By ResearchSEA
Wednesday, October 28, 2009
Press Release - Researchers at the University of Alabama
at Birmingham and RIKEN has identified the gene encoding the
receptor for immunoglobulin M (IgM), a class of antibody that
appears first in immune response. The landmark finding promises
advances in our understanding of early immune response and in the
treatment of immunological diseases.
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| Figure 1: Internalization of IgM antibodies by Hela cells
ectopically expressing the IgM receptor (FcμR). (A)
Internalization of antibodies (red) that recognize the FcμR. (B)
Internalization of IgM antibodies (green). (C) IgG antibodies
(green) do not bind to FcμR and are not internalized |
| Copyright : RIKEN |
A team made up of researchers at the University of Alabama at
Birmingham and RIKEN has identified the gene encoding the receptor
for immunoglobulin M (IgM), a class of antibody that appears first
in immune response. The landmark finding, to appear in the November
23rd issue of the Journal of Experimental Medicine (available
online October 26th), promises advances in our understanding of
early immune response and in the treatment of immunological
diseases.
In immune systems, the function of antibodies is to bind to
pathogens such as viruses and bacteria and tag them for removal.
Once tagged, white blood cells such as macrophages capture and
eliminate the invading pathogen using receptors on the cell surface
that recognize the attached antibody.
Whereas receptors for other classes of antibodies have been studied
extensively, the genetic identity of receptors for IgM (FcμR)
has remained a mystery for more than 30 years despite its key
contribution to early immune response and natural immunity.
To identify the FcμR gene, researchers constructed cDNA
libraries from chronic lymphocytic leukemia cells, known to express
high levels of IgM receptors, and introduced them into a mouse
T-cell line that does not naturally bind to IgM antibodies. By
analyzing the IgM-binding ability of the library-introduced
T-cells, researchers were able to isolate and identify the FcμR
gene.
In clarifying the molecular nature of a receptor known to
profoundly influence immune response, identification of the FcμR
gene fills a crucial gap in our understanding of immune systems,
opening the door to new possibilities in the treatment of immune
deficiencies and allergy diseases.
For more information, please contact:
Dr. Hiromi Kubagawa
University of Alabama at Birmingham,
Tel: +1-205-975-7201
Dr. Hiroshi Ohno
Laboratory for Epithelial Immunobiology
RIKEN Research Center for Allergy and Immunology
Tel: 045-503-7031
Dr. Ji-Yang Wang
Laboratory for Immune Diversity
RIKEN Research Center for Allergy and Immunology
Tel: 045-503-7042
Ms. Saeko Okada (PI officer)
Global Relations Office
RIKEN
Tel: +81-(0)48-462-1225 / Fax: +81-(0)48-467-9443
Email: koho@riken.jp
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| Figure 2: Schematic structure of FcμR and the proposed role
of the cytoplasmic region in signal transduction. (A) Schematic
structure. (B) Upon crosslinking of the FcμR, the serine (S) and
tyrosion (Y) residues are phosphorylated, suggesting that these
residues play a role in signal transduction. |
| Copyright : RIKEN |
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Journal information
Journal of Experimental Medicine
SOURCE
