PMID- 7613162
OWN - NLM
STAT- MEDLINE
DCOM- 19950824
LR  - 20191210
IS  - 1018-2438 (Print)
IS  - 1018-2438 (Linking)
VI  - 107
IP  - 1-3
DP  - 1995 May-Jun
TI  - Role of glycosylation sites in the IgE Fc molecule.
PG  - 328-9
AB  - The Fc region of immunoglobulin E (IgE) comprising the C epsilon 3 and C epsilon 
      4 domains (residues 329-547) is sufficient for binding to the high-affinity IgE 
      Fc receptor (Fc epsilon RI alpha). Three potential N-linked glycosylation sites 
      are present within the C epsilon 3 domain. To determine the effect of the 
      glycosylation sites on IgE Fc synthesis and on Fc epsilon RI alpha binding, 
      site-directed mutagenesis was performed. Mutant IgE Fc constructs were expressed 
      in COS cells and analyzed for protein synthesis and secretion, and Fc epsilon RI 
      alpha binding activity. We find that only N371 and N394 are glycosylated, and 
      that the residues surrounding the glycosylation site at N394 are required for Fc 
      epsilon RI alpha binding activity.
FAU - Nettleton, M Y
AU  - Nettleton MY
AD  - Department of Inflammation and Autoimmune Diseases, Hoffmann-La Roche, Nutley, NJ 
      07110, USA.
FAU - Kochan, J P
AU  - Kochan JP
LA  - eng
PT  - Journal Article
PL  - Switzerland
TA  - Int Arch Allergy Immunol
JT  - International archives of allergy and immunology
JID - 9211652
RN  - 0 (Immunoglobulin Fc Fragments)
RN  - 0 (Receptors, IgE)
RN  - 0 (Recombinant Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Animals
MH  - Cell Line, Transformed
MH  - Chlorocebus aethiops
MH  - Glycosylation
MH  - Humans
MH  - Immunoglobulin E/*chemistry/genetics/metabolism
MH  - Immunoglobulin Fc Fragments/*chemistry/genetics/metabolism
MH  - Mutagenesis, Site-Directed
MH  - Protein Binding
MH  - Protein Processing, Post-Translational
MH  - Receptors, IgE/metabolism
MH  - Recombinant Proteins/metabolism
EDAT- 1995/05/01 00:00
MHDA- 1995/05/01 00:01
CRDT- 1995/05/01 00:00
PHST- 1995/05/01 00:00 [pubmed]
PHST- 1995/05/01 00:01 [medline]
PHST- 1995/05/01 00:00 [entrez]
AID - 10.1159/000237017 [doi]
PST - ppublish
SO  - Int Arch Allergy Immunol. 1995 May-Jun;107(1-3):328-9. doi: 10.1159/000237017.