief, tissues were treated in 2 major ways. In one technique, the intestinal EC were separated from intestinal pieces by incubating 0.5–1 cm2 pieces of tissue in Dithriothreitol (0.15%, DTT, EMD Chemicals) (Fig. 1) [21] (link) followed by EDTA with shaking at 37°C. In another protocol, minced tissues were directly treated with EDTA solution (Fig. 2) as reported earlier [53] (link), [81] (link). Mucus and large debris were removed from the supernatant by filtering through loosely packed glass wool. After epithelial removal, LPL were collected by mincing the remaining tissue into 1–2 mm pieces, followed by digestion in complete RPMI-5 medium containing 5% fetal calf serum (FCS) (RPMI-5) containing 60 units/ml of Type II collagenase (Sigma-Aldrich) again with shaking at 37°C. For enrichment of lymphocytes, supernatants of LPLs were centrifuged over discontinuous Percoll (Sigma-Aldrich) density gradients followed by washing with PBS [53] (link), [81] (link). All isolated cells were washed twice and resuspended in complete RPMI-10 medium containing 10% FCS before staining. All cells were >90% viable by trypan blue dye exclusion method.
Pan D., Das A., Liu D., Veazey R.S, & Pahar B. (2012). Isolation and Characterization of Intestinal Epithelial Cells from Normal and SIV-Infected Rhesus Macaques. PLoS ONE, 7(1), e30247.
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Publication 2012
Animals Biopsy Blood Vessel Calcium Cells Collagenase Colon Common Cold Digestion Edetic Acid Fetal Bovine Serum Hemoglobin, Sickle Intestines Jejunum Lipoprotein Lipase Lymphocyte Magnesium Mesentery Mucus mutalipocin II Nodes, Lymph Percoll Tissues Trypan Blue
4
Quantitative Analysis of Chondrogenic and Osteogenic Markers
Cited 7 times
Total cellular RNA was extracted from the cultures by using the RNeasy Protect Mini Kit with an on-column RNase-free DNase treatment (Qiagen, Hilden, Germany) [16 (link),37 (link),46 (link)]. RNA was eluted in 30 μl RNase-free water. Reverse transcription was carried out with 8 μl of eluate by using the 1st Strand cDNA Synthesis kit for RT-PCR (AMV) (Roche Applied Science). An aliquot of the cDNA product (2 μl) was amplified with real-time PCR by using the Brilliant SYBR Green QPCR Master Mix (Stratagene, Agilent Technologies, Waldbronn, Germany) [16 (link)] on an Mx3000P QPCR operator system (Stratagene) as follows: (95°C, 10 minutes), amplification by 40 cycles (denaturation at 95°C, 30 seconds; annealing at 55°C, 1 minute; extension at 72°C, 30 seconds), denaturation (95°C, 1 minute), and final incubation (55°C, 30 seconds). The primers (Invitrogen GmbH) used were SOX9 (chondrogenic marker) (forward 5'-ACACACAGCTCACTCGACCTTG-3'; reverse 5'-GGGAATTCTGGTTGGTCCTCT-3'), type II collagen (COL2A1) (chondrogenic marker) (forward 5'-GGACTTTTCTCCCCTCTCT-3'; reverse 5'-GACCCGAAGGTCTTACAGGA-3'), type I collagen (COL1A1) (osteogenic marker) (forward 5'-ACGTCCTGGTGAAGTTGGTC-3'; reverse 5'-ACCAGGGAAGCCTCTCTCTC-3'), type X collagen (COL10A1) (marker of hypertrophy) (forward 5'-CCCTCTTGTTAGTGCCAACC-3'; reverse 5'-AGATTCCAGTCCTTGGGTCA-3'), alkaline phosphatase (ALP) (osteogenic marker) (forward 5'-TGGAGCTTCAGAAGCTCAACACCA-3'; reverse 5'-ATCTCGTTGTCTGAGTACCAGTCC-3'), matrix metalloproteinase 13 (MMP13) (marker of terminal differentiation) (forward 5'-AATTTTCACTTTTGGCAATGA-3'; reverse 5'-CAAATAATTTATGAAAAAGGGATGC-3'), osteopontin (OP) (osteogenic marker) (forward 5'-ACGCCGACCAAGGAAAACTC-3'; reverse 5'-GTCCATAAACCACACTATCACCTCG-3'), runt-related transcription factor 2 (RUNX2) (osteogenic marker) (forward 5'-GCAGTTCCCAAGCATTTCAT-3'; reverse 5'-CACTCTGGCTTTGGGAAGAG-3'), β-catenin (mediator of the Wnt signaling pathway for osteoblast lineage differentiation) (forward 5'-CAAGTGGGTGGTATAGAGG-3'; reverse 5'-GCGGGACAAAGGGCAAGA-3'), parathyroid hormone-related protein (PTHrP) (hypertrophy-associated gene) (forward 5'-CGACGACACACGCACTTGAAAC-3'; reverse 5'-CGACGCTCCACTGCTGAACC-3'), lipoprotein lipase (LPL) (adipogenic marker) (forward 5'-GAGATTTCTCTGTATGGCACC-3'; reverse 5'-CTGCAAATGAGACACTTTCTC-3'), peroxisome proliferator-activated receptor gamma 2 (PPARG2) (adipogenic marker) (forward 5'-GCTGTTATGGGTGAAACTCTG-3'; reverse 5'-ATAAGGTGGAGATGCAGGCTC-3'), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (housekeeping gene and internal control) (forward 5'-GAAGGTGAAGGTCGGAGTC-3'; reverse 5'-GAAGATGGTGATGGGATTTC-3') (all 150 nM final concentration) [13 (link),15 (link),16 (link),46 (link)-49 (link)]. Control conditions included reactions using water and non-reverse-transcribed mRNA. Specificity of the products was confirmed by melting curve analysis and agarose gel electrophoresis. The threshold cycle (Ct) value for each gene of interest was measured for each amplified sample by using the MxPro QPCR software (Stratagene), and values were normalized to GAPDH expression by using the 2-ΔΔCt method, as previously described [16 (link)].
Venkatesan J.K., Ekici M., Madry H., Schmitt G., Kohn D, & Cucchiarini M. (2012). SOX9 gene transfer via safe, stable, replication-defective recombinant adeno-associated virus vectors as a novel, powerful tool to enhance the chondrogenic potential of human mesenchymal stem cells. Stem Cell Research & Therapy, 3(3), 22.
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Publication 2012
Adipogenesis Alkaline Phosphatase Anabolism beta-Catenin brilliant green Cells Chondrogenesis Collagen Type I Collagen Type II Collagen Type X Deoxyribonuclease I Differentiation Antigens DNA, Complementary Electrophoresis, Agar Gel Endoribonucleases Genes Genes, Housekeeping Glyceraldehyde-3-Phosphate Dehydrogenases Hypertrophy Lipoprotein Lipase Matrix Metalloproteinase 13 Neoplasm Metastasis Oligonucleotide Primers Osteoblasts Osteogenesis Osteopontin PPAR gamma PTHLH protein, human Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction Reverse Transcription RNA, Messenger RUNX2 protein, human SOX9 protein, human Training Programs Wnt Signaling Pathway
5
Cannabinoid Modulation of GABAergic Transmission
Cited 7 times
The cells were voltage clamped at −70 mV holding potential. Pipette offset potential, series resistance (Rs), and capacitance were compensated before recording. Only cells with low holding current (<50 pA) and stable baseline were used. Input resistance (Rin), Rs, and membrane capacity (Cm) were also measured before each recording by using 5-mV hyperpolarizing pulses. To ensure consistent recording qualities, only cells with Rs < 20 MΩ, Rin > 500 MΩ, and Cm > 10 pF were accepted. Further, if these values changed by more than 20% during measurements, the recordings were discarded (35 ). The pipette solution contained (in mm): HEPES 10, KCl 140, EGTA 5, CaCl2 0.1, Mg-ATP 4, and Na-GTP 0.4 (pH 7.3 with NaOH). The resistance of the patch electrodes was 2–3 MΩ. Spike-mediated transmitter release was blocked in all experiments by adding the voltage-sensitive Na-channel inhibitor tetrodotoxin (TTX) (750 nm; Tocris) to the aCSF 10 min before control miniature postsynaptic currents (mPSCs) were recorded. Picrotoxin (100 μm; Sigma, St. Louis, MO) was used in the aCSF to verify that mPSCs were related to GABAA-R activation. In subsequent experiments, modulation of mPSCs by CB1 was addressed by treating slices with the CB1 agonist WIN55,212 (1 μm; Tocris) for 10 min. In other experiments, slices were incubated with the CB1 antagonist AM251 (1 μm; Tocris) for 10 min and recorded. Then WIN55,212 (1 μm) was added and recording repeated after 10 min. Finally, the source of endogenous cannabinoids that regulate GABAergic afferents to GnRH neurons was investigated: the diacylglycerol (DAG) lipase inhibitor tetrahydrolipstatin (THL) was added to the intracellular solution at 10 μm to block 2-AG synthesis. To minimize THL spill, the GnRH cells were approached rapidly (<1 min), and the flow rate of aCSF was increased from 5–6 to 8–9 ml/min. Just before release of the positive pressure in the pipette, the flow rate was restored to 5–6 ml/min to avoid any mechanical movement of the slice. The pipette solution containing THL was allowed to equilibrate with the intracellular milieu of the cell for 25 min before control recording. Then AM251 was added for 10 min and recording repeated.
Farkas I., Kalló I., Deli L., Vida B., Hrabovszky E., Fekete C., Moenter S.M., Watanabe M, & Liposits Z. (2010). Retrograde Endocannabinoid Signaling Reduces GABAergic Synaptic Transmission to Gonadotropin-Releasing Hormone Neurons. Endocrinology, 151(12), 5818-5829.
Publication 2010
AM 251 Anabolism Cardiac Arrest Cells Egtazic Acid Endocannabinoids Gonadorelin HEPES Lipoprotein Lipase Movement Neuron, Afferent Orlistat Picrotoxin Postsynaptic Current Pressure Protoplasm Pulses Tetrodotoxin Tissue, Membrane

Most recents protocols related to «Lipoprotein Lipase»

1
Lipid Absorption Assay in Mice

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Publication 2023
Biological Assay Body Weight Corn oil Lipids Lipoprotein Lipase Lipoproteins Liquid Chromatography Mice, House Nonesterified Fatty Acids Plasma Plasma Proteins Tail Triglycerides tyloxapol Veins
2
Metabolic Profiling in Murine Obesity Models

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Publication 2023
Animals Biological Assay BLOOD Blood Glucose Body Weight Centrifugation Cholesterol Cold Temperature Diet Duodenum Enzymes Feces Formalin Freezing Glucose Glucose Tolerance Test Ileum Institutional Animal Care and Use Committees Intestines, Small Jejunum Lipase Lipids Lipoprotein (a) Lipoprotein Lipase Mice, House Nitrogen Nonesterified Fatty Acids pathogenesis Plasma Protocol Compliance Therapy, Diet Tissues Triglycerides
3
Characterization of Murine Lymphocyte Subsets
IELs and LPLs were passed through a 40-um cell strainer to a obtain single-cell suspension. A single-cell suspension was stimulated with PMA (50 ng/ml) and ionomycin (500 ng/ml) and incubated with brefeldin A (5 ug/ml) for 5 h, followed by staining for intracellular cytokines and surface markers. Exclusion of dead cells was performed with LIVE/DEAD Fixable Zombie Dead Cell Stain Kit (BioLegend). All cell preparations were Fc-blocked by CD16/32 antibody (BioLegend) prior to staining. Cell surface staining was performed with PerCP/Cy5.5 anti-mouse CD8α, FITC anti-mouse CD3, BV510 anti-mouse CD4, APC anti-mouse CD103, PE anti-mouse CD69 antibody and BV421 anti-mouse CD62L antibody (all from BioLegend). For detection of intracellular cytokines, cells were fixed in 4% PFA and permeabilized with BD perm/wash™ (BD Biosciences), followed by staining with Bv421 anti-mouse TNF-αand AF647 anti- mouse IFN-γ (BioLegend). Flow cytometric analysis was performed on an LSR Fortessa, and cell results were acquired using Diva software (BD Biosciences) and analyzed with FlowJo software. Sorting was performed on an Aria SORP high-speed cell sorter (BD Biosciences).
Shi F., Zhang S., Zhang N., Yu Y., Sun P., Tang X., Liu X, & Suo X. (2023). Tissue-resident, memory CD8+ T cells are effective in clearing intestinal Eimeria falciformis reinfection in mice. Frontiers in Immunology, 14, 1128637.
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Publication 2023
Alexa Fluor 647 alpha HML-1 Antibodies, Anti-Idiotypic Brefeldin A Cells CY5.5 cyanine dye Cytokine Flow Cytometry Fluorescein-5-isothiocyanate IFNG protein, mouse Ionomycin Lipoprotein Lipase Muromonab-CD3 Mus NRG1 protein, human Progressive Encephalomyelitis with Rigidity Protoplasm SELL protein, human Stains
4
Isolation of Intestinal Lymphocyte Subsets
Cecum samples were first freed from residual fat tissue, Peyer’s patches, feces and then cut into smaller pieces and incubated in Hanks’ Balanced Salt Solution with 2% FCS, 5 mM of EDTA and 2 mM of dithiothreitol for 30 min at 37°C and vortexed. The inter-epithelial lymphocytes (IEL) fraction was dissected by filtering over a 70 μm cell strainer. To recover the lamina propria lymphocytes (LPL) fraction, IEL-depleted intestine pieces were washed in Hanks’ Balanced Salt Solution supplemented with 2% FCS and enzymatically digested for 45 min at 37°C with Collagenase type IV (Solarbio), Neutral protease and DNase I (Solarbio) in 1640 medium. Single-cell suspensions were generated by filtering over a 70-μm cell strainer. The IELs and LPLs were purified by density centrifugation on a 67% and 44% percoll gradient (Cytiva).
Shi F., Zhang S., Zhang N., Yu Y., Sun P., Tang X., Liu X, & Suo X. (2023). Tissue-resident, memory CD8+ T cells are effective in clearing intestinal Eimeria falciformis reinfection in mice. Frontiers in Immunology, 14, 1128637.
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Publication 2023
Cecum Cells Centrifugation Deoxyribonuclease I Dithiothreitol Edetic Acid Feces Hanks Balanced Salt Solution Intestines Lamina Propria Lipoprotein Lipase Lymphocyte Matrix Metalloproteinase 2 Neprilysin Percoll Peyer Patches Tissue, Adipose
5
Serum Lipid and NEFA Measurement Protocol
AS described in our previous study [16 (link)], the venous blood was placed at room temperature for three hours, then it was centrifuged by 3000× g for 20 min at 4 °C to obtain serum samples. The serum samples were sent to Servicebio (Wuhan, China). A biochemical analyzer (Chemray 240, Rayto Life and Analytical Sciences Co., Ltd. Shenzhen, China) with the corresponding reagent (Huili Biology, Changchun, China) was used to measure the serum triglyceride (TG), total cholesterol (TC), high-density lipoprotein cholesterol (HDL-C), and low-density lipoprotein cholesterol (LDL-C).
In the presence of cholesterol hydrolase, cholesterol is hydrolyzed into fatty acids, which are then further oxidized to produce hydrogen peroxide. The Trinder reaction was used to detect hydrogen peroxide concentrations. Calculated using the formula, the TC concentration was determined by comparing the hydrogen peroxide concentration in the cholesterol standard solution to the hydrogen peroxide concentration in the serum. To remove free glycerol from the serum, glycerol kinase was applied. Hydrogen peroxide was produced by breaking down TG with lipoprotein lipase. Follow-up tests were consistent with cholesterol testing methods. Phosphotungstic acid-magnesium reagents were needed to precipitate apoB-containing lipoproteins, and HDL-C was measured from the supernatant. The detection principle was the same as cholesterol. Sulfated polyethylene was used to precipitate and disperse LDL-C, then it was calculated by subtracting the cholesterol in the supernatant without LDL-C from the total cholesterol.
Serum NEFAs were determined using commercial assay kits according to the instructions (Nanjing Jiancheng Bioengineering Institute, Nanjing, China). Acetyl-CoA synthase catalyzed the production of hydrogen peroxide from NEFA. It was consistent with the above method of detecting hydrogen peroxide. All the detection methods were recommended by the Chinese Medical Association.
Wang D.X., Qing S.L., Miao Z.W., Luo H.Y., Tian J.S., Zhang X.P., Wang S.N., Zhang T.G, & Miao C.Y. (2023). Hepatic Nampt Deficiency Aggravates Dyslipidemia and Fatty Liver in High Fat Diet Fed Mice. Cells, 12(4), 568.
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Publication 2023
APOB protein, human Biological Assay Chinese Cholesterol Cholesterol, beta-Lipoprotein Coenzyme A, Acetyl Fatty Acids Glycerin Glycerol Kinase High Density Lipoprotein Cholesterol Hydrolase Lipase Lipoprotein Lipase Lipoproteins lipoprotein triglyceride Magnesium Nitric Oxide Synthase Nonesterified Fatty Acids Peroxide, Hydrogen Phosphotungstic Acid Polyethylene, High-Density Serum Triglycerides Veins

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More about "Lipoprotein Lipase"

Lipoprotein lipase (LPL) is a crucial enzyme involved in lipid metabolism and energy homeostasis.
It plays a key role in the hydrolysis of triglycerides in lipoproteins, enabling the uptake and utilization of fatty acids by tissues.
LPL deficiency can lead to hypertriglyceridemia and other metabolic disorders.
Resarch on LPL is crucial for understanding lipid metabolism and developing therapies for related conditions.
LPL is also known as triglyceride lipase, clearing factor lipase, and post-heparin plasma lipase.
It is produced by various tissues, including adipose, muscle, and heart.
The enzyme acts on chylomicrons and very low-density lipoproteins (VLDLs), breaking down their triglyceride content and allowing the uptake of fatty acids by cells.
Experimental techniques used in LPL research include the use of DNase I, Ionomycin, Percoll, TRIzol reagent, PMA, Brefeldin A, TRIzol, Collagenase D, and Tyloxapol.
These methods are used for cell isolation, RNA extraction, enzyme activity assays, and protein purification, among other applications.
Undertsanding the role of LPL and its regulation is crucial for developing therapies for conditions like hypertriglyceridemia, obesity, and cardiovascular disease.
PubCompare.ai's platform streamlines LPL research by providing AI-driven access to the latest protocols, pre-prints, and patents, facilitating the identification of optimal experimental approaches.