Lipoprotein Particles Interact with Membranes and Transfer Their Cargo without Receptors
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00118331" target="_blank" >RIV/00216224:14740/20:00118331 - isvavai.cz</a>
Výsledek na webu
<a href="https://pubs.acs.org/doi/10.1021/acs.biochem.0c00748" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.biochem.0c00748</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.biochem.0c00748" target="_blank" >10.1021/acs.biochem.0c00748</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Lipoprotein Particles Interact with Membranes and Transfer Their Cargo without Receptors
Popis výsledku v původním jazyce
Lipid transfer from lipoprotein particles to cells is essential for lipid homeostasis. High-density lipoprotein (HDL) particles are mainly captured by cell membrane-associated scavenger receptor class B type 1 (SR-B1) from the bloodstream, while low-density and very-low-density lipoprotein (LDL and VLDL, respectively) particles are mostly taken up by receptor-mediated endocytosis. However, the role of the target lipid membrane itself in the transfer process has been largely neglected so far. Here, we study how lipoprotein particles (HDL, LDL, and VLDL) interact with synthetic lipid bilayers and cell-derived membranes and transfer their cargo subsequently. Employing cryoelectron microscopy, spectral imaging, and fluorescence (cross correlation spectroscopy allowed us to observe integration of all major types of lipoprotein particles into the membrane and delivery of their cargo in a receptor-independent manner. Importantly, the biophysical properties of the target cell membranes change upon delivery of cargo. The concept of receptor-independent interaction of lipoprotein particles with membranes helps us to better understand lipoprotein particle biology and can be exploited for novel treatments of dyslipidemia diseases.
Název v anglickém jazyce
Lipoprotein Particles Interact with Membranes and Transfer Their Cargo without Receptors
Popis výsledku anglicky
Lipid transfer from lipoprotein particles to cells is essential for lipid homeostasis. High-density lipoprotein (HDL) particles are mainly captured by cell membrane-associated scavenger receptor class B type 1 (SR-B1) from the bloodstream, while low-density and very-low-density lipoprotein (LDL and VLDL, respectively) particles are mostly taken up by receptor-mediated endocytosis. However, the role of the target lipid membrane itself in the transfer process has been largely neglected so far. Here, we study how lipoprotein particles (HDL, LDL, and VLDL) interact with synthetic lipid bilayers and cell-derived membranes and transfer their cargo subsequently. Employing cryoelectron microscopy, spectral imaging, and fluorescence (cross correlation spectroscopy allowed us to observe integration of all major types of lipoprotein particles into the membrane and delivery of their cargo in a receptor-independent manner. Importantly, the biophysical properties of the target cell membranes change upon delivery of cargo. The concept of receptor-independent interaction of lipoprotein particles with membranes helps us to better understand lipoprotein particle biology and can be exploited for novel treatments of dyslipidemia diseases.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biochemistry
ISSN
0006-2960
e-ISSN
—
Svazek periodika
59
Číslo periodika v rámci svazku
45
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
8
Strana od-do
4421-4428
Kód UT WoS článku
000592835200010
EID výsledku v databázi Scopus
2-s2.0-85096347640