Serum amyloid A generates high density lipoprotein with cellular lipid in an ABCA1- or ABCA7-dependent manner

Abe-Dohmae, Sumiko; Kato, Koichi; Kumon, Yoshitaka; Hu, Wei; Ishigami, Hideaki; Iwamoto, Noriyuki; Okazaki, Mitsuyo; Wu, Chen-Ai; Tsujita, Maki; Ueda, Kazumitsu; Yokoyama, Shinji

doi:10.1194/jlr.m600145-jlr200

Cited by 51 publications

(46 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…a Significant statistical difference (P , 0.001) from the none group with a matched genotype. and overexpressed (13). However, endogenously expressed ABCA7 is not expressed on the cell surface and may not be involved in HDL biogenesis (20,26).…”

Section: Discussionmentioning

confidence: 99%

“…300-13). A stock solution (1 mg/ml) was prepared according to the manufacturer's instructions and stored at 4jC as described previously (13). Concentrations of SAA and TNF-a were determined using ELISA kits (Biosource International Co.).…”

Section: Reagents and Antibodiesmentioning

confidence: 99%

“…We demonstrated that SAA generates cholesterol-containing HDL directly from cellular lipid and that this reaction is mediated by ABCA1 and/or ABCA7 transfected to HEK293 cells (13).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo

Abe-Dohmae

Tsujita

et al. 2008

Journal of Lipid Research

Self Cite

View full text Add to dashboard Cite

Serum amyloid A (SAA) was markedly increased in the plasma and in the liver upon acute inflammation induced by intraperitoneal injection of lipopolysaccharide (LPS) in mice, and SAA in the plasma was exclusively associated with HDL. In contrast, no HDL was present in the plasma and only a small amount of SAA was found in the VLDL/LDL fraction (d , 1.063 g/ml) after the induction of inflammation in ABCA1-knockout (KO) mice, although SAA increased in the liver. Primary hepatocytes isolated from LPS-treated wild-type (WT) and ABCA1-KO mice both secreted SAA into the medium. SAA secreted from WT hepatocytes was associated with HDL, whereas SAA from ABCA1-KO hepatocytes was recovered in the fraction that was .1.21 g/ml. The behavior of apolipoprotein A-I (apoA-I) was the same as that of SAA in HDL biogenesis by WT and ABCA1-KO mouse hepatocytes. Lipid-free SAA and apoA-I both stabilized ABCA1 and caused cellular lipid release in WT mouse-derived fibroblasts, but not in ABCA1-KO mousederived fibroblasts, in vitro when added exogenously. We conclude that both SAA and apoA-I generate HDL largely in hepatocytes only in the presence of ABCA1, likely being secreted in a lipid-free form to interact with cellular ABCA1. In the absence of ABCA1, nonlipidated SAA is seemingly removed rapidly from the extracellular space.-Hu, W., 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. 2008. 49: 386-393.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Reagents and Antibodiesmentioning

confidence: 99%

See 1 more Smart Citation

Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo

Abe-Dohmae

Tsujita

et al. 2008

Journal of Lipid Research

Self Cite

View full text Add to dashboard Cite

show abstract

“…However, the effects of SAA on HDL functions are not necessarily deleterious ( 26,38 ). For instance, similar to apoA-I, lipid-free SAA promotes effl ux of cholesterol and phospholipids from cells and, hence, is proposed to play a protective role in cholesterol removal from macrophages at the sites of infl ammation ( 14,26,39 ). Interestingly, certain key functions of HDL in reverse cholesterol transport are relatively unaffected by the biochemical changes in acute-phase HDL; this includes the stimulation of cholesteryl ester transfer protein (CETP) or the net effect on cell cholesterol effl ux ( 15 ).…”

mentioning

confidence: 99%

“…In addition to its putative role in immune response, SAA was proposed to modulate blood coagulation ( 11 ), monocyte and neturophil chemotaxis ( 12 ), and HDL functions in cholesterol transport and metabolism (13)(14)(15)(16). SAA is implicated in retinol transport ( 10 ), and elevated plasma SAA is a cardiovascular risk factor ( 17 ).…”

mentioning

confidence: 99%

Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL

Jayaraman

Haupt

Gursky

2015

Journal of Lipid Research

View full text Add to dashboard Cite

High Density Lipoprotein Structure–Function and Role in Reverse Cholesterol Transport

Lund‐Katz

Phillips

2010

Subcellular Biochemistry

219

196

View full text Add to dashboard Cite

High density lipoprotein (HDL) possesses important anti-atherogenic properties and this review addresses the molecular mechanisms underlying these functions. The structures and cholesterol transport abilities of HDL particles are determined by the properties of their exchangeable apolipoprotein (apo) components. ApoA-I and apoE, which are the best characterized in structural terms, contain a series of amphipathic α-helical repeats. The helices located in the amino-terminal two-thirds of the molecule adopt a helix bundle structure while the carboxy-terminal segment forms a separately folded, relatively disorganized, domain. The latter domain initiates lipid binding and this interaction induces changes in conformation; the α-helix content increases and the amino-terminal helix bundle can open subsequently. These conformational changes alter the abilities of apoA-I and apoE to function as ligands for their receptors. The apoA-I and apoE molecules possess detergent-like properties and they can solubilize vesicular phospholipid to create discoidal HDL particles with hydrodynamic diameters of ~10 nm. In the case of apoA-I, such a particle is stabilized by two protein molecules arranged in an anti-parallel, double-belt, conformation around the edge of the disc. The abilities of apoA-I and apoE to solubilize phospholipid and stabilize HDL particles enable these proteins to be partners with ABCA1 in mediating efflux of cellular phospholipid and cholesterol, and the biogenesis of HDL particles. ApoA-I-containing nascent HDL particles play a critical role in cholesterol transport in the circulation whereas apoE-containing HDL particles mediate cholesterol transport in the brain. The mechanisms by which HDL particles are remodeled by lipases and lipid transfer proteins, and interact with SR-BI to deliver cholesterol to cells, are reviewed.

show abstract

Serum amyloid A generates high density lipoprotein with cellular lipid in an ABCA1- or ABCA7-dependent manner

Cited by 51 publications

References 51 publications

Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo

Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo

Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL

High Density Lipoprotein Structure–Function and Role in Reverse Cholesterol Transport

Contact Info

Product

Resources

About