PMID- 1310043
OWN - NLM
STAT- MEDLINE
DCOM- 19920226
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 31
IP  - 2
DP  - 1992 Jan 21
TI  - Rotational motion of monomeric and dimeric immunoglobulin E-receptor complexes.
PG  - 567-75
AB  - Erythrosin 5'-thiosemicarbazide labeled immunoglobulin E (IgE) was used to 
      monitor the rotational dynamics of monomeric and dimeric Fc epsilon RI receptors 
      for IgE on rat basophilic leukemia (RBL) basophilic leukemia (RBL) cells using 
      time-resolved phosphorescence anisotropy. Receptors were studied both on living 
      RBL cells and on membrane vesicles derived from RBL cell plasma membrane. The 
      un-cross-linked IgE-receptor complexes on cells and vesicles exhibit rotational 
      correlation times that are consistent with those expected for freely rotating 
      monomers, but a small fraction of these complexes on cells may be rotationally 
      immobile. A comparison of the initial phosphorescence anisotropy values for 
      erythrosin-labeled IgE-receptor complexes on cells and vesicles reveals a fast 
      component of rotational motion that is greater on the vesicles and may be due to 
      a site of segmental flexibility in the receptor itself. Dimers of IgE-receptor 
      complexes formed with anti-IgE monoclonal antibodies appear to be largely 
      immobile on cells, but they are mobile on vesicles with a 2-fold larger 
      rotational correlation time than the monomeric complexes. The results suggest 
      that dimeric IgE-receptor complexes undergo interactions with other membrane 
      components on intact cells that do not occur on the membrane vesicles. The 
      possible significance of these interactions to receptor function is discussed.
FAU - Myers, J N
AU  - Myers JN
AD  - Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, New York 
      14853-1301.
FAU - Holowka, D
AU  - Holowka D
FAU - Baird, B
AU  - Baird B
LA  - eng
GR  - AI18306/AI/NIAID NIH HHS/United States
GR  - AI22449/AI/NIAID NIH HHS/United States
GR  - GM07273/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - PN2ZH5LOQY (Erythrosine)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/chemistry
MH  - Antigens, Differentiation, B-Lymphocyte/*chemistry/immunology
MH  - Cell Membrane/chemistry
MH  - Erythrosine/analogs & derivatives
MH  - Fluorescence Polarization
MH  - Leukemia, Basophilic, Acute
MH  - Macromolecular Substances
MH  - Protein Conformation
MH  - Rats
MH  - Receptors, Fc/*chemistry/immunology
MH  - Receptors, IgE
MH  - Tumor Cells, Cultured
EDAT- 1992/01/21 00:00
MHDA- 1992/01/21 00:01
CRDT- 1992/01/21 00:00
PHST- 1992/01/21 00:00 [pubmed]
PHST- 1992/01/21 00:01 [medline]
PHST- 1992/01/21 00:00 [entrez]
AID - 10.1021/bi00117a038 [doi]
PST - ppublish
SO  - Biochemistry. 1992 Jan 21;31(2):567-75. doi: 10.1021/bi00117a038.