Immunoglobulin
(Ig) is a protein secreted by plasma cells, the differentiated B cells, and
binds with a particular antigen. Immunoglobulin is also called antibody. All
antibodies have the same Y-shaped structure and in their monomer form consists
of two identical heavy chains and two identical light chains.1 Immunoglobulin
is divided by five classes, namely IgG, IgM, IgA, IgD and IgE.2
Those classes are determined by the structure difference
in heavy-chain constant region. For this reason, those classes have no effects
towards the antibody specifity, whereas
the antibody specifity is determined by antigen binding sites.3
Immunoglobulins
belong to the group of glycoproteins called globulins. Immunoglobulin consists
of four polypeptides chains, that is two identical Heavy (H) chains and two
identical Light (L) chains. In every H and L chain are two distinct regions. In
the tips of the chain, there is V (variable) region as the sites of antigen
binding. It is V region that recognizes and attaches specifically to particular
antigen.3 The remainder L and H is the constant (C) region, nearly
the same to all antibodies in the same class, is responsible on the kind of
antigen-antibody reactions occurs.2
Immunoglobulin
and antibody is the important part of body’s defense in
protecting body from antigens (strange objects)
that go inside the body. Immunoglobulin can be found in blood plasma.4
When an antigen go inside the body, B cell, or B lymphocyte, encounters by
binding immunoglobulin molecules, exist as integral proteins within plasma
membrane of B cell, towards the antigen. When immunoglobulin molecule binds
with specific epitope on the antigen, particular cytokines is secreted by
T-helper cells, then B cell becomes activated, proliferates into plasma cells and memory cells.1,4
Each of plasma B cells is the manufacturer of immunoglobulin that the specifity
is the same as parent B cells that binds with antigens. Next, these
antibodies go inside blood and lymphatic circulations, as well as in
extracellular fluid, and then bind with proper antigen epitopes in anywhere in
the body. Once the antibody has coated proper antigen, other cells and chemical
processes will be activated to eliminate the antigen.4 The ways of
antibodies inactivating antigens are neutralizing antigens,
immobilizing bacteria, agglutinating and precipitating antigens, activating
complement system, enhancing phagocytosis, opsonizing, stimulating inflammation
and preventing bacterial and viral adhesions.3,4
There
are five classes of immunoglobulin (Ig). IgM plays a role by coating
(opsonizing) antigen for destructing and fixing complement system. IgM antibody
is associated with primary immune response and frequently used to diagnosing
acute exposure to an immunogen or pathogen. IgD has unclear functions, as it is
unknown participating within major antibody effector mechanisms.5
IgG antibody is responsible in resistance against many viruses, bacteria and
bacterial toxins. IgE plays an important role in allergy response and when this
antibody binds with antigen, it will stimulate the cell to release histamine
and other chemicals for accelerating inflammation in the immediate region.3
Then, IgA is found in a huge quantities in mucous membranes of digestive, urogenital
and respiratory systems, and functions in preventing pathogens attach on the
surface of cells.6
References
1. Reece
JB, Urry LA, Cain ML, Wasserman SA, Minorsky PV, Jackson RB. Campbell biology,
9th ed. San Francisco (CA): Pearson Benjamin Cummings; 2011.
2. Tortora
GJ, Derrickson B. Principles of anatomy and physiology, 12th ed. Danvers (MA):
John Wiley adn Sons, Inc; 2009.
3. Martini
FH, Nath JL, Bartholomew EF. Fundamentals of anatomy and physiology, 10th ed.
San Francisco: Pearson Benjamin Cummings; 2014.
4. Raven
PH, Johnson GB, Mason KA, Losos JB, Singer SR. Biology, 9th ed. New York:
McGraw-Hill; 2011.
5. Schroeder
HW, Cavacini L. Structure and function of immunoglobulins. J Allergy Clin
Immunol. 2010 Feb; 125(202): S41–S52
6. Enger
ED, Ross FC, Bailey DB. Concepts in biology, 14th ed. New York: McGraw-Hill;
2012.
*proudly written by using Vancouver Writing System
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