Rapid clearance of serum amyloid a from high-density lipoproteins

Bausserman, Linda; Herbert, Peter N.; Rodger, R F; Nicolosi, Robert J.

doi:10.1016/0005-2760(84)90221-2

Cited by 45 publications

(23 citation statements)

References 28 publications

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“…It has also been demonstrated that oxidized low density lipoprotein induces acute phase SAA, thus suggesting that SAA participates in vascular injury and atherosclerosis (43). According to previous reports, low concentrations of SAA are associated with HDLs; however, free SAA is also found at higher concentrations of SAA in the circulation (44,45). Marked increases in SAA have been used as an important indicator of the presence of inflammatory diseases such as atherosclerosis (46).…”

Section: Discussionmentioning

confidence: 96%

Serum Amyloid A Induces CCL2 Production via Formyl Peptide Receptor-Like 1-Mediated Signaling in Human Monocytes

Lee

Kim

Shim

et al. 2008

The Journal of Immunology

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Although the presence of an elevated level of serum amyloid A (SAA) has been regarded as a cardiovascular risk factor, the role of SAA on the progress of atherosclerosis has not been fully elucidated. In the present study, we investigated the effect of SAA on the production of CCL2, an important mediator of monocyte recruitment, and the mechanism underlying the action of SAA in human monocytes. The stimulation of human monocytes with SAA elicited CCL2 production in a concentration-dependent manner. The production of CCL2 by SAA was found to be mediated by the activation of NF-κB. Moreover, the signaling events induced by SAA included the activation of ERK and the induction of cyclooxygenase-2, which were required for the production of CCL2. Moreover, SAA-induced CCL2 induction was inhibited by a formyl peptide receptor-like 1 (FPRL1) antagonist. We also found that the stimulation of FPRL1-expressing RBL-2H3 cells induced CCL2 mRNA accumulation, but the vector-expressing RBL-2H3 cells combined with SAA did not. Taken together, our findings suggest that SAA stimulates CCL2 production and, thus, contributes to atherosclerosis. Moreover, FPRL1 was found to be engaged in SAA-induced CCL2 induction, and cyclooxygenase-2 induction was found to be essential for SAA-induced CCL2 expression. These results suggest that SAA and FPRL1 offer a developmental starting point for the treatment of atherosclerosis.

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Section: Discussionmentioning

confidence: 96%

Serum Amyloid A Induces CCL2 Production via Formyl Peptide Receptor-Like 1-Mediated Signaling in Human Monocytes

Lee

Kim

Shim

et al. 2008

The Journal of Immunology

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“…In the blood, SAA is associated with high density lipoproteins, but it dissociates from lipoproteins at higher concentrations (36,37). Free SAA was also detected in cultured vascular cells (8) and rheumatoid arthritis synovial tissues (9).…”

Section: Discussionmentioning

confidence: 99%

Aspirin-Triggered Lipoxins Override the Apoptosis-Delaying Action of Serum Amyloid A in Human Neutrophils: A Novel Mechanism for Resolution of Inflammation

Kebir

József

Khreiss

et al. 2007

The Journal of Immunology

127

157

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Myeloperoxidase (MPO), a heme protein abundantly expressed in the azurophilic granules in neutrophils generates cytotoxic oxidants and signals through the adhesion molecule CD11b/CD18 (Mac‐1) to activate and rescue neutrophils from apoptosis. Since aspirin‐triggered 15‐epi‐lipoxin A4 (15‐epi‐LXA4) inhibits Mac‐1‐mediated neutrophil adhesion, we studied its impact on MPO suppression of neutrophil apoptosis. Pretreatment of neutrophils with 15‐epi‐LXA4 or its metabolically stable analog 15‐epi‐16‐p‐fluorophenoxy‐LXA4 through downregulation of surface expression of Mac‐1 and inhibition of MPO release overcame the powerful anti‐apoptosis signal from MPO. 15‐epi‐LXA4 promoted apoptosis by attenuating MPO‐induced concurrent activation of ERK and phosphatidylinositol 3‐kinase/Akt‐mediated phosphorylation of Bad and reducing the expression of the anti‐apoptotic protein Mcl‐1. These led to collapse of mitochondrial transmembrane potential, cytochrome c release, resulting in increased caspase‐3 activity. The pro‐apoptotic action of 15‐epi‐LXA4 was predominant over MPO‐mediated effects even when 15‐epi‐LXA4 was added at 4‐hour post‐MPO. 15‐epi‐LXA4 did not inhibit the catalytic activity of MPO. Our results indicate that through overriding the MPO survival signal, aspirin‐triggered lipoxins may prevent neutrophil‐mediated tissue injury. (Grant support: CIHR MOP‐64283).

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“…Several studies have investigated SAA catabolism in mice (30,31) and in monkeys (32,33). Because SAA1.1 and SAA2.1 are present in the same lipoprotein fraction in plasma and have a similar molecular mass, as well as amino acid sequence, it has been difficult to determine plasma degradation rates of these individual isoforms in naturally occurring HDL.…”

Section: Lipoprotein Cholesterol Distributionsmentioning

confidence: 99%

Impact of individual acute phase serum amyloid A isoforms on HDL metabolism in mice

Kim

Beer

Wroblewski

et al. 2016

Journal of Lipid Research

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Rapid clearance of serum amyloid a from high-density lipoproteins

Cited by 45 publications

References 28 publications

Serum Amyloid A Induces CCL2 Production via Formyl Peptide Receptor-Like 1-Mediated Signaling in Human Monocytes

Serum Amyloid A Induces CCL2 Production via Formyl Peptide Receptor-Like 1-Mediated Signaling in Human Monocytes

Aspirin-Triggered Lipoxins Override the Apoptosis-Delaying Action of Serum Amyloid A in Human Neutrophils: A Novel Mechanism for Resolution of Inflammation

Impact of individual acute phase serum amyloid A isoforms on HDL metabolism in mice

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