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Titel
Low density lipoproteins as circulating fast temperature sensors
VerfasserPrassl, Ruth ; Pregetter, Magdalena ; Amenitsch, Heinz ; Kriechbaum, Manfred ; Schwarzenbacher, Robert ; Chapman, John M. ; Laggner, Peter
Erschienen in
PLoS ONE, Lawrence, Kan., 2008, Jg. 3, S. 1-8
ErschienenPublic Library of Science, 2008
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
Schlagwörter (EN)Lipids / Body temperature / Cholesteryl esters / Transition temperature / Lasers / Small-angle scattering / Blood / Melting
Projekt-/ReportnummerP-16479-CHE
Projekt-/ReportnummerP-20455-B12
ISSN1932-6203
URNurn:nbn:at:at-ubs:3-6028 Persistent Identifier (URN)
DOI10.1371/journal.pone.0004079 
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Low density lipoproteins as circulating fast temperature sensors [0.25 mb]
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Zusammenfassung (Englisch)

Background: The potential physiological significance of the nanophase transition of neutral lipids in the core of low density lipoprotein (LDL) particles is dependent on whether the rate is fast enough to integrate small (2C) temperature changes in the blood circulation. Methodology/Principal Findings: Using sub-second, time-resolved small-angle X-ray scattering technology with synchrotron radiation, we have monitored the dynamics of structural changes within LDL, which were triggered by temperature-jumps and -drops, respectively. Our findings reveal that the melting transition is complete within less than 10 milliseconds. The freezing transition proceeds slowly with a half-time of approximately two seconds. Thus, the time period over which LDL particles reside in cooler regions of the body readily facilitates structural reorientation of the apolar core lipids. Conclusions/Significance: Low density lipoproteins, the biological nanoparticles responsible for the transport of cholesterol in blood, are shown to act as intrinsic nano-thermometers, which can follow the periodic temperature changes during blood circulation. Our results demonstrate that the lipid core in LDL changes from a liquid crystalline to an oily state within fractions of seconds. This may, through the coupling to the protein structure of LDL, have important repercussions on current theories of the role of LDL in the pathogenesis of atherosclerosis.