The Ohio State University460 West 12th Avenue,
392, Biomedical Research Tower,
Columbus, OH 43210
614-247-7650
Fax: 614-247-7669
Clark.Anderson@osumc.edu
Research Interests
IgG Fc receptors researchDr. Anderson is interested in how two families of IgG Fc receptors work, specifically, how one family mediates inflammatory and protective effects of IgG antibodies and how another binds both IgG and albumin, extending the half-lives of these two molecules by protecting them from degradation, transporting (at least IgG) across the placenta from maternal to fetal circulation.
IgG antibodies bind antigens to form immune complexes that interact with the plasma membranes of several types of cells to trigger a number of inflammatory and protective biologic processes. These processes include the endocytosis of antibody-coated particles such as bacteria or viruses by cells, the stimulation of secretion of inflammatory mediators, the cell-mediated killing of antibody-coated target or tumor cells and the modulation of the immune responses by lymphocytes and other cells of the immune system. Mediating these processes in man are three distinct classes of integral membrane Fc receptors which bind IgG (FcgR) immune complexes. These receptors, encoded by eight genes on chromosome 1, constitute a small subfamily within the immunoglobulin gene superfamily. Upon clustering by immune complexes the receptors trigger intracellular enzymatic cascades by activating non-receptor tyrosine kinases and phosphatases. Dr. Anderson's lab uses the methods of immunology, cell biology, molecular biology and biochemistry to study these processes.
It is apparent that IgG is transported across the placenta from maternal circulation to the fetus, conveying the full complement of mother's protective antibody, by a transporter molecule with high affinity for IgG (FcRn) that is not a member of the family of classical FcgR described above. This molecule, present in the trophoblast of the placenta and in many cells of the body throughout life, is also responsible for protecting IgG from its normal catabolic fate, accounting for the long lifespan of IgG. Dr. Anderson's lab is interested in how this receptor works in health and disease. We have recently found that FcRn binds albumin and rescues it from a degradative fate, extending its half-life to near that of IgG.
Reagents
- Mab 32.2. Monoclonal antibody to extracellular portion of FcãRI first described by Anderson et al, 1986
- Protein available from Medarex, Inc. Cell line available from ATCC catalog #HB-9469
- Mab IV.3. Monoclonal antibody to extracellular portion of FcãRII first described by Looney et al, 1986
- Protein available from Medarex, Inc. Cell line available from ATCC catalog #HB-217
- Mab CT6.1D7. Monoclonal antibody to cytoplasmic tail of FcãRI first described by L. K. Ernst et al, 1998. Cell line available from ATCC catalog #CRL-2438
Education
Immunochemistry Fellowship: National Jewish Center, 1971-1977
Clinical Immunology Fellowship: National Jewish Center and University of Colorado, 1973-1974
Medicine residency: University of Colorado, 1969-1971
Vietnam War doctor draft, 1966-1969
Medicine Internship: University of Colorado, 1965-1966
Biochemistry Graduate Program, University of Chicago, 1965
MD: University of Chicago, 1964
Lecture
Watch lecture, “Dr. Anderson’s Talk About His Career”
Transcript of lecture