Serum amyloid A (SAA) is a family of ancient proteins that can be traced from present-day humans back half a billion years to sea cucumbers and oysters. A new study by researchers from the Boston University Chobanian & Avedisian School of Medicine explores the link between the dual nature of this small plasma protein: how it works to clear toxic debris from wounds and inflammation sites, but also its role in forming fibrous deposits of the pathologic amyloid in vital organs such as the kidney and liver in the life-threatening disease AA amyloidosis.
detergent more potent than bile," said Shobini Jayaraman, Ph.D., senior staff scientist in pharmacology, physiology & biophysics and the lead author of this study.
"This finding solidifies our theory that SAA clears cell membrane debris from the sites of injury and inflammation in animals and humans," said Olga Gursky, Ph.D., professor of pharmacology, physiology & biophysics, the senior author of the study and the principal investigator on the NIH grant that supports this research.
The study found that secretory phospholipase A2, an inflammatory enzyme that raises in blood together with SAA and acts synergistically with it in removing cell membrane debris, can also promote SAA amyloid deposition, said Jayaraman. The dual nature of proteins that both transport lipids and form amyloids is present in other diseases, like Alzheimer's amyloid-beta peptide. Apolipoprotein A-I, the major protein in"good cholesterol," can also form pathologic amyloids resulting in atherosclerosis and systemic amyloidosis, said Gursky.
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