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the negatively charged IDR of GPIHBP1 (Montrer GPIHBP1 Protéines) traverses a vast space, facilitating capture of LPL (Montrer LCP1 Protéines) by capillary endothelial cells and simultaneously contributing to GPIHBP1 (Montrer GPIHBP1 Protéines)'s ability to preserve LPL (Montrer LCP1 Protéines) structure and activity.
nder optimal conditions, the electrochemical DNA biosensor exhibited desirable performance for the determination of rs1801177 (of the lipoprotein lipase )with a wide linearity ranging from 10 fM to 10nM and a relatively low detection limit of 3.33 fM (S/N=3).
A link between the expression of LPL (Montrer LCP1 Protéines) in the tumor cells and a poor clinical outcome of patients suffering chronic lymphocytic leukemia has been established. (Review)
When her TG levels normalized after incidental use of prednisone, an autoimmune mechanism was suspected. Immunoblot analyses showed the presence of autoantibodies to LPL (Montrer LCP1 Protéines) in the patient's plasma. Autoantibodies to LPL (Montrer LCP1 Protéines) decreased by 37% while patient was on prednisone, and by 68% as she subsequently transitioned to hydroxychloroquine monotherapy
Updated LPL (Montrer LCP1 Protéines) structural models were generated by combining disulfide mapping, computational modeling, and data derived from single-molecule Forster resonance energy transfer. New computational suggest that LPL (Montrer LCP1 Protéines) may dimerize using an interface that is different from the dimerization interface suggested by crystal packing contacts seen in structures of pancreatic lipase (Montrer PNLIP Protéines).
This meta-analysis suggested that LPL (Montrer LCP1 Protéines) HindIII variants were associated with a decreased risk of stroke in the Asian population, but not in the non-Asian population.
LPL (Montrer LCP1 Protéines) HindIII (+/-) and PvuII (+/-), but not the Ser447Ter, might significantly reduce the risk of ischemic stroke.
apoC-III (Montrer APOC3 Protéines) potently inhibits triglyceride hydrolysis when LPL (Montrer LCP1 Protéines) is bound to GPIHBP1 (Montrer GPIHBP1 Protéines)
The results of this meta-analysis suggested that the LPL (Montrer LCP1 Protéines) S447X polymorphism is likely to be a protective factor in the development of hypertension.
Sequence variation in Kuwaiti Arabs was compared to other populations and was found to be similar with regards to the number of SNPs, InDels and distribution of the number of variants across the LPL (Montrer LCP1 Protéines) gene locus and minor allele frequency
isothermal titration calorimetry (ITC) can be used for quantitative measurements of LPL activity and interactions under in vivo-like conditions, for comparisons of the properties of plasma samples from patients and control subjects as substrates for LPL, as well as for testing of drug candidates developed with the aim to affect the LPL system.
miR (Montrer MYLIP Protéines)-29b targets LPL and TDG (Montrer TDG Protéines) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
apoC-I (Montrer APOC1 Protéines) and apoC-III (Montrer APOC3 Protéines) inhibit lipolysis by displacing LPL from lipid emulsion particles. We also propose a role for these apolipoproteins in the irreversible inactivation of LPL by factors such as angptl4 (Montrer ANGPTL4 Protéines).
ANGPTL4 (Montrer ANGPTL4 Protéines) is more accurately described as a reversible, noncompetitive inhibitor of LPL.
Our findings confirmed that three novel SNPs we identified in the LPL gene can affect fatty acid composition and carcass traits. Therefore, selection for AA and GA genotypes should be recommended to genetically improve beef quality and flavor.
Single nucleotide polymorphisms of the LPL gene might be useful genetic markers for growth traits in the bovine reproduction and breeding.
Results describe the functional role of the secondary structure in the lipoprotein lipase-binding portion of apolipoprotein CII (Montrer APOC2 Protéines).
regions that are responsive to activation by apoC-II (Montrer APOC2 Protéines)
domain (192-238) is absolutely necessary for apolipoprotein AV (Montrer APOA5 Protéines) in lipid binding and lipoprotein lipase activation
the negatively charged IDR of GPIHBP1 (Montrer GPIHBP1 Protéines) traverses a vast space, facilitating capture of LPL by capillary endothelial cells and simultaneously contributing to GPIHBP1 (Montrer GPIHBP1 Protéines)'s ability to preserve LPL structure and activity.
LPL in the hypothalamus is an important regulator of body weight and glucose homeostasis
These results identify LPL as an important regulator of fatty acid transport to skeletal compartments and demonstrate an intricate functional link between systemic and skeletal fatty acid and glucose metabolism.
mutation of a conserved cysteine in GPIHBP1 (Montrer GPIHBP1 Protéines) abolishes the ability of GPIHBP1 (Montrer GPIHBP1 Protéines) to bind LPL
The data suggests that ANGPTL3 (Montrer ANGPTL3 Protéines) is part of the machinery causing dyslipidemia majorily via LPL inhibition in mastitis mice.
Using in vitro ketosis model by glucose starvation, studied inhibition of ketosis by momilactone B. Found momilactone B could regulate the angiopoietin-like-3 (ANGPTL3 (Montrer ANGPTL3 Protéines))-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 (Montrer HMGCS2 Protéines) through the increased expression of STAT5b (Montrer STAT5B Protéines).
physiological changes in adipose tissue ANGPTL4 (Montrer ANGPTL4 Protéines) expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4 (Montrer ANGPTL4 Protéines)(-/-) mice. We conclude that ANGPTL4 (Montrer ANGPTL4 Protéines) promotes loss of intracellular LPL by stimulating LPL degradation after LPL processing in the endoplasmic reticulum (ER).
LPL moved quickly from heparan sulfate proteoglycans (HSPGs) on adipocytes to GPIHBP1 (Montrer GPIHBP1 Protéines)-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG (Montrer SDC2 Protéines)-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 (Montrer GPIHBP1 Protéines) on endothelial cells
our study reveals that hepatic LPL is involved in the regulation of plasma LPL activity and lipid homeostasis.
The induction of LPL activity by fasting in core transgenic mice activated PPARalpha (Montrer PPARA Protéines) downstream target genes that are involved in fatty acid beta-oxidation.
LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism.
, O 1-4-5
, adipose lipoprotein lipase
, triacylglycerol lipase