PMID- 10792502
OWN - NLM
STAT- MEDLINE
DCOM- 20000531
LR  - 20190513
IS  - 0019-2805 (Print)
IS  - 1365-2567 (Electronic)
IS  - 0019-2805 (Linking)
VI  - 99
IP  - 4
DP  - 2000 Apr
TI  - Antibody cross-linking of human CD9 and the high-affinity immunoglobulin E 
      receptor stimulates secretion from transfected rat basophilic leukaemia cells.
PG  - 546-52
AB  - Previous studies have shown that antibody cross-linking of the tetraspanin 
      protein CD9 stimulates the degranulation of platelets and eosinophils, although 
      the mechanism of activation is unclear. In this work we transfected human CD9 
      into the rat basophilic leukaemia (RBL-2H3) cell line and studied the stimulation 
      of secretion from these cells in response to a panel of anti-CD9 antibodies. 
      Intact immunoglobulin G1 (IgG1) antibodies activated transfected cells whereas 
      F(ab')2 fragments of antibody and an intact IgG2a did not. Stimulation of 
      secretion was inhibited by co-incubation with monomer murine immunoglobulin E 
      (IgE) but not with an IgG1 isotype control, indicating that the response involves 
      the endogenous high-affinity IgE receptor (FcepsilonRI). The anti-CD9 antibody 
      activation curve was biphasic, and supraoptimal antibody concentrations 
      stimulated little or no degranulation, indicating that multivalent binding of 
      human CD9 molecules is necessary for the formation of an active complex with rat 
      FcepsilonRI. Immunoprecipitation of FcepsilonRI under mild detergent conditions 
      co-precipitated CD9, suggesting the presence of pre-existing complexes of CD9 and 
      FcepsilonRI that could be activated by antibody cross-linking. These data are 
      further evidence that tetraspanins are involved in FcepsilonRI signalling and may 
      reflect the participation of tetraspanins in the formation of complexes with 
      other membrane proteins that use components of Fc receptors for signal 
      transduction.
FAU - Higginbottom, A
AU  - Higginbottom A
AD  - Department of Molecular Biology and Biotechnology, University of Sheffield, 
      Sheffield, UK.
FAU - Wilkinson, I
AU  - Wilkinson I
FAU - McCullough, B
AU  - McCullough B
FAU - Lanza, F
AU  - Lanza F
FAU - Azorsa, D O
AU  - Azorsa DO
FAU - Partridge, L J
AU  - Partridge LJ
FAU - Monk, P N
AU  - Monk PN
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Immunology
JT  - Immunology
JID - 0374672
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD)
RN  - 0 (CD9 protein, human)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, IgE)
RN  - 0 (Tetraspanin 29)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, CD/genetics/*immunology
MH  - Cell Line
MH  - Humans
MH  - Immunoglobulin G/*immunology
MH  - Leukemia, Basophilic, Acute/*immunology
MH  - Lymphocyte Activation/*immunology
MH  - Lymphocytes/immunology
MH  - *Membrane Glycoproteins
MH  - Rats
MH  - Receptors, IgE/*immunology
MH  - Tetraspanin 29
MH  - Transfection
PMC - PMC2327194
EDAT- 2000/05/03 09:00
MHDA- 2000/06/03 09:00
PMCR- 2001/04/01
CRDT- 2000/05/03 09:00
PHST- 2000/05/03 09:00 [pubmed]
PHST- 2000/06/03 09:00 [medline]
PHST- 2000/05/03 09:00 [entrez]
PHST- 2001/04/01 00:00 [pmc-release]
AID - imm992 [pii]
AID - 10.1046/j.1365-2567.2000.00992.x [doi]
PST - ppublish
SO  - Immunology. 2000 Apr;99(4):546-52. doi: 10.1046/j.1365-2567.2000.00992.x.