The use of styrene-maleic acid copolymer (SMA) for studies on T cell membrane rafts

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F19%3A00501169" target="_blank" >RIV/67985823:_____/19:00501169 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/19:00501169 RIV/61388955:_____/19:00501169 RIV/68378050:_____/19:00501169

Result on the web

<a href="https://doi.org/10.1016/j.bbamem.2018.08.006" target="_blank" >https://doi.org/10.1016/j.bbamem.2018.08.006</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbamem.2018.08.006" target="_blank" >10.1016/j.bbamem.2018.08.006</a>

Result language

angličtina

Original language name

The use of styrene-maleic acid copolymer (SMA) for studies on T cell membrane rafts

Original language description

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 L-o 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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10406 - Analytical chemistry

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochimica Et Biophysica Acta-Biomembranes

ISSN

0005-2736

e-ISSN

—

Volume of the periodical

1861

Issue of the periodical within the volume

1

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

12

Pages from-to

130-141

UT code for WoS article

000451494500015

EID of the result in the Scopus database

2-s2.0-85051646885