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LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Zusätzlich bieten wir Ihnen Lipoprotein Lipase Antikörper (142) und Lipoprotein Lipase Proteine (15) und viele weitere Produktgruppen zu diesem Protein an.
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Guinea Pig Lipoprotein Lipase ELISA Kit für Sandwich ELISA - ABIN2345123
Chan, Wong, Pang, Barrett, Watts et al.: Inter-relationships between proprotein convertase subtilisin/kexin type 9, apolipoprotein C-III and plasma apolipoprotein B-48 transport in obese subjects: a stable isotope study in the postprandial ... in Clinical science (London, England : 1979) 2014
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Mouse (Murine) Lipoprotein Lipase ELISA Kit für Sandwich ELISA - ABIN367674
Feng, Hai-ning, Xiao-man, Zun-chen, Sheng-rong, Das: Effect of yellow capsicum extract on proliferation and differentiation of 3T3-L1 preadipocytes. in Nutrition (Burbank, Los Angeles County, Calif.) 2014
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Human Lipoprotein Lipase ELISA Kit für Sandwich ELISA - ABIN366804
Levine, Hull, Buchwald, Villablanca: The spontaneous firing patterns of forebrain neurons. II. Effects of unilateral caudate nuclear ablation. in Brain research 1974
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Human Lipoprotein Lipase ELISA Kit für Sandwich ELISA - ABIN414399
Wang, Puthanveetil, Wang, Kim, Abrahani, Rodrigues: Severity of diabetes governs vascular lipoprotein lipase by affecting enzyme dimerization and disassembly. in Diabetes 2011
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Mouse (Murine) Lipoprotein Lipase ELISA Kit für Sandwich ELISA - ABIN415412
Liu, Xu, Liu, Ding, Liu, Chen, Fan, Zhang, Zheng, Zou, Lyu, Zhang: Regulation of plasma lipid homeostasis by hepatic lipoprotein lipase in adult mice. in Journal of lipid research 2016
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 (zeige LCP1 ELISA Kits) gene locus and minor allele frequency
Regression analysis revealed significant risk for memory loss that are dependent on age and genetic variants like LPL (zeige LCP1 ELISA Kits).
The findings in this study suggest that there is a poor concordance between apo E (zeige APOE ELISA Kits) genotyping and lipoprotein electrophoresis in diagnosing dysbetalipoproteinemia.
mutation of a conserved cysteine in GPIHBP1 (zeige GPIHBP1 ELISA Kits) abolishes the ability of GPIHBP1 (zeige GPIHBP1 ELISA Kits) to bind LPL (zeige LCP1 ELISA Kits)
ANGPTL8 has a functional LPL (zeige LCP1 ELISA Kits) inhibitory motif, but only inhibits LPL (zeige LCP1 ELISA Kits) and increases plasma TG levels in mice in the presence of ANGPTL3 (zeige ANGPTL3 ELISA Kits)
The expression of COBLL1, LPL, and ZAP70 corresponded to patient prognosis and to IGHV mutational status, although not absolutely. When we combined all three markers together and performed the ROC analysis, AUC increased compared to the AUC of individual gene expression.
heterozygous N291S mutation in the lipoprotein lipase gene impairs whole-body insulin (zeige INS ELISA Kits) sensitivity and affects a distinct set of plasma metabolites in humans
LPL (zeige LCP1 ELISA Kits) is important for the maturation of small discoidal HDL (zeige HSD11B1 ELISA Kits) particles into large spherical HDL (zeige HSD11B1 ELISA Kits) particles, while HL is important for HDL (zeige HSD11B1 ELISA Kits) remodeling of very large HDL (zeige HSD11B1 ELISA Kits) particles into intermediate-size HDL (zeige HSD11B1 ELISA Kits) particles, as shown in lipoprotein lipase and hepatic lipase (zeige LIPC ELISA Kits) deficiency
The authors now show: (1) that ANGPTL4 (zeige ANGPTL4 ELISA Kits) inactivates LPL (zeige LCP1 ELISA Kits) by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 (zeige GPIHBP1 ELISA Kits) renders LPL (zeige LCP1 ELISA Kits) largely refractory to this inhibition; and (3) that both the LU domain and the intrinsically disordered acidic domain of GPIHBP1 (zeige GPIHBP1 ELISA Kits) are required for this protective effect.
Carrier status for the two common LPL (zeige LCP1 ELISA Kits) variants: 447Ter (low TG/high HDL (zeige HSD11B1 ELISA Kits)-C) and 291Ser (high TG/low HDL (zeige HSD11B1 ELISA Kits)-C) was determined. Compared with the reference variant, the prevalence of metabolic syndrome was lower in carriers of the 447Ter variant (11.2% vs. 17.9%, P < 0.001) but with no difference in carriers of the 291Ser variant (18.4% vs. 16.5%, P = 0.59).
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 (zeige MYLIP ELISA Kits)-29b targets LPL and TDG (zeige TDG ELISA Kits) genes and regulates apoptosis and triglyceride production in mammary epithelial cells.
apoC-I (zeige APOC1 ELISA Kits) and apoC-III (zeige APOC3 ELISA Kits) 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 (zeige ANGPTL4 ELISA Kits).
ANGPTL4 (zeige ANGPTL4 ELISA Kits) 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 (zeige APOC2 ELISA Kits).
regions that are responsive to activation by apoC-II (zeige APOC2 ELISA Kits)
domain (192-238) is absolutely necessary for apolipoprotein AV (zeige APOA5 ELISA Kits) in lipid binding and lipoprotein lipase activation
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 (zeige GPIHBP1 ELISA Kits) abolishes the ability of GPIHBP1 (zeige GPIHBP1 ELISA Kits) to bind LPL
The data suggests that ANGPTL3 (zeige ANGPTL3 ELISA Kits) 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 (zeige ANGPTL3 ELISA Kits))-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 (zeige HMGCS2 ELISA Kits) through the increased expression of STAT5b (zeige STAT5B ELISA Kits).
physiological changes in adipose tissue ANGPTL4 (zeige ANGPTL4 ELISA Kits) expression during fasting and cold resulted in inverse changes in the amount of mature-glycosylated LPL in wild-type mice, but not Angptl4 (zeige ANGPTL4 ELISA Kits)(-/-) mice. We conclude that ANGPTL4 (zeige ANGPTL4 ELISA Kits) 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 (zeige GPIHBP1 ELISA Kits)-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG (zeige SDC2 ELISA Kits)-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 (zeige GPIHBP1 ELISA Kits) 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 (zeige PPARA ELISA Kits) downstream target genes that are involved in fatty acid beta-oxidation.
This study shows that TNF-alpha (zeige TNF ELISA Kits), by a Foxo1 (zeige FOXO1 ELISA Kits) dependent pathway, increases the transcription of ANGPTL4 (zeige ANGPTL4 ELISA Kits) which is secreted by the cells and causes inactivation of LPL.
Our findings suggest that neuronal LPL is involved in the regulation of body weight and composition in response to either the change in quantity (HF feeding) or quality (n-3 PUFA-enriched) of dietary fat
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