Lp(a) (lipoprotein[a]) is associated with cardiovascular disease, but neither the causal nature nor the underlying mechanisms are fully documented. This study investigated whether Lp(a) triggers ather Show more
Lp(a) (lipoprotein[a]) is associated with cardiovascular disease, but neither the causal nature nor the underlying mechanisms are fully documented. This study investigated whether Lp(a) triggers atherogenesis by dysregulating vascular redox-sensitive inflammatory state. Plasma Lp(a) was measured in 1027 patients with advanced coronary artery disease undergoing cardiac surgery. These patients were genotyped, and a modified Increased plasma Lp(a) ( This study demonstrates for the first time that a genetically determined increase in plasma Lp(a) results in dysregulated vascular redox/nitrosative signaling in patients with atherosclerosis. Show less
This study uses label-free methods to determine the binding interactions of lysophosphatidic acid (LPA) with bovine and human serum albumin (BSA and HSA). LPA is a bioactive lysophospholipid (LysoPL) Show more
This study uses label-free methods to determine the binding interactions of lysophosphatidic acid (LPA) with bovine and human serum albumin (BSA and HSA). LPA is a bioactive lysophospholipid (LysoPL) that signals through a G-protein-coupled receptor (GPCR). Plasma LPAs are primarily carried by albumin; however, their binding interactions with the carrier protein (HSA) are not as well studied as those with fatty acids, drugs, or metal ions. Therefore, the aim of this study is to determine the binding sites of LPA in serum albumin through spectroscopic methods. Intrinsic fluorescence quenching experiments in conjunction with a label-free, free solution light interferometric assay have been employed to determine the binding Show less