Lipid droplets are novel sites of N-acylethanolamine inactivation by fatty acid amide hydrolase-2

Journal of Biological Chemistry

Volumn 285, Issue 4, 2010, Pages 2796-2806

  Kaczocha, Martin ^a   Glaser, Sherrye T ^b   Chae, Janiper ^a   Brown, Deborah A ^a   Deutsch, Dale G ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b Stony Brook University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY ASSAYS; BIOCHEMICAL CHARACTERIZATION; DISTRIBUTION PATTERNS; ENDOPLASMIC RETICULUM; ENZYME FATTY ACID AMIDE HYDROLASE; FATTY ACID AMIDE HYDROLASE; FUNCTIONAL SITES; HYDROPHOBIC REGIONS; IN-CELL; IN-VIVO; INTACT CELLS; LIPID DROPLETS; N-ACYLETHANOLAMINES; N-TERMINALS;

ACIDS; ACOUSTOELECTRIC EFFECTS; AMIDES; ENZYMES; FATTY ACIDS; HYDROLYSIS; MAMMALS; PIEZOELECTRIC DEVICES;

DROP FORMATION;

ANANDAMIDE; ENZYME; ETHANOLAMINE DERIVATIVE; FAT DROPLET; FATTY ACID AMIDASE; FATTY ACID AMIDE HYDROLASE 2; N ACYLETHANOLAMINE; PALMIDROL; UNCLASSIFIED DRUG; AMIDASE; AMIDE; ARACHIDONIC ACID DERIVATIVE; CARBON; DIAGNOSTIC AGENT; ENDOCANNABINOID; FATTY ACID AMIDE HYDROLASE 2, HUMAN; N ACYLETHANOLAMINES; N-ACYLETHANOLAMINES;

ANIMAL CELL; ARTICLE; ASSAY; CATABOLISM; CHEMICAL ANALYSIS; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME LOCALIZATION; HOMOGENATE; HUMAN; HUMAN CELL; HYDROLYSIS; IMMUNOFLUORESCENCE; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; ANIMAL; CELL COMPARTMENTALIZATION; CELL FRACTIONATION; CELL STRAIN COS1; CERCOPITHECUS; CHEMISTRY; CYTOPLASM; ENZYME ACTIVATION; ENZYMOLOGY; GENETIC TRANSFECTION; GENETICS; GLYCOSYLATION; HELA CELL; HYDROPHOBICITY; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT;

MAMMALIA;

AMIDOHYDROLASES; ANIMALS; ARACHIDONIC ACIDS; CARBON RADIOISOTOPES; CELL COMPARTMENTATION; CELL FRACTIONATION; CERCOPITHECUS AETHIOPS; COS CELLS; CYTOPLASM; ENDOCANNABINOIDS; ENZYME ACTIVATION; ETHANOLAMINES; GLYCOSYLATION; HELA CELLS; HUMANS; HYDROLYSIS; HYDROPHOBICITY; POLYUNSATURATED ALKAMIDES; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; TRANSFECTION;

EID: 77449131626     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.058461     Document Type: Article

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