|
|
||||||||
Journal of Lipid Research, Vol 37, 2109-2116, Copyright © 1996 by Lipid Research, Inc.
JS Liang, BM Schreiber, M Salmona, G Phillip, WA Gonnerman, FC de Beer and JD Sipe
The human apoSAA proteins comprise both acute phase (apoSAA1, apoSAA2) and
constitutive (apoSAA4) isoforms; all are expressed in human atherosclerotic
lesions as well as in liver. Recombinant acute phase apoSAA binds
cholesterol with an affinity of approximately 170 nM and enhances
cholesterol uptake by HepG2 cells (J. Lipid Res. 1995. 36:37- 46). In the
present study, we sought to define the region of acute phase apoSAA
involved in cholesterol binding and to investigate the ability of
constitutive apoSAA4 to bind cholesterol. Binding of [3H]cholesterol to
apoSAAp was inhibited by unlabeled cholesterol (1- 100 nM), but not
significantly by vitamin D and estradiol. Direct binding of acute phase,
but not constitutive, apoSAA to the surfaces of polystyrene microtiter
wells was strongly diminished in the presence of cholesterol. The ability
of apoSAAp to bind cholesterol was inhibited by antibodies to human apoSAA1
and to peptide 1-18 of apoSAA1. There was only slight inhibition of
cholesterol binding by antibodies to peptide 40-63, and no inhibition by
antibodies to peptides spanning regions containing amino acid residues
14-44 and 59-104. [3H]cholesterol uptake by neonatal rabbit aortic smooth
muscle and HepG2 cells was enhanced by a synthetic peptide corresponding to
amino acids 1-18 of hSAA1, but not by peptides corresponding to amino acids
1- 18 of hSAA4. [3H]cholesterol uptake by HepG2 cells was slightly
increased by a peptide corresponding to amino acids 40-63 of hSAA1. These
findings suggest that apoSAA modulates the local flux of cholesterol
between cells and lipoproteins during inflammation and atherosclerosis.
ARTICLES
Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells
Department of Biochemistry, Boston University School of Medicine, MA 02118, USA.
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
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] |
||||
![]() |
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] |
||||
![]() |
L. Wang and W. Colon Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer Protein Sci., July 1, 2005; 14(7): 1811 - 1817. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Chait, C. Y. Han, J. F. Oram, and J. W. Heinecke Thematic review series: The Immune System and Atherogenesis. Lipoprotein-associated inflammatory proteins: markers or mediators of cardiovascular disease? J. Lipid Res., March 1, 2005; 46(3): 389 - 403. [Abstract] [Full Text] [PDF] |
||||
![]() |
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] |
||||
![]() |
A. Abbas, P. J. Fadel, Z. Wang, D. Arbique, I. Jialal, and W. Vongpatanasin Contrasting Effects of Oral Versus Transdermal Estrogen on Serum Amyloid A (SAA) and High-Density Lipoprotein-SAA in Postmenopausal Women Arterioscler. Thromb. Vasc. Biol., October 1, 2004; 24(10): e164 - e167. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Recinos III, B. K. Carr, D. B. Bartos, I. Boldogh, J. R. Carmical, L. M. Belalcazar, and A. R. Brasier Liver gene expression associated with diet and lesion development in atherosclerosis-prone mice: induction of components of alternative complement pathway Physiol Genomics, September 16, 2004; 19(1): 131 - 142. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Wang, H. A. Lashuel, T. Walz, and W. Colon Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel PNAS, December 10, 2002; 99(25): 15947 - 15952. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. R. Brasier, A. Recinos III, and M. S. Eledrisi Vascular Inflammation and the Renin-Angiotensin System Arterioscler. Thromb. Vasc. Biol., August 1, 2002; 22(8): 1257 - 1266. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. C. TUCKER and G. H. SACK JR Expression of serum amyloid A genes in mouse brain: unprecedented response to inflammatory mediators FASEB J, October 1, 2001; 15(12): 2241 - 2246. [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 |