Scientists have shown that a protein called transthyretin (TTR) that is present in the blood may accelerate the development of atherosclerosis -- a potentially fatal heart disease in which the arteries are progressively narrowed and hardened over time, reducing blood flow to the heart.
TTR has been shown to cleave a blood compound called apolipoprotein A-I (ApoA-I), which can produce structures called fibrils that are shaped like strands and accumulate in blood vessels. These fibrils have been observed in people with a mutation of the gene that makes ApoA-I, but whether cleavage by TTR promotes the formation of such fibrils has not been assessed yet.
Monica Mendes Sousa and colleagues determined that when ApoA-I is cleaved by TTR, it tends to form fibrils faster than the uncleaved ApoA-I. This discovery may provide new ways to treat people with atherosclerosis by stopping TTR from cleaving ApoA-I and slowing down the formation of fibrils in blood vessels
Article: "ApoA-I cleaved by transthyretin has reduced ability to promote cholesterol efflux and increased amyloidogenicity," by Marcia Almeida Liz, Claudio M. Gomes, Maria Joao Saraiva, and Monica Mendes SousaNovember 2007 issue of the Journal of Lipid Research (Vol. 48, No. 11)
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