26.07.2013 Views

Untitled - D Ank Unlimited

Untitled - D Ank Unlimited

Untitled - D Ank Unlimited

SHOW MORE
SHOW LESS

You also want an ePaper? Increase the reach of your titles

YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.

antiglial fibrillary acidic protein (GFAP) antibody 58 antigranulocyte antibodies<br />

antiglial fibrillary acidic protein (GFAP) antibody<br />

A rabbit polyclonal antibody directed against glial fibrillary<br />

acidic protein present in the cytoplasm of most human<br />

astrocytes and ependymal cells. This reagent may be used<br />

to aid in the identification of cells of glial lineage. The<br />

antibody is intended for qualitative staining in sections of<br />

formalin-fixed, paraffin-embedded tissue. Anti-GFAP antibody<br />

specifically binds to the glial fibrillary acidic protein<br />

located in the cytoplasm of normal and neoplastic glial<br />

cells. Unexpected antigen expression or loss of expression<br />

may occur, especially in neoplasms. Occasionally, stromal<br />

elements surrounding heavily stained tissue and/or cells<br />

will show immunoreactivity. The clinical interpretation of<br />

any staining or its absence must be complemented by morphological<br />

studies and evaluation of proper controls.<br />

antiglobulin<br />

An antibody raised by immunization of one species, such as a<br />

rabbit, with immunoglobulin from another species, such as a<br />

human. Rabbit anti-human globulin has been used for many<br />

years in an antiglobulin test to detect incomplete antibodies<br />

coating red blood cells, as in erythroblastosis fetalis or autoimmune<br />

hemolytic anemia. Antiglobulin antibodies are specific<br />

for epitopes in the Fc regions of immunoglobulin molecules<br />

used as immunogens, rendering them capable of agglutinating<br />

cells whose surface antigens are combined with the Fab regions<br />

of IgG molecules whose Fc regions are exposed.<br />

antiglobulin consumption test<br />

An assay to test for the presence of an antibody in serum<br />

which is incubated with antigen-containing cells or antigencontaining<br />

particles. After washing, the cells or particles<br />

are treated with antiglobulin reagents and incubated further.<br />

If any antibody has complexed with the cells or particles,<br />

antiglobulin will be taken up. Antiglobulin depletion from<br />

the mixture is evaluated by assaying the free antiglobulin<br />

in the supernatant through combination with incomplete<br />

antibody-coated erythrocytes. No hemagglutination reveals<br />

that the antiglobulin reagent was consumed in the first step<br />

of the reaction and shows that the patient’s original serum<br />

contained the antibody in question.<br />

antiglobulin inhibition test<br />

An assay based upon interference with the antiglobulin test<br />

through reaction of the antiglobulin reagent with antibody<br />

against it prior to combination with incomplete antibodycoated<br />

erythrocytes. This is the basis for the so-called<br />

antiglobulin consumption test.<br />

antiglobulin test<br />

When red blood cells are coated with antibodies that are<br />

not agglutinable in saline, such as those from an infant with<br />

erythroblastosis fetalis, a special anti-human immunoglobulin<br />

(Ig) prepared by immunizing rabbits with human IgG<br />

may be employed to crosslink the antibody-coated red cells<br />

to produce agglutination. Although previously considered<br />

to be incomplete antibodies, they are known to be bivalent<br />

but may be of a smaller size than saline agglutinable-type<br />

antibodies. R.R.A. Coombs developed this test in England in<br />

the 1940s. In addition to its usefulness in hemolytic disease<br />

of the newborn, the Coombs’ test detects incomplete<br />

antibody-coated erythrocytes from patients with autoimmune<br />

hemolytic anemia. In the direct Coombs’ test, red blood cells<br />

linked to saline nonagglutinable antibody are first washed,<br />

combined with rabbit anti-human immunoglobulin serum,<br />

and then observed for agglutination. In the indirect Coombs’<br />

Epitope<br />

on cell<br />

surface<br />

Mechanism of the antiglobulin test to demonstrate<br />

nonagglutinating antibodies on red cell surfaces in<br />

autoimmune hemolytic anemia<br />

Nonagglutinating<br />

specific antibody<br />

Rabbit antihuman<br />

immunoglobulin<br />

Antiglobulin test.<br />

Epitope<br />

on cell<br />

surface<br />

test, serum containing the saline nonagglutinable antibodies<br />

is combined with red blood cells that are coated but not<br />

agglutinated. The rabbit anti-human immunoglobulin is then<br />

added to these antibody-coated red cells, and agglutination<br />

is observed as in the direct Coombs’ reaction. A third assay<br />

termed the non-gamma test requires the incubation of erythrocytes<br />

with anti-C3 or anti-C4 antibodies. Agglutination<br />

reflects the presence of these complement components on red<br />

blood cell surfaces. This is an indirect technique to identify<br />

IgM antibodies that have fixed complement, such as those<br />

that are specific for Rh blood groups.<br />

antiglutinin<br />

Mammalian seminal plasma substance that prevents<br />

washed spermatozoa from spontaneously agglutinating<br />

(i.e., autoagglutinating).<br />

anti-GM1 antibodies<br />

Antibodies found in 2 to 40% of Guillain–Barré syndrome<br />

(GBS) patients. They are mainly IgG 1, IgG 1, or IgA rather<br />

than IgM, even though IgM anti-GM 1 antibodies have been<br />

found in a few GBS cases. Anti-GM 1 antibodies are more<br />

frequent in GBS patients who experienced Campylobacter<br />

jejuni infection (up to 50% of cases). Titers are highest<br />

initially and fall as the disease progresses. These antibodies<br />

are present in spinal fluid, apparently due to disruption<br />

of the blood–nerve barrier. Anti-GM 1 antibodies recognize<br />

surface epitopes on Campylobacter bacteria, stains, and<br />

possibly a saccharide identical to the terminal tetrasaccharide<br />

of GM 1 that has been found in Campylobacter<br />

lipopolysaccharide. IgG anti-GM 1 has been postulated to<br />

selectively injure motor nerves in GBS.<br />

antigranulocyte antibodies<br />

Antigranulocyte antibodies play a significant role in the<br />

pathogenesis of febrile transfusion reactions, drug-induced<br />

neutropenia, isoimmune neonatal neutropenia, autoimmune<br />

neutropenia (including Felty’s syndrome), Graves’<br />

disease, Evans syndrome, systemic lupus erythematosus<br />

(SLE), and primary autoimmune neutropenia of children.<br />

Antigranulocyte antibodies are best detected and quantitated<br />

by flow cytometry.

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!