PMID- 23777450
OWN - NLM
STAT- MEDLINE
DCOM- 20140217
LR  - 20130802
IS  - 1535-3907 (Electronic)
IS  - 1535-3893 (Linking)
VI  - 12
IP  - 8
DP  - 2013 Aug 2
TI  - N-linked glycan structures of the human Fcgamma receptors produced in NS0 cells.
PG  - 3721-37
LID - 10.1021/pr400344h [doi]
AB  - Immune recognition of nonself is coordinated through complex mechanisms involving 
      both innate and adaptive responses. Circulating antibodies communicate with 
      effector cells of the innate immune system through surface receptors known as Fcgamma 
      receptors (FcgammaRs). The FcgammaRs are single-pass transmembrane glycoproteins 
      responsible for regulating innate effector responses toward antigenic material. 
      Although immunoglobulin G (IgG) antibodies bind to a range of receptors, 
      including complement receptors and C-type lectins, we have focused on the Fcgamma 
      receptors. A total of five functional FcgammaRs are broadly classified into three 
      families (FcgammaRI, FcgammaRII, and FcgammaRIII) and together aid in controlling both 
      inflammatory and anti-inflammatory responses of the innate immune system. Due to 
      the continued success of monoclonal antibodies in treating cancer and autoimmune 
      disorders, research is typically directed toward improving the interaction of 
      antibodies with the FcgammaRs through manipulation of IgG properties such as N-linked 
      glycosylation. Biochemical studies using recombinant forms of the FcgammaRs are often 
      used to quantitate changes in binding affinity, a key indicator of a likely 
      biological outcome. However, analysis of the FcgammaRs themselves is imperative as 
      recombinant FcgammaRs differ greatly from those observed in humans. In particular, 
      the N-linked glycan composition is significantly important due to its function in 
      the IgG-FcgammaR interaction. Here, we present data for the N-linked glycans present 
      on FcgammaRs produced in NS0 cells, namely, FcgammaRIa, FcgammaRIIa, FcgammaRIIB, FcgammaRIIIa, and 
      FcgammaRIIIb. Importantly, these FcgammaRs demonstrate typical murine glycosylation in 
      the form of alpha-galactose epitopes, N-glycolylneuraminic acid, and other key glycan 
      properties that are generally expressed in murine cell lines and therefore are 
      not typically observed in humans.
FAU - Cosgrave, Eoin F J
AU  - Cosgrave EF
AD  - NIBRT Glycobiology Group, National Institute for Bioprocessing Research and 
      Training, Foster's Avenue, Mount Merrion, Blackrock, County Dublin, Ireland.
FAU - Struwe, Weston B
AU  - Struwe WB
FAU - Hayes, Jerrard M
AU  - Hayes JM
FAU - Harvey, David J
AU  - Harvey DJ
FAU - Wormald, Mark R
AU  - Wormald MR
FAU - Rudd, Pauline M
AU  - Rudd PM
LA  - eng
PT  - Journal Article
DEP - 20130711
PL  - United States
TA  - J Proteome Res
JT  - Journal of proteome research
JID - 101128775
RN  - 0 (FCGR1A protein, human)
RN  - 0 (Fc gamma receptor IIA)
RN  - 0 (Fc gamma receptor IIB)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Neuraminic Acids)
RN  - 0 (Polysaccharides)
RN  - 0 (Protein Isoforms)
RN  - 0 (Receptors, IgG)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Cell Line, Tumor
MH  - Galactose/chemistry/metabolism
MH  - Gene Expression
MH  - Glycosylation
MH  - Humans
MH  - Immunoglobulin G/*chemistry/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neuraminic Acids/chemistry/metabolism
MH  - Polysaccharides/analysis/*chemistry
MH  - Protein Binding
MH  - Protein Isoforms/chemistry/genetics/metabolism
MH  - Receptors, IgG/*chemistry/genetics/metabolism
MH  - Species Specificity
EDAT- 2013/06/20 06:00
MHDA- 2014/02/18 06:00
CRDT- 2013/06/20 06:00
PHST- 2013/06/20 06:00 [entrez]
PHST- 2013/06/20 06:00 [pubmed]
PHST- 2014/02/18 06:00 [medline]
AID - 10.1021/pr400344h [doi]
PST - ppublish
SO  - J Proteome Res. 2013 Aug 2;12(8):3721-37. doi: 10.1021/pr400344h. Epub 2013 Jul 
      11.