Apolipoprotein M associates to lipoproteins through its retained signal peptide.
Author
Summary, in English
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.
Department/s
Publishing year
2008
Language
English
Pages
826-828
Publication/Series
FEBS Letters
Volume
582
Issue
5
Full text
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Links
Document type
Journal article
Publisher
Wiley-Blackwell
Topic
- Biological Sciences
Status
Published
Research group
- Clinical Chemistry, Malmö
ISBN/ISSN/Other
- ISSN: 1873-3468