PMID- 22288459
OWN - NLM
STAT- MEDLINE
DCOM- 20120628
LR  - 20220309
IS  - 1749-6632 (Electronic)
IS  - 0077-8923 (Linking)
VI  - 1253
DP  - 2012 Apr
TI  - Novel roles for the IgG Fc glycan.
PG  - 170-80
LID - 10.1111/j.1749-6632.2011.06305.x [doi]
AB  - IgG antibodies trigger leukocyte activation and inflammation by forming immune 
      complexes that crosslink activating Fcgamma receptors (FcgammaRs). This is essential to 
      combat infection, but detrimental if antibodies target or cross-react with 
      autoantigens. The high specificity and long serum half-life of IgG antibodies 
      confers tremendous therapeutic potential. Indeed, antibodies have been 
      successfully employed to target cancers, autoreactive B cells, and 
      pro-inflammatory cytokines. Conversely, IgG antibodies can also initiate 
      anti-inflammatory responses. In the form of intravenous immunoglobulin (IVIG), 
      IgGs are routinely administered to treat inflammatory autoimmune diseases. 
      Importantly, the N-linked glycans on the IgG Fc are absolutely required for 
      initiating these IgG effector functions. In fact, the Fc glycan composition 
      dictates IgG affinity to individual FcgammaRs, and in a broader sense, binding to 
      different FcgammaRs classes: activating, inhibitory, and anti-inflammatory (dendritic 
      cell-specific ICAM-3 grabbing nonintegrin, DC-SIGN). The Fc glycan requirements 
      to initiate and suppress inflammation will be discussed herein.
CI  - (c) 2012 New York Academy of Sciences.
FAU - Anthony, Robert M
AU  - Anthony RM
AD  - Leonard Wagner Laboratory of Molecular Genetics and Immunology, The Rockefeller 
      University, New York, New York 10065, USA. ranthony01@rockefeller.edu
FAU - Wermeling, Fredrik
AU  - Wermeling F
FAU - Ravetch, Jeffrey V
AU  - Ravetch JV
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20120130
PL  - United States
TA  - Ann N Y Acad Sci
JT  - Annals of the New York Academy of Sciences
JID - 7506858
RN  - 0 (Immunoglobulin Fc Fragments)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulins, Intravenous)
RN  - 0 (Polysaccharides)
SB  - IM
MH  - Animals
MH  - Antibody Affinity
MH  - Humans
MH  - Immunoglobulin Fc Fragments/*chemistry/*immunology
MH  - Immunoglobulin G/*chemistry/*immunology
MH  - Immunoglobulins, Intravenous/chemistry/therapeutic use
MH  - Inflammation/immunology/therapy
MH  - Mice
MH  - Models, Immunological
MH  - Models, Molecular
MH  - Molecular Structure
MH  - Polysaccharides/*chemistry/*immunology
EDAT- 2012/02/01 06:00
MHDA- 2012/06/29 06:00
CRDT- 2012/02/01 06:00
PHST- 2012/02/01 06:00 [entrez]
PHST- 2012/02/01 06:00 [pubmed]
PHST- 2012/06/29 06:00 [medline]
AID - 10.1111/j.1749-6632.2011.06305.x [doi]
PST - ppublish
SO  - Ann N Y Acad Sci. 2012 Apr;1253:170-80. doi: 10.1111/j.1749-6632.2011.06305.x. 
      Epub 2012 Jan 30.