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  • Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.

Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.

Science (New York, N.Y.) (2004-11-20)
Robert Zimmermann, Juliane G Strauss, Guenter Haemmerle, Gabriele Schoiswohl, Ruth Birner-Gruenberger, Monika Riederer, Achim Lass, Georg Neuberger, Frank Eisenhaber, Albin Hermetter, Rudolf Zechner
ABSTRACT

Mobilization of fatty acids from triglyceride stores in adipose tissue requires lipolytic enzymes. Dysfunctional lipolysis affects energy homeostasis and may contribute to the pathogenesis of obesity and insulin resistance. Until now, hormone-sensitive lipase (HSL) was the only enzyme known to hydrolyze triglycerides in mammalian adipose tissue. Here, we report that a second enzyme, adipose triglyceride lipase (ATGL), catalyzes the initial step in triglyceride hydrolysis. It is interesting that ATGL contains a "patatin domain" common to plant acyl-hydrolases. ATGL is highly expressed in adipose tissue of mice and humans. It exhibits high substrate specificity for triacylglycerol and is associated with lipid droplets. Inhibition of ATGL markedly decreases total adipose acyl-hydrolase activity. Thus, ATGL and HSL coordinately catabolize stored triglycerides in adipose tissue of mammals.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Lipase from Candida sp., recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
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 Candida rugosa, powder, yellow-brown, ≥2 U/mg
Sigma-Aldrich
Lipase from Rhizopus oryzae, powder (fine), ~10 U/mg
Sigma-Aldrich
Lipase from Aspergillus oryzae, ≥20,000 U/g
Sigma-Aldrich
Lipase from Mucor miehei, powder, slightly brown, ~1 U/mg
Sigma-Aldrich
Lipase acrylic resin, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Lipase from Candida rugosa, Type VII, ≥700 unit/mg solid
Sigma-Aldrich
Lipase from Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
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 Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
Sigma-Aldrich
Lipase from Pseudomonas cepacia, powder, light beige, ≥30 U/mg
Sigma-Aldrich
Lipase A Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~2 U/mg
Sigma-Aldrich
Lipase immobilized from Candida antarctica, beads, slightly brown, >2 U/mg
Sigma-Aldrich
Lipase from Aspergillus niger, powder (fine), ~200 U/g
Sigma-Aldrich
Lipase from Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase B Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~9 U/mg