Effects of bile salts on glucosylceramide containing membranes

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)


Interna författare/redaktörer


Publikationens författare: Halin J, Mattjus P
Förläggare: ELSEVIER SCIENCE BV
Publiceringsår: 2011
Tidskrift: BBA - Biomembranes
Tidskriftsakronym: BBA-BIOMEMBRANES
Volym: 1808
Nummer: 12
Artikelns första sida, sidnummer: 2886
Artikelns sista sida, sidnummer: 2893
Antal sidor: 8
ISSN: 0005-2736


Abstrakt

The glycolipid transfer protein (GLTP) is capable of transporting glycolipids from a donor membrane, through the aqueous environment, to an acceptor membrane. The GLTP mediated glycolipid transfer from sphingomyelin membranes is very slow. In contrast, the transfer is fast from membranes composed of phosphatidylcholine. The lateral glycolipid membrane organization is known to be driven by their tendency to mix non-randomly with different membrane lipids. Consequently, the properties of the membrane lipids surrounding the glycolipids play an important role in the ability of GLTP to bind and transfer its substrates. Since GLTP transfer of glycolipids is almost nonexistent from sphingomyelin membranes, we have used this exceptionality to investigate if membrane intercalators can alter the membrane packing and induce glycolipid transfer. We found that the bile salts cholate, deoxycholate, taurocholate and taurodeoxycholate, cause glucosylceramide to become transferrable by GLTP. Other compounds, such as single chain lipids, ceramide and nonionic surfactants, that have membrane-perturbing effects, did not affect the transfer capability of GLTP. We speculate that the strong hydrogen bonding network formed in the interfacial region of glycosphingolipid-sphingomyelin membranes is disrupted by the membrane partition of the bile salts causing the glycosphingolipid to become transferrable.


Nyckelord

BODIPY-labeled lipid, Glucosylceramide, Glycolipid, Glycolipid transfer protein, Hydrogen bond, Lipid lateral packing

Senast uppdaterad 2019-10-12 vid 03:38