Current Atherosclerosis Reports

, Volume 2, Issue 1, pp 36–46

Mechanism of action of niacin on lipoprotein metabolism

  • Vaijinath S. Kamanna
  • Moti L. Kashyap
Article

DOI: 10.1007/s11883-000-0093-1

Cite this article as:
Kamanna, V.S. & Kashyap, M.L. Curr Atheroscler Rep (2000) 2: 36. doi:10.1007/s11883-000-0093-1

Abstract

It is generally accepted that the increased concentrations of apolipoprotein (apo) B containing very low-density lipoproteins (VLDL) and low-density lipoproteins (LDL), and decreased levels of apo AI containing high-density lipoproteins (HDL) are correlated to atherosclerotic cardiovascular disease. Current evidence indicates that the post-translational apo-B degradative processes regulate the hepatic assembly and secretion of VLDL and the subsequent generation of LDL particles. The availability of triglycerides (TG) for the addition to apo B during intracellular processing appears to play a central role in targeting apo B for either intracellular degradation or assembly and secretion as VLDL particles. Based on the availability of TG, the liver secretes either dense TG-poor VLDL2 or large TG-rich VLDL1 particles, and these particles serve as precursors for the formation of more buoyant or small, dense LDL particles by lipid transfer protein- and hepatic lipase-mediated processes. HDLs are a heterogenous class of lipoproteins, and apo AI (the major protein of HDL) participates in reverse cholesterol transport, a process by which excess cholesterol is eliminated. Recent studies indicate that HDL particles containing only apo A-I (LPA-I) are more effective in reverse cholesterol transport and more anti-atherogenic than HDL particles containing both apo A-I and apo A-II (LPA-I+A-II).

Copyright information

© Current Science Inc 2000

Authors and Affiliations

  • Vaijinath S. Kamanna
    • 1
  • Moti L. Kashyap
    • 2
  1. 1.Department of Medicine (Gerontology)University of CaliforniaIrvineUSA
  2. 2.Department of Veterans Affairs Healthcare SystemCholesterol Research CenterLong BeachUSA