Structural analyses of apolipoprotein A-IV polymorphisms Q360H and T347S elucidate the inhibitory effect against thrombosis.

ABSTRACT: Apolipoprotein A-IV (apoA-IV) is an abundant lipid-binding protein in blood plasma. We previously reported that apoA-IV, as an endogenous inhibitor, competitively binds platelet αIIbβ3 integrin from its N-terminal residues, reducing the potential risk of thrombosis. This study aims to investigate how the apoA-IV^Q360H and apoA-IV^T347S mutations affect the structure and function of apoA-IV. These mutations are linked to increased risk of cardiovascular diseases because of multiple single-nucleotide polymorphisms in the C-terminal region of apoA-IV. We postulate that the structural hindrance caused by the C-terminal motifs may impede the binding of apoA-IV to platelets at its N-terminal binding site. However, the mechanistic impact of Q360H and T347S polymorphisms on thi

SUBMITTER: Shoara AA 

PROVIDER: S-EPMC12017984 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature