Glycosylation of endothelial lipase at asparagine-116 reduces activity and the hydrolysis of native lipoproteins in vitro and in vivo

Glycosylation of endothelial lipase at asparagine-116 reduces activity and the hydrolysis of native lipoproteins in vitro and in vivo

We previously identified that four of five putative N-linked glycosylation sites of human endothelial lipase (EL) are utilized and suggested that the substitution of asparagine-116 (Asn-116) with alanine (Ala) (N116A) increased the hydrolytic activity of EL. The current study demonstrates that mutag...

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Bibliographic Details
Main Authors: Robert J. Brown, Gwen C. Miller, Griffon Nathalie, Christopher J. Long, Daniel J. Rader
Format: Article
Language:English
Published: Elsevier 2007-05-01
Series:Journal of Lipid Research
Subjects:
lipase
lipoprotein hydrolysis
adenovirus
glycosylation
site-directed mutagenesis
heparin
Online Access:http://www.sciencedirect.com/science/article/pii/S002222752043559X

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http://www.sciencedirect.com/science/article/pii/S002222752043559X

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