Apolipoprotein M associates to lipoproteins through its retained signal peptide.

Olof Axler; Josefin Ahnström; Björn Dahlbäck

doi:10.1016/j.febslet.2008.02.007

Apolipoprotein M associates to lipoproteins through its retained signal peptide.

Olof Axler, Josefin Ahnström, Björn Dahlbäck

Clinical Chemistry, Malmö

Research output: Contribution to journal › Article › peer-review

171 Downloads (Pure)

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.

Original language	English
Pages (from-to)	826-828
Journal	FEBS Letters
Volume	582
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2008.02.007
Publication status	Published - 2008

Subject classification (UKÄ)

Biological Sciences

Access to Document

10.1016/j.febslet.2008.02.007

DahlbackElsevier

http://www.ncbi.nlm.nih.gov/pubmed/18279674?dopt=Abstract

Cite this

@article{9951c7b2b69f47cc8264e24805a5c66b,

title = "Apolipoprotein M associates to lipoproteins through its retained signal peptide.",

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 = "Olof Axler and Josefin Ahnstr{\"o}m and Bj{\"o}rn Dahlb{\"a}ck",

year = "2008",

doi = "10.1016/j.febslet.2008.02.007",

language = "English",

volume = "582",

pages = "826--828",

journal = "FEBS Letters",

issn = "1873-3468",

publisher = "Wiley-Blackwell",

number = "5",

}

TY - JOUR

T1 - Apolipoprotein M associates to lipoproteins through its retained signal peptide.

AU - Axler, Olof

AU - Ahnström, Josefin

AU - Dahlbäck, Björn

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/39649100855

U2 - 10.1016/j.febslet.2008.02.007

DO - 10.1016/j.febslet.2008.02.007

M3 - Article

C2 - 18279674

SN - 1873-3468

VL - 582

SP - 826

EP - 828

JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

Apolipoprotein M associates to lipoproteins through its retained signal peptide.

Abstract

Subject classification (UKÄ)

Access to Document

Other files and links

Fingerprint

Apolipoprotein M – Studies of Structure and Function

APOLIPOPROTEIN M

Cite this