J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on January 1, 2004

Papers In Press, published online ahead of print September 16, 2003
J. Lipid Res., doi:10.1194/jlr.M300071-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
M300071-JLR200v1
45/1/63    most recent
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 Liu, C. Y. Y.
Right arrow Articles by McCormick, S. P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Liu, C. Y. Y.
Right arrow Articles by McCormick, S. P. A.
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?

Submitted on February 10, 2003
Revised on September 5, 2003
Accepted on September 8, 2003

Mutation of lysine residues in apolipoprotein B-100 causes defective lipoprotein[a] formation

Catherine Y. Y. Liu, Ric Broadhurst, Santica M. Marcovina, and Sally P. A. McCormick

Biochemistry Dept., University of Otago, Dunedin

Corresponding Author: sally.mccormick{at}stonebow.otago.ac.nz

Lipoprotein(a) [Lp(a)] is assembled by a two-step process involving an initial lysine-dependent binding between apolipoprotein B100 and apolipoprotein(a) that facilitates the formation of a disulphide bond between apoB100Cys4326 and apo(a)Cys4057. Previous studies of transgenic mice expressing apoB95 (4330 amino acids) and apoB97 (4397 amino acids) have shown that apoB100 amino acids 4330–4397 are important for the initial binding to apo(a). Furthermore, a lysine-rich peptide spanning apoB100 amino acids 4372-4392 has recently been shown to bind apo(a) and inhibit Lp(a) assembly in vitro. This suggests that a putative apo(a) binding site exists in the apoB4372-4392 region. The aim of our study was to establish whether the apoB4372-4392 sequence was important for Lp(a) assembly in the context of the full length apoB100. Transgenic mice were created that expressed a mutant human apoB100, apoB100K4>S4, in which all four lysine residues in the 4372-4392 sequence were mutated to serines. The apoB100K4>S4 mutant showed a reduced capacity to form Lp(a) in vitro compared to wild-type human apoB100. Double transgenic mice expressing both apoB100K4>S4 and apo(a) contained significant amounts of free apo(a) in the plasma indicating a less efficient assembly of Lp(a) in vivo. Taken together, these results clearly show that the apoB4372-4392 sequence plays a role in Lp(a) assembly. a


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
R. J. Sharp, M. A. Perugini, S. M. Marcovina, and S. P. A. McCormick
Structural features of apolipoprotein B synthetic peptides that inhibit lipoprotein(a) assembly
J. Lipid Res., December 1, 2004; 45(12): 2227 - 2234.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.