The use of styrene-maleic acid copolymer (SMA) for studies on T cell membrane rafts
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
30463696
DOI
10.1016/j.bbamem.2018.08.006
PII: S0005-2736(18)30237-2
Knihovny.cz E-zdroje
- Klíčová slova
- GPI-anchored proteins, Membrane proteins, Membrane rafts, SMA, Src family kinases, T lymphocytes,
- MeSH
- anizotropie MeSH
- buněčná membrána chemie MeSH
- cholesterol chemie MeSH
- detergenty chemie MeSH
- gelová chromatografie MeSH
- Jurkat buňky MeSH
- lidé MeSH
- lipidové dvojvrstvy chemie MeSH
- lipidy chemie MeSH
- maleáty chemie MeSH
- mastné kyseliny chemie MeSH
- membránové mikrodomény chemie MeSH
- membránové proteiny chemie MeSH
- membrány umělé MeSH
- myši inbrední C57BL MeSH
- myši MeSH
- polymery chemie MeSH
- radiační rozptyl MeSH
- rozpustnost MeSH
- styren chemie MeSH
- světlo MeSH
- T-lymfocyty cytologie MeSH
- ultracentrifugace MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- cholesterol MeSH
- detergenty MeSH
- lipidové dvojvrstvy MeSH
- lipidy MeSH
- maleáty MeSH
- maleic acid MeSH Prohlížeč
- mastné kyseliny MeSH
- membránové proteiny MeSH
- membrány umělé MeSH
- polymery MeSH
- styren MeSH
An emerging alternative to the use of detergents in biochemical studies on membrane proteins is apparently the use styrene-maleic acid (SMA) amphipathic copolymers. These cut the membrane into nanodiscs (SMA-lipid particles, SMALPs), which contain membrane proteins possibly surrounded by their native lipid environment. We examined this approach for studies on several types of T cell membrane proteins, previously defined as raft or non-raft associated, to see whether the properties of the raft derived SMALPs differ from non-raft SMALPs. Our results indicate that two types of raft proteins, GPI-anchored proteins and two Src family kinases, are markedly present in membrane fragments much larger (>250 nm) than those containing non-raft proteins (<20 nm). Lipid probes sensitive to membrane fluidity (membrane order) indicate that the lipid environment in the large SMALPs is less fluid (more ordered) than in the small ones which may indicate the presence of a more ordered lipid Lo phase which is characteristic of membrane rafts. Also the lipid composition of the small vs. large SMALPs is markedly different - the large ones are enriched in cholesterol and lipids containing saturated fatty acids. In addition, we confirm that T cell membrane proteins present in SMALPs can be readily immunoisolated. Our results support the use of SMA as a potentially better (less artifact prone) alternative to detergents for studies on membrane proteins and their complexes, including membrane rafts.
Institute of Physiology of the Czech Academy of Sciences Vídeňská 1083 142 20 Praha 4 Czech Republic
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