Advanced

HDL Stimulates apoM Secretion.

Ahnström, Josefin LU ; Axler, Olof LU and Dahlbäck, Björn LU (2010) In Protein Peptide Letters Jul 1. p.1285-1289
Abstract
Apolipoprotein M (apoM) in human plasma is mainly associated with HDL. A retained signal peptide anchors apoM to the lipoproteins. To investigate the role of the signal peptide in the transfer of apoM from the synthesizing cell to the lipoproteins, wildtype apoM cDNA and the Q(22)A mutant, introducing a signal peptidase cleavage site, were used to stably transfect HEK293 cells, which intrinsically do not express apolipoproteins. When cultured under serum-free conditions, wildtype apoM was, in contrast to Q(22)A, poorly secreted. Addition of serum or purified HDL stimulated secretion of wildtype apoM, which was recovered in the medium incorporated in HDL. The liver cell line HepG2, which synthesizes HDL, was cultured under serum-free... (More)
Apolipoprotein M (apoM) in human plasma is mainly associated with HDL. A retained signal peptide anchors apoM to the lipoproteins. To investigate the role of the signal peptide in the transfer of apoM from the synthesizing cell to the lipoproteins, wildtype apoM cDNA and the Q(22)A mutant, introducing a signal peptidase cleavage site, were used to stably transfect HEK293 cells, which intrinsically do not express apolipoproteins. When cultured under serum-free conditions, wildtype apoM was, in contrast to Q(22)A, poorly secreted. Addition of serum or purified HDL stimulated secretion of wildtype apoM, which was recovered in the medium incorporated in HDL. The liver cell line HepG2, which synthesizes HDL, was cultured under serum-free conditions and found to secrete apoM as part of an HDL-like particle. In conclusion, due to its retained signal peptide, apoM is poorly secreted unless HDL is either coexpressed or added to the culture medium. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Protein Peptide Letters
volume
Jul 1
pages
1285 - 1289
publisher
Bentham Science Publishers
external identifiers
  • wos:000281430400015
  • pmid:20518736
  • scopus:77958457557
ISSN
0929-8665
language
English
LU publication?
yes
id
86f4ef65-67ee-4488-aecf-3aebb9e50abd (old id 1626429)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/20518736?dopt=Abstract
date added to LUP
2010-07-05 09:34:58
date last changed
2018-05-29 11:06:23
@article{86f4ef65-67ee-4488-aecf-3aebb9e50abd,
  abstract     = {Apolipoprotein M (apoM) in human plasma is mainly associated with HDL. A retained signal peptide anchors apoM to the lipoproteins. To investigate the role of the signal peptide in the transfer of apoM from the synthesizing cell to the lipoproteins, wildtype apoM cDNA and the Q(22)A mutant, introducing a signal peptidase cleavage site, were used to stably transfect HEK293 cells, which intrinsically do not express apolipoproteins. When cultured under serum-free conditions, wildtype apoM was, in contrast to Q(22)A, poorly secreted. Addition of serum or purified HDL stimulated secretion of wildtype apoM, which was recovered in the medium incorporated in HDL. The liver cell line HepG2, which synthesizes HDL, was cultured under serum-free conditions and found to secrete apoM as part of an HDL-like particle. In conclusion, due to its retained signal peptide, apoM is poorly secreted unless HDL is either coexpressed or added to the culture medium.},
  author       = {Ahnström, Josefin and Axler, Olof and Dahlbäck, Björn},
  issn         = {0929-8665},
  language     = {eng},
  pages        = {1285--1289},
  publisher    = {Bentham Science Publishers},
  series       = {Protein Peptide Letters},
  title        = {HDL Stimulates apoM Secretion.},
  volume       = {Jul 1},
  year         = {2010},
}