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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
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Lipase from Candida sp., recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
Sigma-Aldrich
Lipase from Rhizopus niveus, powder (fine), ≥1.5 U/mg
Sigma-Aldrich
Lipase from Rhizopus oryzae, powder (fine), ~10 U/mg
Sigma-Aldrich
Lipase from Mucor miehei, powder, slightly brown, ~1 U/mg
Sigma-Aldrich
Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
Sigma-Aldrich
Lipoprotein Lipase from Pseudomonas sp., lyophilized, powder, ≥1200 U/mg
Sigma-Aldrich
Lipoprotein Lipase from Pseudomonas sp., lyophilized, powder, yellow-brown, ≥160 U/mg
Sigma-Aldrich
Lipase acrylic resin, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Lipase from Aspergillus oryzae, ≥20,000 U/g
Sigma-Aldrich
Lipase from Aspergillus oryzae, solution, ≥100,000 U/g, white, beige
Sigma-Aldrich
Lipase from Candida rugosa, powder, yellow-brown, ≥2 U/mg
Sigma-Aldrich
Lipase from Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
Sigma-Aldrich
Lipase from Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase from Candida rugosa, Type VII, ≥700 unit/mg solid
Sigma-Aldrich
Lipase from porcine pancreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
Sigma-Aldrich
Lipase from porcine pancreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
Sigma-Aldrich
Lipase from wheat germ, Type I, lyophilized powder, 5-15 units/mg solid
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
Sigma-Aldrich
Lipoprotein Lipase from bovine milk, ammonium sulfate suspension, ≥2,000 units/mg protein (BCA)
Sigma-Aldrich
Lipase from Aspergillus niger, powder (fine), ~200 U/g
Sigma-Aldrich
Lipase from Pseudomonas cepacia, powder, light beige, ≥30 U/mg
Sigma-Aldrich
Lipase immobilized from Candida antarctica, beads, slightly brown, >2 U/mg
Sigma-Aldrich
Lipase A Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~2 U/mg
Sigma-Aldrich
Lipase B Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~9 U/mg
Sigma-Aldrich
Lipoprotein Lipase from Burkholderia sp., lyophilized powder, ≥50,000 units/mg solid
Sigma-Aldrich
Lipase from Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)