Merck
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  • ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells.

ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells.

EMBO reports (2005-10-22)
Elena Smirnova, Elysa B Goldberg, Kira S Makarova, Lin Lin, William J Brown, Catherine L Jackson
ABSTRACT

Lipid droplets (LDs), also called adiposomes, are found in many eukaryotic cells, and are highly upregulated in lipid-storage cells, such as adipocytes. The mechanism by which adiposomes and their component neutral lipids are degraded is an important health issue with the rapidly spreading epidemic of obesity. Recently, a novel triglyceride lipase (adipose triglyceride lipase (ATGL)) that catalyses the initial step in triglyceride hydrolysis in adipocyte LDs was identified. Here, we show that ATGL also functions in non-adipocyte cells, and has an important role in LD degradation in these cells. Overexpression of wild-type ATGL causes a marked decrease in LD size, whereas a catalytically inactive mutant retains the ability to localize to LDs, but is unable to decrease their size. Depletion of ATGL by RNA interference leads to a significant increase in the size of LDs. These results show that ATGL has an important role in LD/adiposome turnover in mammalian cells.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Lipase from Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
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Lipase from Candida rugosa, Type VII, ≥700 unit/mg solid
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Lipase from Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
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Lipase from Aspergillus oryzae, ≥20,000 U/g
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Lipase from Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
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Lipase from Mucor miehei, powder, slightly brown, ~1 U/mg
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Lipase from Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
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Lipase from Rhizopus niveus, powder (fine), ≥1.5 U/mg
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Lipase from Candida rugosa, powder, yellow-brown, ≥2 U/mg
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Lipase from Candida sp., recombinant, expressed in Aspergillus niger
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Lipase from Rhizopus oryzae, powder (fine), ~10 U/mg
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Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
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Lipase from Aspergillus niger, powder (fine), ~200 U/g
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Lipase from Pseudomonas cepacia, powder, light beige, ≥30 U/mg
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Lipase immobilized from Candida antarctica, beads, slightly brown, >2 U/mg
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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
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