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In vivo stable-isotope kinetic study suggests intracellular assembly of lipoprotein(a).

Abstract：

OBJECTIVE:Lipoprotein(a) [Lp(a)] consists of apolipoprotein B-100 (apoB-100) as part of an LDL-like particle and the covalently linked glycoprotein apolipoprotein(a) [apo(a)]. Detailed mechanisms of its biosynthesis, assembly, secretion and catabolism are still poorly understood. To address the Lp(a) assembly mechanism, we studied the in vivo kinetics of apo(a) and apoB-100 from Lp(a) and LDL apoB-100 in nine healthy probands using stable-isotope methodology. METHODS:The level of isotope enrichment was used to calculate the fractional synthesis rate (FSR), production rate (PR) and retention time (RT) using SAAMII software and multicompartmental modeling. RESULTS:We observed a similar mean PR for apo(a) (1.15 nmol/kg/d) and apoB-100 (1.31 nmol/kg/d) from Lp(a), which differed significantly from the PR for apoB-100 from LDL (32.6 nmol/kg/d). Accordingly, mean FSR and RT values for Lp(a)-apo(a) were similar to those of Lp(a)-apoB and different from those for LDL-apoB. CONCLUSION:Two different kinetic apoB pools within Lp(a) and LDL suggest intracellular Lp(a) assembly from apo(a) and newly synthesized LDL.

journal_name

Atherosclerosis

journal_title

Atherosclerosis

authors

Frischmann ME,Ikewaki K,Trenkwalder E,Lamina C,Dieplinger B,Soufi M,Schweer H,Schaefer JR,König P,Kronenberg F,Dieplinger H

doi

10.1016/j.atherosclerosis.2012.09.031

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

322-7

issue

2

eissn

0021-9150

issn

1879-1484

pii

S0021-9150(12)00649-1

journal_volume

225

pub_type

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