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Apolipoprotein M associates to lipoproteins through its retained signal peptide.

Axler, Olof LU ; Ahnström, Josefin LU and Dahlbäck, Björn LU (2008) In FEBS Letters 582(5). p.826-828
Abstract
Apolipoprotein M (apoM) is predominantly associated with HDL. In this study, it was investigated whether apoM's uncleaved signal peptide is necessary for the protein's ability to associate with lipoproteins. ApoM with a cleavable signal peptide, Q22A, was expressed, together with wild-type apoM, in HEK293 cells. On size-exclusion chromatography, the elution profile of wild-type apoM was similar to that of human HDL-associated plasma apoM. In contrast, the size of the Q22A mutant corresponded to free, unassociated apoM. This strongly indicates that the signal peptide is indeed necessary for apoM's ability to associate with lipid.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEBS Letters
volume
582
issue
5
pages
826 - 828
publisher
Wiley-Blackwell
external identifiers
  • PMID:18279674
  • WOS:000257670100048
  • Scopus:39649100855
ISSN
1873-3468
DOI
10.1016/j.febslet.2008.02.007
language
English
LU publication?
yes
id
9951c7b2-b69f-47cc-8264-e24805a5c66b (old id 1041863)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18279674?dopt=Abstract
date added to LUP
2008-03-03 13:30:06
date last changed
2016-10-13 04:29:25
@misc{9951c7b2-b69f-47cc-8264-e24805a5c66b,
  abstract     = {Apolipoprotein M (apoM) is predominantly associated with HDL. In this study, it was investigated whether apoM's uncleaved signal peptide is necessary for the protein's ability to associate with lipoproteins. ApoM with a cleavable signal peptide, Q22A, was expressed, together with wild-type apoM, in HEK293 cells. On size-exclusion chromatography, the elution profile of wild-type apoM was similar to that of human HDL-associated plasma apoM. In contrast, the size of the Q22A mutant corresponded to free, unassociated apoM. This strongly indicates that the signal peptide is indeed necessary for apoM's ability to associate with lipid.},
  author       = {Axler, Olof and Ahnström, Josefin and Dahlbäck, Björn},
  issn         = {1873-3468},
  language     = {eng},
  number       = {5},
  pages        = {826--828},
  publisher    = {ARRAY(0x8408868)},
  series       = {FEBS Letters},
  title        = {Apolipoprotein M associates to lipoproteins through its retained signal peptide.},
  url          = {http://dx.doi.org/10.1016/j.febslet.2008.02.007},
  volume       = {582},
  year         = {2008},
}