Adenoviral vector-mediated overexpression of serum amyloid A in apoA-I-deficient mice

Serum amyloid A (SAA) is an acute phase reactant that can become the predominant apolipoprotein of high density lipoprotein (HDL) during severe inflammatory states. However, the function of SAA is unknown. To study the ability of SAA to form HDL in the absence of apolipoprotein A-I, we expressed the...

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Bibliographic Details
Published in:Journal of lipid research 1997-08, Vol.38 (8), p.1583-1590
Main Authors: Webb, N R, de Beer, M C, van der Westhuyzen, D R, Kindy, M S, Banka, C L, Tsukamoto, K, Rader, D L, de Beer, F C
Format: Article
Language:English
Subjects:
Acute-Phase Reaction - blood
Adenoviridae - genetics
Animals
Apolipoprotein A-I - deficiency
Apolipoprotein A-I - genetics
Apolipoproteins - genetics
Apolipoproteins - metabolism
Apolipoproteins A - blood
Apolipoproteins E - blood
Cholesterol - blood
Cholesterol, HDL - blood
Cholesterol, HDL - chemistry
Gene Expression
Genetic Vectors
Humans
Mice
Mice, Inbred C57BL
Mice, Knockout
Serum Amyloid A Protein - genetics
Serum Amyloid A Protein - metabolism
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Summary:Serum amyloid A (SAA) is an acute phase reactant that can become the predominant apolipoprotein of high density lipoprotein (HDL) during severe inflammatory states. However, the function of SAA is unknown. To study the ability of SAA to form HDL in the absence of apolipoprotein A-I, we expressed the mouse SAA pI 6.15 (CE/J) isoform in apolipoprotein A-I knock-out (apoA-I (-/-)) mice using a recombinant adenovirus. As a control, apoA-I (-/-) mice were injected with an adenovirus expressing human apoA-I. High level expression of plasma SAA was obtained in the absence of any endogenous acute phase SAA production. SAA expression increased plasma HDL cholesterol levels about 2-fold, but to a lesser extent than the expression of apoA-I (about 10-fold). The HDL particles isolated by density ultracentrifugation from SAA-expressing mice were heterogeneous in size and composition and rich in free cholesterol as well as apoE and apoA-IV. Of the SAA expressed in the plasma, only a small fraction (4%) was associated with HDL particles in contrast to expressed apoA-I, of which 62% was associated with HDL. We conclude that SAA is unable to substitute for apoA-I in HDL particle formation.
ISSN:0022-2275
DOI:10.1016/S0022-2275(20)37176-5