Metabolism of PLTP, CETP, and LCAT on multiple HDL sizes using the Orbitrap Fusion Lumos.

摘要: Recent in vivo tracer studies demonstrated that targeted mass spectrometry (MS) on the Q Exactive Orbitrap could determine metabolism of HDL proteins 100s-fold less abundant than apolipoprotein A1 (APOA1). In this study, we demonstrate Lumos can measure whose abundances are 1000s-fold APOA1, specifically lipid transfer phospholipid protein (PLTP), cholesterol ester (CETP), and lecithin-cholesterol acyl transferase (LCAT). Relative to Exactive, improved detection by reducing enrichment compression, thereby providing consistent data across multiple sizes from 6 participants. We determined compartmental modeling PLTP is secreted medium large (alpha2, alpha1, alpha0) transferred larger during circulation where it catabolized. CETP mainly alpha1 alpha2 remains these circulation. LCAT small alpha3, prebeta). Unlike CETP, LCAT's appearance markedly delayed, indicating may reside for a time outside systemic before attaching plasma. The determination proteins' unique metabolic structures was possible due advances MS technologies.