PMID- 2946319
OWN - NLM
STAT- MEDLINE
DCOM- 19870109
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 25
IP  - 19
DP  - 1986 Sep 23
TI  - Phospholipid distribution in the microenvironment of the immunoglobulin 
      E-receptor from rat basophilic leukemia cell membrane.
PG  - 5686-93
AB  - It has been previously found that lipids were required to maintain intact the 
      tetrameric structure of the receptor for immunoglobulin E (IgE) (Fc epsilon R) in 
      detergent solutions [Rivnay, B., Rossi, G., Henkart, M., & Metzger, H. (1984) J. 
      Biol. Chem. 259, 1212-1217, and references cited therein]. Failure of 
      commercially obtained lipids to provide sufficient protection, however, 
      underscored the necessity for development of additional analytical approaches. In 
      order to identify the phospholipid distribution in the intimate natural 
      environment of this receptor, both the plasma membrane vesicles and the 
      ligand-receptor complex (IgE-Fc epsilon R) have been isolated by affinity 
      chromatography. The phospholipids of both preparations were compared. After 
      extensive washing with detergent lipid micelles, IgE-Fc epsilon R retained 0.1-1% 
      of the total phospholipids in the purified plasma membrane. The receptor-bound 
      lipids were shown to contain phosphatidylcholine and sphingomyelin; the content 
      of the latter lipid was enriched 2-5-fold compared with that in the plasma 
      membranes. This pattern was observed with several detergents employed for 
      purification and under a variety of experimental conditions. In light of the 
      general distribution of choline phospholipids in the outer leaflet of plasma 
      membranes, this enrichment may not be a characteristic of this particular 
      receptor exclusively. These observations should be particularly helpful in 
      studies on aggregation-induced functions of the isolated Fc epsilon receptor. In 
      general, the methods employed enable isolation of purified and lipid-protected 
      integral proteins and also provide an appropriate reference source of intact 
      membrane vesicles. These qualities render this approach useful in similar studies 
      of other membrane proteins.
FAU - Rivnay, B
AU  - Rivnay B
FAU - Fischer, G
AU  - Fischer G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Membrane Lipids)
RN  - 0 (Micelles)
RN  - 0 (Phospholipids)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - 0 (Receptors, Immunologic)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Animals
MH  - Basophils/immunology
MH  - Cell Membrane/immunology
MH  - Immunoglobulin E/*metabolism
MH  - Leukemia, Experimental/*immunology
MH  - Membrane Lipids/*analysis
MH  - Mice
MH  - Micelles
MH  - Microsomes/immunology
MH  - Phospholipids/*analysis
MH  - Rats
MH  - Receptors, Fc/*metabolism
MH  - Receptors, IgE
MH  - Receptors, Immunologic/*metabolism
EDAT- 1986/09/23 00:00
MHDA- 1986/09/23 00:01
CRDT- 1986/09/23 00:00
PHST- 1986/09/23 00:00 [pubmed]
PHST- 1986/09/23 00:01 [medline]
PHST- 1986/09/23 00:00 [entrez]
AID - 10.1021/bi00367a051 [doi]
PST - ppublish
SO  - Biochemistry. 1986 Sep 23;25(19):5686-93. doi: 10.1021/bi00367a051.