PMID- 21780815
OWN - NLM
STAT- MEDLINE
DCOM- 20120117
LR  - 20211020
IS  - 1520-5207 (Electronic)
IS  - 1520-6106 (Print)
IS  - 1520-5207 (Linking)
VI  - 115
IP  - 35
DP  - 2011 Sep 8
TI  - 2D-ELDOR study of heterogeneity and domain structure changes in plasma membrane 
      vesicles upon cross-linking of receptors.
PG  - 10462-9
LID - 10.1021/jp2016243 [doi]
AB  - 2D electron-electron double resonance (2D-ELDOR) with the "full Sc-" method of 
      analysis is applied to the study of plasma membrane vesicles. Membrane structural 
      changes upon antigen cross-linking of IgE receptors (IgE-FcepsilonRI) in plasma 
      membrane vesicles (PMVs) isolated from RBL-2H3 mast cells are investigated, for 
      the first time, by means of these 2D-ELDOR techniques. Spectra of 
      1-palmitoyl-2-(16-doxyl stearoyl) phosphatidylcholine (16-PC) from PMVs before 
      and after this stimulation at several temperatures are reported. The results 
      demonstrate a coexistence of liquid-ordered (L(o)) and liquid-disordered (L(d)) 
      components. We find that upon cross-linking, the membrane environment is 
      remodeled to become more disordered, as shown by a moderate increase in the 
      population of the L(d) component. This change in the relative amount of the L(o) 
      versus L(d) components upon cross-linking is consistent with a model wherein the 
      IgE receptors, which when clustered by antigen to cause cell stimulation, lead to 
      more disordered lipids, and their dynamic and structural properties are slightly 
      altered. This study demonstrates that 2D-ELDOR, analyzed by the full Sc- method, 
      is a powerful approach for capturing the molecular dynamics in biological 
      membranes. This is a particular case showing how 2D-ELDOR can be applied to study 
      physical processes in complex systems that yield subtle changes.
FAU - Chiang, Yun-Wei
AU  - Chiang YW
AD  - Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, 
      New York 14853-1301, United States.
FAU - Costa-Filho, Antonio J
AU  - Costa-Filho AJ
FAU - Baird, Barbara
AU  - Baird B
FAU - Freed, Jack H
AU  - Freed JH
LA  - eng
GR  - R01 EB003150-25/EB/NIBIB NIH HHS/United States
GR  - R01 EB003150/EB/NIBIB NIH HHS/United States
GR  - P41 RR016292-09/RR/NCRR NIH HHS/United States
GR  - R01 EB003150-29/EB/NIBIB NIH HHS/United States
GR  - R01 AI018306-28/AI/NIAID NIH HHS/United States
GR  - P41 RR016292-10/RR/NCRR NIH HHS/United States
GR  - R01 EB003150-26/EB/NIBIB NIH HHS/United States
GR  - P41 GM103521/GM/NIGMS NIH HHS/United States
GR  - R01 AI018306-29/AI/NIAID NIH HHS/United States
GR  - P41 RR016292/RR/NCRR NIH HHS/United States
GR  - 2R01EB003-150/EB/NIBIB NIH HHS/United States
GR  - AI018306/AI/NIAID NIH HHS/United States
GR  - R01 EB003150-30/EB/NIBIB NIH HHS/United States
GR  - R01 AI018306/AI/NIAID NIH HHS/United States
GR  - P41 RR016292-11/RR/NCRR NIH HHS/United States
GR  - P41RR016292/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20110816
PL  - United States
TA  - J Phys Chem B
JT  - The journal of physical chemistry. B
JID - 101157530
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Receptors, IgE)
SB  - IM
MH  - Animals
MH  - Cell Line, Tumor
MH  - Cell Membrane/*chemistry
MH  - Cross-Linking Reagents/chemistry
MH  - Electron Spin Resonance Spectroscopy/methods
MH  - Rats
MH  - Receptors, IgE/*chemistry
PMC - PMC3165081
MID - NIHMS314225
EDAT- 2011/07/26 06:00
MHDA- 2012/01/18 06:00
PMCR- 2012/09/08
CRDT- 2011/07/26 06:00
PHST- 2011/07/26 06:00 [entrez]
PHST- 2011/07/26 06:00 [pubmed]
PHST- 2012/01/18 06:00 [medline]
PHST- 2012/09/08 00:00 [pmc-release]
AID - 10.1021/jp2016243 [doi]
PST - ppublish
SO  - J Phys Chem B. 2011 Sep 8;115(35):10462-9. doi: 10.1021/jp2016243. Epub 2011 Aug 
      16.