| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 275, Issue 21, 16267-16274, May 26, 2000
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Biophysics, Center for Advanced Biomedical
Research, Boston University School of Medicine,
Boston, Massachusetts 02118
Apolipoprotein (apo) B-100, an essential protein
for the assembly and secretion of very low density lipoproteins depends
on lipid binding (lipidation) for its secretion. Seven of its 8 disulfides are clustered within the N-terminal 21%. The role of these
disulfides in the secretion of lipidated or unlipidated truncated forms
of apoB was studied in C127 cells expressing apoB-17, apoB-29, or apoB-41. These cells do not express microsomal triglyceride transfer protein yet secrete apoB-41 on triacylglycerol-rich lipoproteins while
apoB-29 and apoB-17 are secreted with little or no lipid, respectively.
Dithiothreitol utilized in pulse-chase studies prevented the
cotranslational formation of disulfides and when added
posttranslationally reduced native disulfides. As a result, the
secretion of reduced apoB forms was blocked and they were retained in
the cells. Reduced apoB polypeptides were rescued following removal of
dithiothreitol, as they underwent post-translational disulfide bonding,
attained their mature form, and were subsequently secreted. Together
the data suggest that in C127 cells the formation of native disulfides is critical for the folding and secretion of apoB independent of its
length, its requirement for lipidation or microsomal triglyceride transfer protein expression. Therefore, these cells provide an appropriate model to study the folding of apoB in great detail.
Disulfide Bonds Are Required for Folding and Secretion of
Apolipoprotein B Regardless of Its Lipidation State*
*
This work was supported by National Institute of Health
Grants HL-58833-03 (to H. H.) and HL-26335-19 (to Donald M. Small).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom all correspondence should be addressed: Dept. of
Biophysics, Boston University School of Medicine, 715 Albany St., Boston, MA 02118. Tel.: 617-638-4012; Fax: 617-638-4041; E-mail: haya@med-biophd.bu.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  J. R. Burnett, S. Zhong, Z. G. Jiang, A. J. Hooper, E. A. Fisher, R. S. McLeod, Y. Zhao, P. H. R. Barrett, R. A. Hegele, F. M. van Bockxmeer, et al. Missense Mutations in APOB within the beta{alpha}1 Domain of Human APOB-100 Result in Impaired Secretion of ApoB and ApoB-containing Lipoproteins in Familial Hypobetalipoproteinemia J. Biol. Chem., August 17, 2007; 282(33): 24270 - 24283. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. S. Ledford, R. B. Weinberg, V. R. Cook, R. R. Hantgan, and G. S. Shelness Self-association and Lipid Binding Properties of the Lipoprotein Initiating Domain of Apolipoprotein B J. Biol. Chem., March 31, 2006; 281(13): 8871 - 8876. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Manchekar, P. E. Richardson, T. M. Forte, G. Datta, J. P. Segrest, and N. Dashti Apolipoprotein B-containing Lipoprotein Particle Assembly: LIPID CAPACITY OF THE NASCENT LIPOPROTEIN PARTICLE J. Biol. Chem., September 17, 2004; 279(38): 39757 - 39766. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Wang and D. M. Small Interfacial properties of amphipathic {beta} strand consensus peptides of apolipoprotein B at oil/water interfaces J. Lipid Res., September 1, 2004; 45(9): 1704 - 1715. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. R. Burnett, J. Shan, B. A. Miskie, A. J. Whitfield, J. Yuan, K. Tran, C. J. McKnight, R. A. Hegele, and Z. Yao A Novel Nontruncating APOB Gene Mutation, R463W, Causes Familial Hypobetalipoproteinemia J. Biol. Chem., April 4, 2003; 278(15): 13442 - 13452. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Nassir, Y. Xie, and N. O. Davidson Apolipoprotein[a] secretion from hepatoma cells is regulated in a size-dependent manner by alterations in disulfide bond formation J. Lipid Res., April 1, 2003; 44(4): 816 - 827. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. A. DeLozier, J. S. Parks, and G. S. Shelness Vesicle-binding properties of wild-type and cysteine mutant forms of {{alpha}}1 domain of apolipoprotein B J. Lipid Res., March 1, 2001; 42(3): 399 - 406. [Abstract] [Full Text]
|
|
|
|
|
|
H. Herscovitz, A. Derksen, M. T. Walsh, C. J. McKnight, D. L. Gantz, M. Hadzopoulou-Cladaras, V. Zannis, C. Curry, and D. M. Small The N-terminal 17% of apoB binds tightly and irreversibly to emulsions modeling nascent very low density lipoproteins J. Lipid Res., January 1, 2001; 42(1): 51 - 59. [Abstract] [Full Text]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
