# STRUCTURE AND FUNCTION OF THE LYMPHOCYTE FCE RECEPTOR

> **NIH NIH R01** · VIRGINIA COMMONWEALTH UNIVERSITY · 1991 · $210,810

## Abstract

The murine lymphocyte receptor for IgE, with regard to both
structure and function is the focus of this application.  Intact
FceR levels increase during B cell activation in the presence of
interleukin 4 (IL-4) suggesting a role for the FceR in B cell
activation.  Anti-FceR both in the soluble and sepharose bound
form will be tested for the capacity to either directly activate B
lymphocytes or to influence B cell activation by anti-
Immunoqlobulin.  Parameters to be measured include calcium
influx, cell size changes, phosphatidyl inositol levels and Ig
production.  The FceR spontaneously releases lower molecular
fragments via proteolysis at the cell surface and preliminary
evidence suggests that these fragments enhance the level of IgE
synthesis in the presence of IL-4.  This phenomena will be further
studied with regard to isotype specificity, role of FceR
carbohydrate in the biologic activity and molecular size of the
FceR fragment involved.  In addition, it will be determined if the
fragment interacts with a specific component on the B cell
membrane.  The site of interaction of IgE with the FceR is
important with regard to receptor degradation and the location of
this site will be explored in detail, both by using anti-peptide
antibodies, mimicking specific areas of the FceR and by using
crosslinking reagents that will label the site(s) of close proximity
with IgE.  Antibodies against the site of the FceR that interacts
with IgE will also be tested for their capacity to induce FceR
upregulation, analogous to IgE and their effect on IgE synthesis
will be determined.  The low affinity FceR on macrophages and T
cells will be further investigated with regard to physiochemical
relationship to the B cell FceR, association with other membrane
components and regulation at the cell surface.  The overall aim is
to gain further insight into the structure and regulation of the low
affinity FceR and to determine if FceR/anti-FceR related
components are useful in the regulation of IgE synthesis.

## Key facts

- **NIH application ID:** 3128118
- **Project number:** 5R01AI018697-11
- **Recipient organization:** VIRGINIA COMMONWEALTH UNIVERSITY
- **SAM.gov UEI:** MLQFL4JSSAA9
- **Principal Investigator:** DANIEL H CONRAD
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1991
- **Award amount:** $210,810
- **Award type:** 5
- **Project period:** 1989-05-01 → 1992-11-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3128118

## Citation

> US National Institutes of Health, RePORTER application 3128118, STRUCTURE AND FUNCTION OF THE LYMPHOCYTE FCE RECEPTOR (5R01AI018697-11). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3128118. Licensed CC0.

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