Apolipoprotein M associates to lipoproteins through its retained signal peptide.
Författare
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.
Avdelning/ar
Publiceringsår
2008
Språk
Engelska
Sidor
826-828
Publikation/Tidskrift/Serie
FEBS Letters
Volym
582
Issue
5
Fulltext
- Available as PDF - 137 kB
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Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Wiley-Blackwell
Ämne
- Biological Sciences
Status
Published
Forskningsgrupp
- Clinical Chemistry, Malmö
ISBN/ISSN/Övrigt
- ISSN: 1873-3468