PMID- 6224847
OWN - NLM
STAT- MEDLINE
DCOM- 19831008
LR  - 20071114
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 131
IP  - 3
DP  - 1983 Sep
TI  - Modulation of the biologic activities of IgE-binding factors. III. Switching of a 
      T cell hybrid clone from the formation of IgE-suppressive factor to the formation 
      of IgE-potentiating factor.
PG  - 1090-5
AB  - Incubation of rat-mouse T cell hybridoma cells, 23B6, with rat immunoglobulin E 
      (IgE) results in the formation of the 15,000-dalton IgE-suppressive factor and 
      the 30,000-dalton IgE-binding factor, which has neither potentiating activity nor 
      suppressive activity on the IgE response. Another T cell hybridoma, 23A4 cells, 
      produces the 30,000-dalton "inactive" IgE-binding factor upon incubation with 
      IgE. Both the 15,000-dalton IgE-suppressive factor and the 30,000-dalton 
      IgE-binding factor lacked affinity for lentil lectin but bound to peanut 
      agglutinin. When the 23B6 cells were incubated with IgE in the presence of 
      lysolecithin, the majority of the 15,000-dalton IgE-binding factor formed by the 
      cells gained affinity for lentil lectin, and this factor selectively potentiated 
      the IgE response. The glycosylation-enhancing factor, which was formed by 
      stimulation of normal spleen cells with lymphocytosis-promoting factor (LPF or 
      pertussigen), also switched 23B6 cells from the formation of IgE-suppressive 
      factor to the formation of IgE-potentiating factor. It was also found that the 
      30,000-dalton "inactive" IgE-binding factor, formed by both 23B6 and 23A4 cells, 
      gained the ability to potentiate the IgE response, when the cells were cultured 
      with IgE in the presence of glycosylation-enhancing factor. The results indicate 
      that IgE-potentiating factor and IgE-suppressive factor share common precursors, 
      and that biologic activities of IgE-binding factors are decided by their 
      carbohydrate moieties. Incubation of the two hybridoma cells with lysolecithin or 
      glycosylation-enhancing factor results in an increase in the proportion of FC 
      epsilon R+ cells, suggesting that the assembly of N-linked oligosaccharide to 
      precursor molecules is intrinsic for the expression of FC epsilon R.
FAU - Huff, T F
AU  - Huff TF
FAU - Uede, T
AU  - Uede T
FAU - Iwata, M
AU  - Iwata M
FAU - Ishizaka, K
AU  - Ishizaka K
LA  - eng
GR  - AI-07056/AI/NIAID NIH HHS/United States
GR  - AI-11202/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Annexins)
RN  - 0 (Blood Proteins)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Lymphokines)
RN  - 0 (Lysophosphatidylcholines)
RN  - 0 (Prostatic Secretory Proteins)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - 0 (Receptors, IgG)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (beta-microseminoprotein)
RN  - 0 (immunoenhancing factor)
RN  - 0 (immunoglobulin-binding factors)
RN  - 0 (lipomodulin)
SB  - IM
MH  - Animals
MH  - Annexins
MH  - Blood Proteins/*biosynthesis/physiology
MH  - *Calcium-Binding Proteins
MH  - Clone Cells/immunology
MH  - *Glycoproteins
MH  - Lymphokines/*biosynthesis/physiology
MH  - Lysophosphatidylcholines/pharmacology
MH  - Mice
MH  - Molecular Weight
MH  - *Prostatic Secretory Proteins
MH  - Proteins/immunology
MH  - Rats
MH  - Rats, Inbred Lew
MH  - Receptors, Fc/metabolism
MH  - Receptors, IgE
MH  - Receptors, IgG
MH  - Receptors, Immunologic/*metabolism
MH  - Rosette Formation
MH  - T-Lymphocytes/*immunology
EDAT- 1983/09/01 00:00
MHDA- 1983/09/01 00:01
CRDT- 1983/09/01 00:00
PHST- 1983/09/01 00:00 [pubmed]
PHST- 1983/09/01 00:01 [medline]
PHST- 1983/09/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1983 Sep;131(3):1090-5.