Characterization of constitutive human serum amyloid A protein (SAA4) as an apolipoprotein

M. C. De Beer, T. Yuan, M. S. Kindy, B. F. Asztalos, P. S. Roheim, F. C. De Beer

Research output: Contribution to journalArticlepeer-review

74 Scopus citations


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 SAA3 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 μg/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 truly three HDL particles, not involved in the initial cholesterol transfer from cells.

Original languageEnglish
Pages (from-to)526-534
Number of pages9
JournalJournal of Lipid Research
Issue number3
StatePublished - 1995


  • acute phase
  • high density lipoprotein

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology


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