J. Lipid Res.  Neurobiology of Lipids (ISSN1683-5506)
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
Right arrow Citation Map
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 Banka, C. L.
Right arrow Articles by de Beer, F. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Banka, C. L.
Right arrow Articles by de Beer, F. C.
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 36, 1058-1065, Copyright © 1995 by Lipid Research, Inc.


ARTICLES

Serum amyloid A (SAA): influence on HDL-mediated cellular cholesterol efflux

CL Banka, T Yuan, MC de Beer, M Kindy, LK Curtiss and FC de Beer
Department of Immunology, Scripps Research Institute, La Jolla, CA 92037, USA.

Normal high density lipoprotein (N-HDL) is remodeled during acute phase (AP) reactions by the association of serum amyloid A (SAA) and the depletion of apolipoprotein (apo) A-I. To determine the impact of this remodeling on HDL function, the capacities of N-HDL and AP-HDL to associate with and promote cholesterol efflux from human monocytic THP- 1 cells were compared. THP-1 cells preferentially bound AP-HDL compared with N-HDL. Examination of the AP-HDL particles bound to THP-1 cells revealed a disproportionate association of an apoSAA-enriched, apoA-I- depleted subpopulation compared with the composition of the starting material. However, N-HDL and AP-HDL promoted cholesterol efflux from THP-1 cells equally efficiently and in a dose-dependent manner. When N- HDL was experimentally remodeled with apoSAA to achieve an apoprotein composition similar to that of the preferentially bound particles, cellular cholesterol efflux was reduced by 30%. The remodelling of HDL with apoSAA during the acute phase reaction alters cholesterol efflux only when apoSAA constitutes more than 50% of the HDL protein.
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. Leukoc. Biol.Home page
D. El Kebir, L. Jozsef, and J. G. Filep
Opposing regulation of neutrophil apoptosis through the formyl peptide receptor-like 1/lipoxin A4 receptor: implications for resolution of inflammation
J. Leukoc. Biol., September 1, 2008; 84(3): 600 - 606.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
N. Cheng, R. He, J. Tian, P. P. Ye, and R. D. Ye
Cutting Edge: TLR2 Is a Functional Receptor for Acute-Phase Serum Amyloid A
J. Immunol., July 1, 2008; 181(1): 22 - 26.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
W. Hu, S. Abe-Dohmae, M. Tsujita, N. Iwamoto, O. Ogikubo, T. Otsuka, Y. Kumon, and S. Yokoyama
Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo
J. Lipid Res., February 1, 2008; 49(2): 386 - 393.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
D. El Kebir, L. Jozsef, T. Khreiss, W. Pan, N. A. Petasis, C. N. Serhan, and J. G. Filep
Aspirin-Triggered Lipoxins Override the Apoptosis-Delaying Action of Serum Amyloid A in Human Neutrophils: A Novel Mechanism for Resolution of Inflammation
J. Immunol., July 1, 2007; 179(1): 616 - 622.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
R. He, L. W. Shepard, J. Chen, Z. K. Pan, and R. D. Ye
Serum Amyloid A Is an Endogenous Ligand That Differentially Induces IL-12 and IL-23
J. Immunol., September 15, 2006; 177(6): 4072 - 4079.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
A. Kontush and M. J. Chapman
Functionally Defective High-Density Lipoprotein: A New Therapeutic Target at the Crossroads of Dyslipidemia, Inflammation, and Atherosclerosis
Pharmacol. Rev., September 1, 2006; 58(3): 342 - 374.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. R. van der Westhuyzen, L. Cai, M. C. de Beer, and F. C. de Beer
Serum Amyloid A Promotes Cholesterol Efflux Mediated by Scavenger Receptor B-I
J. Biol. Chem., October 28, 2005; 280(43): 35890 - 35895.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
S. P. Tam, J. B. Ancsin, R. Tan, and R. Kisilevsky
Peptides derived from serum amyloid A prevent, and reverse, aortic lipid lesions in apoE-/- mice
J. Lipid Res., October 1, 2005; 46(10): 2091 - 2101.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. N. Baranova, T. G. Vishnyakova, A. V. Bocharov, R. Kurlander, Z. Chen, M. L. Kimelman, A. T. Remaley, G. Csako, F. Thomas, T. L. Eggerman, et al.
Serum Amyloid A Binding to CLA-1 (CD36 and LIMPII Analogous-1) Mediates Serum Amyloid A Protein-induced Activation of ERK1/2 and p38 Mitogen-activated Protein Kinases
J. Biol. Chem., March 4, 2005; 280(9): 8031 - 8040.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Cai, M. C. de Beer, F. C. de Beer, and D. R. van der Westhuyzen
Serum Amyloid A Is a Ligand for Scavenger Receptor Class B Type I and Inhibits High Density Lipoprotein Binding and Selective Lipid Uptake
J. Biol. Chem., January 28, 2005; 280(4): 2954 - 2961.
[Abstract] [Full Text] [PDF]


Home page
CirculationHome page
B. D. Johnson, K. E. Kip, O. C. Marroquin, P. M Ridker, S. F. Kelsey, L. J. Shaw, C. J. Pepine, B. Sharaf, C. N. Bairey Merz, G. Sopko, et al.
Serum Amyloid A as a Predictor of Coronary Artery Disease and Cardiovascular Outcome in Women: The National Heart, Lung, and Blood Institute-Sponsored Women's Ischemia Syndrome Evaluation (WISE)
Circulation, February 17, 2004; 109(6): 726 - 732.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
V. G. Cabana, N. Feng, C. A. Reardon, J. Lukens, N. R. Webb, F. C. de Beer, and G. S. Getz
Influence of apoA-I and apoE on the formation of serum amyloid A-containing lipoproteins in vivo and in vitro
J. Lipid Res., February 1, 2004; 45(2): 317 - 325.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
R. He, H. Sang, and R. D. Ye
Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R
Blood, February 15, 2003; 101(4): 1572 - 1581.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
S. P. Tam, A. Flexman, J. Hulme, and R. Kisilevsky
Promoting export of macrophage cholesterol: the physiological role of a major acute-phase protein, serum amyloid A 2.1
J. Lipid Res., September 1, 2002; 43(9): 1410 - 1420.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
W. Khovidhunkit, J. K. Shigenaga, A. H. Moser, K. R. Feingold, and C. Grunfeld
Cholesterol efflux by acute-phase high density lipoprotein: role of lecithin:cholesterol acyltransferase
J. Lipid Res., June 1, 2001; 42(6): 967 - 975.
[Abstract] [Full Text]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
A. Artl, G. Marsche, S. Lestavel, W. Sattler, and E. Malle
Role of Serum Amyloid A During Metabolism of Acute-Phase HDL by Macrophages
Arterioscler. Thromb. Vasc. Biol., March 1, 2000; 20(3): 763 - 772.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
V. G. Cabana, C. A. Reardon, B. Wei, J. R. Lukens, and G. S. Getz
SAA-only HDL formed during the acute phase response in apoA-I+/+ and apoA-I-/- mice
J. Lipid Res., June 1, 1999; 40(6): 1090 - 1103.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
J. B. Ancsin and R. Kisilevsky
The Heparin/Heparan Sulfate-binding Site on Apo-serum Amyloid A. IMPLICATIONS FOR THE THERAPEUTIC INTERVENTION OF AMYLOIDOSIS
J. Biol. Chem., March 12, 1999; 274(11): 7172 - 7181.
[Abstract] [Full Text] [PDF]


Home page
NEJMHome page
C. Gabay and I. Kushner
Acute-Phase Proteins and Other Systemic Responses to Inflammation
N. Engl. J. Med., February 11, 1999; 340(6): 448 - 454.
[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 © 1995 by the American Society for Biochemistry and Molecular Biology.