# RECEPTORS FOR IMMUNOGLOBULIN G ON LEUKOCYTES

> **NIH NIH R01** · THOMAS JEFFERSON UNIVERSITY · 1993 · $251,702

## Abstract

Receptors for the Fc portion of IgG (FcgammaR) are expressed on most
hematopoietic cell types.  By binding antigen specific immunoglobulins,
they provide an important link between the intra and extracellular
compartments and are essential for the interactions between cells of the
non adaptive (innate) and the adaptive systems of defense.  They belong
to an heterogeneous family of membrane receptors and mediate a wide array
of cellular responses to antibody antigen complexes.  The diversity of
these responses is the result of the structural heterogeneity of the
FcgammaR, related to differences in their intracytoplasmic domains, and
to the presence, within the receptor complex, or receptor associated
molecules that are important both for receptor expression and signal
transduction.  We have demonstrated that the low affinity receptor for
IgG expressed on Natural Killer (NK) cells and macrophages (FcgammaRIIIA)
transmembrane glycoprotein that, upon ligand binding, regulates functions
of these cells by transducing signals that result in cell activation.
Its counterpart on polymorphonuclear neutrophils (FcgammaRIIIB), a
glycosilphosphatidylinositol linked molecule, is devoid of such
functions.  NK cell activation induced via FcgammaRIII primarily depends
on induced activation of kinases.  The working hypothesis of this
proposal is that distinct specialized effector functions are mediated by
different FcgammaR types, that depend on induction of distinct
biochemical events in the same or different cell types, and that
interactions of FcgammaR with other proteins cooperate in this function.
In order to elucidate the role of the different types of FcgammaR on NK
cells, myelomonocytic cells, and lymphocytes, we propose:  1) to identify
those molecules that, activated upon interaction of FcgammaRIII on NK
cells with its ligands, regulate signal transduction, and 2) to analyze
functional role, an the mechanisms regulating them, of distinct FcgammaR
types on B lymphocytes and myelomonocytic cells.  Specifically, we
propose to identify the kinases activated upon FcgammaRIII-ligand
binding.  The role of the substrates for these kinases, and of
phosphatases, in controlling FcGgammaRIII-mediated signal transduction
will also be analyzed.  The molecular events occurring in
myeloid/monocytic cells and B lymphocytes upon immune complexes binding
will be studied and the interactions between different FcgammaR expressed
on the same cell types will be dissected, to determine the relative role
played by FcgammaRII on these cells.  These studies are expected to
result in the identification of common or distinctive features of
behavior of FcgammaR, to provide information on FcgammaR-dependent
functions on hematopoietic cells, and to pose the basis for understanding
the mechanisms by which functions of cells of the innate system of
defense are regulated.

## Key facts

- **NIH application ID:** 3174892
- **Project number:** 2R01CA037155-09
- **Recipient organization:** THOMAS JEFFERSON UNIVERSITY
- **SAM.gov UEI:** R8JEVL4ULGB7
- **Principal Investigator:** BICE PERUSSIA
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $251,702
- **Award type:** 2
- **Project period:** 1984-04-01 → 1998-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3174892

## Citation

> US National Institutes of Health, RePORTER application 3174892, RECEPTORS FOR IMMUNOGLOBULIN G ON LEUKOCYTES (2R01CA037155-09). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3174892. Licensed CC0.

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