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Merck

Role of SN1 lipases on plasma lipids in metabolic syndrome and obesity.

Arteriosclerosis, thrombosis, and vascular biology (2014-01-25)
Verónica Miksztowicz, Laura Schreier, Mary McCoy, Diego Lucero, Eduardo Fassio, Jeffrey Billheimer, Daniel J Rader, Gabriela Berg
ZUSAMMENFASSUNG

To assess the phospholipase activity of endothelial (EL) and hepatic lipase (HL) in postheparin plasma of subjects with metabolic syndrome (MS)/obesity and their relationship with atherogenic and antiatherogenic lipoproteins. Additionally, to evaluate lipoprotein lipase (LPL) and HL activity as triglyceride (TG)-hydrolyses to complete the analyses of SN1 lipolytic enzymes in the same patient. Plasma EL, HL, and LPL activities were evaluated in 59 patients with MS and 36 controls. A trend toward higher EL activity was observed in MS. EL activity was increased in obese compared with normal weight group (P=0.009) and was negatively associated with high-density lipoprotein-cholesterol (P=0.014 and P=0.005) and apolipoprotein A-I (P=0.045 and P=0.001) in control and MS group, respectively. HL activity, as TG-hydrolase, was increased in MS (P=0.025) as well as in obese group (P=0.017); directly correlated with low-density lipoprotein-cholesterol (P=0.005) and apolipoprotein B (P=0.003) and negatively with high-density lipoprotein-cholesterol (P=0.021) in control group. LPL was decreased in MS (P<0.001) as well as in overweight and obese compared with normal weight group (P=0.015 and P=0.004, respectively); inversely correlated %TG-very low-density lipoproteins (P=0.04) and TG/apolipoprotein B index (P=0.013) in control group. These associations were not found in MS. We describe for the first time EL and HL activity as phospholipases in MS/obesity, being both responsible for high-density lipoprotein catabolism. Our results elucidate part of the remaining controversies about SN1 lipases activity in MS and different grades of obesity. The impact of insulin resistance on the activity of the 3 enzymes determines the lipoprotein alterations observed in these states.

MATERIALIEN
Produktnummer
Marke
Produktbeschreibung

Sigma-Aldrich
Lipase aus Candida rugosa, Type VII, ≥700 unit/mg solid
Sigma-Aldrich
Lipase aus Schweinepankreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
Sigma-Aldrich
Lipase-Acrylharz aus Candida antarctica, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Lipoprotein-Lipase aus Kuhmilch, ammonium sulfate suspension, ≥2,000 units/mg protein (BCA)
Sigma-Aldrich
Lipoprotein-Lipase aus Pseudomonas sp., lyophilized, powder, ≥1200 U/mg
Sigma-Aldrich
Lipase B Candida antarctica, rekombinant aus Aspergillus oryzae, powder, beige, ~9 U/mg
Sigma-Aldrich
Lipase aus Schweinepankreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
Sigma-Aldrich
Lipase aus Aspergillus niger, powder (fine), ~200 U/g
Sigma-Aldrich
Lipase aus Aspergillus oryzae, solution, ≥100,000 U/g, white, beige
Sigma-Aldrich
Lipase aus Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
Sigma-Aldrich
Lipase aus Candida sp., recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Lipase, immobilisiert aus Candida antarctica, beads, slightly brown, >2 U/mg
Sigma-Aldrich
Lipase aus Rhizomucor miehei, ≥20,000 U/g
Sigma-Aldrich
Lipase aus Pseudomonas cepacia, powder, light beige, ≥30 U/mg
Sigma-Aldrich
Lipase aus Weizenkeimen, Type I, lyophilized powder, 5-15 units/mg solid
Sigma-Aldrich
Lipase aus Rhizopus oryzae, powder (fine), ~10 U/mg
Sigma-Aldrich
Lipase aus Candida rugosa, powder, yellow-brown, ≥2 U/mg
Sigma-Aldrich
Lipase aus Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
Sigma-Aldrich
Lipoprotein-Lipase aus Pseudomonas sp., lyophilized powder, ≥50,000 units/mg solid
Sigma-Aldrich
Lipase aus Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
Sigma-Aldrich
Lipase aus Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
Sigma-Aldrich
Lipase aus Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase aus Rhizopus niveus, powder (fine), ≥1.5 U/mg
Sigma-Aldrich
Lipase A Candida antarctica, rekombinant aus Aspergillus oryzae, powder, beige, ~2 U/mg
Sigma-Aldrich
Lipase aus Mucor miehei, powder, slightly brown, ~1 U/mg
Sigma-Aldrich
Lipase aus Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)