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Serum amyloid A (SAA) is a multi-gene family consisting of highly conserved protein sequences that are known to cluster on chromosome 11 in humans [1] and chromosome 7 in mice [2]. The acute-phase proteins SAA1 and SAA2 (mass of ~12 kDa, 104 amino acids) share > 93% identity in primary sequence structure, are secreted predominantly by hepatocytes and are induced by a broad spectrum of inflammatory cytokines [3]. Extra-hepatic production of acute-phase SAA occurs in many organs and tissues of body including vascular smooth muscle cells and endothelial cells (EC) that are also capable of secreting SAA [4, 5]. By contrast, SAA4 is a glycosylated form that is constitutively produced in a wide range of (histologically) normal tissues and cells [6]. The final isoform, SAA3, is a pseudogene that is not transcribed in humans [1]. In rodents, SAA3 is a functional protein that is expressed in extra-hepatic cells, such as macrophages and adipocytes in response to prolactin or lipolysaccaride (LPS) stimuli thereby, contributing to local inflammation in adipose tissues [7, 8].

Role of SAA in Promoting Endothelial Activation: Inhibition by High-Density Lipoprotein