IgA - It exists in two isotypes, IgA1 (90%) and IgA2 (10%):IgA1 is found in serum and made by bone

marrow B cells. In IgA2, the heavy and light chains are not linked with disulfide but with noncovalent
bonds. IgA2 is made by B cells located in the mucosae and has been found to secrete into colostrum,
maternal milk, tears and saliva. In secretory IgA, the form of IgA that is found in secretions, polymers
of 2-4 IgA monomers are linked by two additional chains. One of these is the J chain (joining chain),
which is a polypeptide of molecular mass 15kD, rich with cysteine and structurally completely
different from other immunoglobulin chains. This chain is formed in the IgA-secreting cells.The
oligomeric forms of IgA in the external (mucosal) secretions also contain a polypeptide of a much
larger molecular mass (70 kD) called the secretory component that is produced by epithelial cells.
This molecule originates from the poly-Ig receptor (130 kD) that is responsible for the uptake and
transcellular transport of oligomeric (but not monomeric) IgA across the epithelial cells and into
secretions such as tears, saliva, sweat, and gut fluid. Found highly in secretions of the eye. The high
prevalence of IgA in mucosal areas is a result of a cooperation between plasma cells that produce
polymeric IgA (pIgA), and mucosal epithelial cells that express an immunoglobulin receptor called
the polymeric Ig receptor (pIgR). pIgA is released from the nearby activated plasma cells and binds to
pIgR. This results in transportation of IgA across mucosal epithelial cells and its cleavage from pIgR
for release into external secretions.In the blood, IgA interacts with an Fc receptor called FcαRI (or
CD89), which is expressed on immune effector cells, to initiate inflammatory reactions. Ligation of
FcαRI by IgA containing immune complexes causes antibody-dependent cell-mediated cytotoxicity
(ADCC), degranulation of eosinophils and basophils, phagocytosis by monocytes, macrophages,
neutrophils and eosinophils, and triggering of respiratory burst activity by polymorphonuclear
leukocytes. Polymeric IgA (mainly the secretory dimer) is produced by plasma cells in the lamina
propria adjacent to mucosal surfaces. It binds to the polymeric immunoglobulin receptor on the
basolateral surface of epithelial cells and is taken up into the cell via endocytosis. The receptor-IgA
complex passes through the cellular compartments before being secreted on the luminal surface of the
epithelial cells, still attached to the receptor. Proteolysis of the receptor occurs and the dimeric IgA
molecule, along with a portion of the receptor known as the secretory component, are free to diffuse
throughout the lumen.[5] In the gut, it can bind to the mucus layer on top of the epithelial cells to form
a barrier capable of neutralizing threats before they reach the cells. Decreased or absent IgA, termed
selective IgA deficiency, can be a clinically significant immunodeficiency.Neisseria gonorrhœae
(which causes gonorrhea) releases a protease which destroys IgA.IgA nephropathy is caused by IgA
deposits in the kidneys. It is not yet known why IgA deposits occur in this chronic disease. Some
theories suggest it is an abnormality of immune system that results in these deposits

IgD- IgD starts to be expressed when the B-cell exits the bone marrow to populate peripheral
lymphoid tissues. When a B-cell reaches its mature state, it co-expresses both IgM and IgD.
No bilogical effector function has been found.

IgE- IgE is a monomeric antibody with 4 Ig-like domains (CH1->CH4). [1] It plays an
important role in allergy, and is especially associated with type 1 hypersensitivity. IgE elicits
an immune response by binding to Fc receptors found on the surface of mast cells and
basophils, and are also found on eosinophils, monocytes, macrophages and platelets in
humans. Fc has two types:FcεRI, the high-affinity IgE receptor FcεRII, also known as CD23,
is the low-affinity IgE receptor .IgE can upregulate the expression of both Fcε receptors.
FcεRI is expressed only on mast cells and/or basophils in both mice and humans.
Aggregation of antigens and binding of IgE to the FcεRI on mast cells causes degranulation
and the release of mediators from the cells, while basophils cross-linked with IgE release type
2 cytokines like interleukin-4 (IL-4) and interleukin-13 (IL-13) and other inflammatory
mediators. The low affinity receptor (FcεRII) is always expressed on B cells, but its
expression can be induced on the surfaces of macrophages, eosinophils, platelets and some T
cells by IL-4. Atopic individuals can have up to 10 times the normal level of IgE in their
blood. IgE that can specifically recognise an "allergen". has a unique long-lived interaction
with its high affinity receptor, FcεRI, so that basophils and mast cells, capable of mediating
inflammatory reactions, become "primed", ready to release chemicals like histamine,
leukotrienes and certain interleukins, which cause many of the symptoms we associate with
allergy, such as airway constriction in asthma, local inflammation in eczema, increased
mucus secretion in allergic rhinitis and increased vascular permeability, ostensibly to allow
other immune cells to gain access to tissues, but which can lead to a potentially fatal drop in
blood pressure as in anaphylaxis.

IgG - composed of four peptide chains -- two heavy chains γ and two light chains. Each IgG
has two antigen binding sites. IgG antibodies are predominantly involved in the secondary
immune response (the main antibody involved in primary response is IgM). The presence of
specific IgG generally corresponds to maturation of the antibody response. IgG is the only
isotype that can pass through the human placenta, thereby providing protection to the fetus in
utero. Along with IgA secreted in the breast milk, residual IgG absorbed through the placenta
provides the neonate with humoral immunity before its own immune system develops.
Colostrum contains a high percentage of IgG, especially in bovine colostrum.IgG can bind to
many kinds of pathogens, for example viruses, bacteria, and fungi, and protects the body
against them by agglutination and immobilization, complement activation (classical
pathway), opsonization for phagocytosis and neutralization of their toxins. It also plays an
important role in Antibody-dependent cell-mediated cytotoxicity(ADCC) and Intracellular
antibody-mediated proteolysis, in which it binds to TRIM21 (the receptor with greatest
affinity to IgG in humans) in order to direct marked virions to the proteasome in the cytosol.
IgG is also associated with Type II and Type III Hypersensitivity. IgG subclasses consists of
IgG1, IgG2, IgG3 and IgG4. 1,3 and 4 cross the placenta and play and important role in
protecting the developing fetus. 3 is the most effective complement activator followed by 1,2
and 4 is not able to complement at all. 1 and 3 bind with high affinity to Fc receptors on
phagocytic cells and thus mediate opsonization. 4 has an intermediate affinity for Fc
receptors and 2 has an extremely low affinity.

IgM – Accounts for 5% to 10% of the total serum immunoglobulin. Because each monomer
has two antigen binding sites, a pentameric IgM has 10 binding sites. Typically, however,
IgM cannot bind 10 antigens at the same time because the large size of most antigens hinders
binding to nearby sites. its polymeric nature, IgM possesses high avidity, and is particularly
effective at complement activation. Its the first immunoglobulin produced in a primary
response to an antigen. Its pentameric valency makes it effcient with epitopes such as rbc
virus. Plays an important role as a secretory immunoglobulin.