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Untitled - D Ank Unlimited

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Fcγ R 269 feline immunity<br />

Fc R<br />

The three principal R types of FcRγ include Fcγ RI, Fcγ<br />

RII, and Fcγ RIII that differ in their ITAMs/ITIMs content,<br />

which determines their role in effector cell activation and<br />

in their IgG affinity. Fcγ R I (CD64), the high affinity IgG<br />

receptor, is expressed exclusively on activated granulocytes<br />

and is upregulated by inflammatory cytokines. Fcγ<br />

R I is comprised of an α chain that binds IgG and and<br />

FcRγ homodimer that contains ITAMs. Fcγ R I unites with<br />

the C terminal region of a single H chain comprising the<br />

Fc region of an IgG molecule. It has the greatest affinity<br />

for IgG1 or IgG3 antibodies. Thus, these IgG, subtypes<br />

are excellent opsonins. Fcγ R I interacts with IgG, leading<br />

to inflammatory cytokine secretion and macrophage<br />

and monocyte induced target cell lysis through an ADCC<br />

mechanism. It also results in the generation of superoxide<br />

by neutrophils. Fcγ RII (CD32) has broader expression but<br />

lower affinity for noncomplexed IgG molecules than does<br />

Fcγ RI. Fcγ RII reacts only with aggregated IgG that is<br />

bound to a multivalent antigen. It is comprised of a single<br />

transmembrane chain. Phagocytes, as well as megakaryocytes<br />

and platelets, express Fcγ RIIA, which contains<br />

ITAM. IgG union with Fcγ RIIA leads to a respiratory burst<br />

in neutrophils and causes platelets to secrete inflammatory<br />

molecules. Fcγ RIIB contains ITIM rather than an ITAM<br />

sequence. It is expressed by lymphoid and myeloid cells.<br />

It is believed that this receptor in B cells may signal the<br />

cell to decrease antibody synthesis when a critical level of<br />

antibody has become bound to surface Fcγ R IIB molecules.<br />

Macrophages, monocytes, neutrophils, megakaryocytes<br />

and platelets express Fcγ RIIC receptors, which possess<br />

an ITAM and show only low binding affinity for IgG. The<br />

Fcγ RIII receptor (CD16) manifests low IgG affinity. The<br />

Fcγ RIIIA isoform is comprised of an IgG binding α chain<br />

and an ITAM-containing FcRγ chain dimer. Phagocytes<br />

and NK cells are the principal sites of Fcγ RIIIA expression.<br />

This isoform may be found also on B cells, mast cells,<br />

Langerhans’ cells, and γδ T cells. The only FcR found on<br />

NK cells is Fcγ RIIIA, which has a classic FcR transmembrane<br />

region that facilitates NK cell induced ADCC and<br />

degranulation of mast cells. Neutrophils alone express<br />

the Fcγ RIIIB isoform, which is comprised of a single-<br />

chain protein without transmembrane chains or ITAMs.<br />

Phosphatidyl inositol residues fix Fcγ RIIIB in the membrane.<br />

Neutrophils employ Fcγ R III receptors to convey a<br />

requirement for vigorous phagocytosis.<br />

Fc RI<br />

Represents a high affinity receptor found on mononuclear<br />

phagocytes. In humans it binds IgG1 and IgG3.<br />

Fc RII<br />

A membrane protein designated as CD32 that serves as<br />

a receptor for the Fc regions of immunoglobulin G (IgG)<br />

molecules.<br />

Fc RIII<br />

Fcγ RII and Fcγ RIII represent low affinity IgG receptors.<br />

In humans, neutrophils, monocytes, eosinophils, platelets,<br />

and B lymphocytes express Fcγ RII on their membranes.<br />

Neutrophils, natural killer cells, eosinophils, macrophages,<br />

and selected T lymphocytes express Fcγ RIII on their<br />

membranes and bind IgGl and IgG3. Paroxysmal nocturnal<br />

hemoglobulinuria patients have deficient Fcγ RIII on their<br />

neutrophil membranes.<br />

FcRn (neonatal)<br />

Fc receptors expressed by neonatal intestinal cells that<br />

bind IgG in breast milk. They facilitate its passage into the<br />

neonatal intestinal lumen and also aid IgG transport in the<br />

adult intestine and placenta. Also called Brambell receptor.<br />

FDCs<br />

Refer to follicular dendritic cells.<br />

Fd fragment<br />

The heavy chain portion of a Fab fragment produced by<br />

papain digestion of an immunoglobulin G (IgG) molecule.<br />

It is on the N terminal side of the papain digestion site.<br />

Fd piece<br />

Refer to Fd fragment.<br />

Fd′ fragment<br />

The heavy chain portion of an Fab′ fragment produced by<br />

reduction of the F(ab′) 2 fragment that results from pepsin<br />

digestion of IgG. It is comprised of V H1, C H1, and the heavy<br />

chain hinge region. Fd contains 235 amino acid residues.<br />

Fd′ piece<br />

Refer to Fd′ fragment.<br />

FDNB (1-fluoro-2-4-dinitrobenzene)<br />

Refer to dinitrofluorobenzene (DNFB).<br />

Feline immunity.<br />

feline immunity<br />

Although peripheral lymphoid tissues and thymus glands of<br />

cats are comparable to those of other mammals, they possess<br />

a population of pulmonary intravascular macrophages that<br />

may cause the animals to manifest increased susceptibility<br />

to septic shock mediated by macrophage-derived tumor<br />

necrosis factor. Forty to 45% of feline peripheral blood<br />

lymphocytes are B cells, and 32 to 41% are T cells; 20% of<br />

feline peripheral blood cells are null cells considered to be<br />

natural killer (NK) cells. Both T helper and T suppressor<br />

activities have been described. Feline interleukin-1 (IL1)<br />

and IL2 as well as IL6 have been identified, although the<br />

physical and chemical properties of the latter are different<br />

from those of the human and mouse interleukins.<br />

Interferons α, β, and γ have been characterized and resemble<br />

those of other species. Although all immunoglobulin<br />

isotypes of other species are recognized in cats, neither IgE<br />

nor IgD has been formally identified. Cats also have secretory<br />

IgA with a J-chain that resembles equivalent molecules<br />

of other species. Although cats do not respond to tuberculin,<br />

they develop good delayed hypersensitivity responses<br />

(viral antigens) in the skin to dinitrochlorobenzene and<br />

F

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