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As the sPLA 2 breaks up these particles, SAA then gathers up and gets rid of the leftover toxic fragments. This revealed that SAA reshapes the lipid membrane into smaller вЂnanoparticlesвЂ™ with tightly curved surfaces that are easier for sPLA 2 to break down. mixed mouse SAA with vesicles of membrane lipids, and then added sPLA 2. to ask whether SAA and sPLA 2 might be working together to clean up the cell membrane debris. Notably, sPLA 2 levels rise at the same time and place as SAA during inflammation. This protein, also known as sPLA 2, is part of a big family of enzymes that break down lipids in the cell membrane. One clue for how SAA works is its relationship to another ancient protein called secretory phospholipase A 2. But, it is not entirely clear how this protein works. Combined with the fact SAA has been conserved for over 500 million years, this suggests that SAA must be important for survival. In humans, SAA levels in the blood rapidly spike to over a thousand times their normal level following inflammation, injury or infection. A small protein called serum amyloid A, SAA for short, was recently proposed to play a pivotal role in this process. These broken fragments of membrane become highly toxic, and must be removed as soon as possible to allow the tissue to heal. When cells get severely damaged, their lipid membranes break apart. eLife digestД¬ell boundaries are made up of fatty substances known as lipids.

We postulate that the removal of lipids and their degradation products constitutes a vital primordial role of SAA in innate immunity this role remains to be tested in vivo. Consequently, SAA and sPLA 2 can act synergistically to remove cellular membrane debris from injured sites, which is a prerequisite for tissue healing. Therefore, SAA solubilized lipid bilayers to generate substrates for sPLA 2 and removed its bioactive products.

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Unlike albumin, SAA effectively removed free fatty acids under acidic conditions, which characterize inflammation sites.

Moreover, SAA sequestered free fatty acids and lysophospholipids to form stable proteolysis-resistant complexes. SAA solubilized phospholipid bilayers to form lipoproteins that provided substrates for sPLA 2. SAA increases simultaneously with secretory phospholipase A 2 (sPLA 2), compelling us to determine how SAA influences sPLA 2 hydrolysis of lipoproteins. In acute inflammation, SAA plasma levels increase ~1,000 fold, suggesting that this protein family has a vital beneficial role. Serum amyloid A (SAA) is an evolutionally conserved enigmatic biomarker of inflammation.