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Journal of Lipid Research, Vol 36, 526-534, Copyright © 1995 by Lipid Research, Inc.
MC de Beer, T Yuan, MS Kindy, BF Asztalos, PS Roheim and FC de Beer
Serum amyloid A proteins (SAAs), a family of homologous molecules, are
apolipoproteins of high density lipoprotein (HDL). They can be divided into
two groups. The first group comprises the well-characterized acute phase
SAAs that associate with HDL during inflammation, thereby remodeling the
HDL particle by displacing apolipoprotein (apo)A-I. The second group
consists of the recently discovered constitutive SAAs, mouse SAA5 and human
SAA4. They exist as minor apolipoproteins on HDL but constitute more than
90% of the total SAA during homeostasis. We have characterized human SAA4
as an apolipoprotein. During homeostasis, SAA4 is synthesized only in the
liver. Purification of SAA4 has been described and its plasma concentration
has been established at 55 +/- 13 micrograms/ml in 26 healthy individuals.
It was present on all HDL density classes and very low density lipoprotein
(VLDL) but was absent from low density lipoprotein (LDL). Using
two-dimensional electrophoresis and phosphorimaging, SAA4 was found to be
associated with a specific subpopulation of only three HDL particles, not
involved in the initial cholesterol transfer from cells.
ARTICLES
Characterization of constitutive human serum amyloid A protein (SAA4) as an apolipoprotein
Department of Biochemistry, University of Kentucky, Lexington, USA.
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