Inhibition of endothelial lipase activity by sphingomyelin in the lipoproteins

Lipids

Volumn 49, Issue 10, 2014, Pages 987-996

  Yang, Peng ^a   Belikova, Natalia A ^a   Billheimer, Jeff ^b   Rader, Daniel J ^b   Hill, John S ^c   Subbaiah, Papasani V ^a,d  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^d JESSE BROWN VA MEDICAL CENTER   (United States)

Author keywords

Enzyme regulation; LC MS; Lysophsphatidylcholine; Molecular species of phosphatidylcholine; Sphingomyelin phosphatidyl choline ratio; Sphingomyelinase; Substrate specificity

Indexed keywords

ENDOTHELIAL LIPASE; HIGH DENSITY LIPOPROTEIN; LIPOPROTEIN; LIPOSOME; LOW DENSITY LIPOPROTEIN; PHOSPHATIDYLCHOLINE; POLYUNSATURATED FATTY ACID; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; VERY LOW DENSITY LIPOPROTEIN; LIPG PROTEIN, HUMAN; RECOMBINANT PROTEIN;

ARTICLE; CONTROLLED STUDY; EMULSION; ENZYME INHIBITION; ENZYME REGULATION; ENZYME SPECIFICITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; MASS SPECTROMETRY; PROTEIN DEGRADATION; ANTAGONISTS AND INHIBITORS; CHEMISTRY; HUMAN; IN VITRO STUDY; METABOLISM;

BACTERIA (MICROORGANISMS);

HUMANS; HYDROLYSIS; IN VITRO TECHNIQUES; LIPASE; LIPOPROTEINS; LIPOPROTEINS, HDL; LIPOPROTEINS, LDL; LIPOSOMES; PHOSPHATIDYLCHOLINES; RECOMBINANT PROTEINS; SPHINGOMYELINS; SUBSTRATE SPECIFICITY;

EID: 84919397386     PISSN: 00244201     EISSN: 15589307     Source Type: Journal    
DOI: 10.1007/s11745-014-3944-1     Document Type: Article

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