J. Lipid Res. Acyl Labeled PIP's available August 1, 2008
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stahnke, G.
Right arrow Articles by Will, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stahnke, G.
Right arrow Articles by Will, H.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Journal of Lipid Research, Vol 32, 477-484, Copyright © 1991 by Lipid Research, Inc.


ARTICLES

Effect of N-linked glycosylation on hepatic lipase activity

G Stahnke, RC Davis, MH Doolittle, H Wong, MC Schotz and H Will
Max-Planck-Institut fur Biochemie, Martinsried/Munich, Federal Republic of Germany.

Hepatic lipase (HL) is a secretory protein synthesized in hepatocytes and bound to liver endothelium. Previous studies have suggested that HL N-linked glycans are required for catalytic activity. To directly test this hypothesis, Xenopus laevis oocytes were used to express native rat HL or HL lacking one or both N-linked glycosylation sites. The expressed and secreted native HL had an apparent molecular mass of 53 kDa, consistent with purified rat liver HL. The mutant lacking both glycosylation sites, while poorly secreted, had an apparent molecular mass of 48 kDa, the same size observed for HL after enzymatic removal of N-linked oligosaccharides. Mutants lacking one of the two sites were intermediate in size and showed reduced secretion. Each of these expressed and secreted proteins had full catalytic activity that was inhibited by antisera to rat HL. Thus, N-linked glycosylation of rat HL, while important to lipase secretion, is not essential for the expression of lipase activity.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Lipid Res.Home page
D. Skropeta, C. Settasatian, M. R. McMahon, K. Shearston, D. Caiazza, K. C. McGrath, W. Jin, D. J. Rader, P. J. Barter, and K.-A. Rye
N-Glycosylation regulates endothelial lipase-mediated phospholipid hydrolysis in apoE- and apoA-I-containing high density lipoproteins
J. Lipid Res., September 1, 2007; 48(9): 2047 - 2057.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
R. J. Brown, G. C. Miller, N. Griffon, C. J. Long, and D. J. Rader
Glycosylation of endothelial lipase at asparagine-116 reduces activity and the hydrolysis of native lipoproteins in vitro and in vivo
J. Lipid Res., May 1, 2007; 48(5): 1132 - 1139.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
G. C. Miller, C. J. Long, E. D. Bojilova, D. Marchadier, K. O. Badellino, N. Blanchard, I. V. Fuki, J. M. Glick, and D. J. Rader
Role of N-linked glycosylation in the secretion and activity of endothelial lipase
J. Lipid Res., November 1, 2004; 45(11): 2080 - 2087.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
B. Perret, L. Mabile, L. Martinez, F. Terce, R. Barbaras, and X. Collet
Hepatic lipase: structure/function relationship, synthesis, and regulation
J. Lipid Res., August 1, 2002; 43(8): 1163 - 1169.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1991 by the American Society for Biochemistry and Molecular Biology.