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Immunoglobulin D
Despite the body having a cell-mediated immune system responsible for destroying
infected cells and invasive pathogens, it also has a humoral immune system mediated by
IgD, IgG, IgA, and IgE. Make up the human immunoglobulin types. IgD is one of the least
abundant immunoglobulins representing about 0.25% of serum antibodies. The molecule has a
185000 molar mass and a 2.8-day half-life, similar to IgE. This paper explores IgG to discover
IgD has the basic immunoglobulin structure comprising identical heavy and light
polypeptide chains. The immunoglobulin also has the Fab region with antigen-binding sites and
the FC region where cellular receptors bind. The two identical antigen binding sites have a
valence of 2 with multiple variable regions at the outermost terminals (Flaherty 75). A hinge
region intersects the Fab and Fc regions giving the immunoglobulin a Y-shaped appearance.
Heat labile disulfide bonds susceptible to proteases join the two regions. The IgG locus
The location of IgD reflects its biological significance. The antibody has a low abundance
of 0.25% making it one of the least abundant antibodies in the human serum. The largest volume
of the antibody is in the nasal, salivary, mammary, and cerebrospinal fluids. Significant volumes
can also be found in lacrimal, bronchial, and mammary fluids, with intestinal sections containing
negligible amounts of the antibody. IgD distribution is more prevalent depending on the presence
of IgD+IgM− plasma secretory cells (Chorny and Cerutti 685). These cells are less abundant in
the intestinal mucosa but have an increased presence in salivary glands, tonsils, nasal mucosa,
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and lachrymal glands. The positioning of immunoglobulin in these regions is strategic for
effective functioning.
IgD is an interesting molecule because its functions remain obscure. However, some
functions are outlined. The primary function of the antibody is its role as a B-cell antigen
receptor. This function makes a regulator for B-cell function when encountering an antigen. The
second function is performed with IgM. Interactions between IgD and IgM in the presence of an
antigen for which the antibodies are specific cause its internalization and presentation to T cells.
The T cells trigger a process through which B cells multiply and differentiate into plasma cells.
This is the mechanism for humoral immune response development (Schultz 1). The third
function is performed in blood, body secretions with IgD and immune effector cells. IgD
activates antimicrobial factors that confer immunity to the human respiratory system. Lastly, IgD
plays a minor role in allergic reactions. These functions make IgD an important part of the
IgD deficiency characterized by low serum IgD levels is associated with few symptoms.
According to Hernandez, about 6% to 11% of blood donors in the US have low or undetectable
IgD levels. Most participants in studies examining this condition present rheumatologic diseases
like juvenile rheumatoid arthritis and psoriatic arthritis. However, patient dying or their disease
conditions worsening is not related to low concentration levels of IgD. Patients with low IgD
concentrations in their bodies have no risk of other conditions worsening. Males and females
report similar occurrences of the condition. These facts make the medical significance of IgD an
Works Cited
Chorny, Alejo, and Andrea Cerutti. “Regulation and Function of Mucosal IGA and IgD.”
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Schultz, Clyde. “Immunoglobulin D.” General Internal Medicine and Clinical Innovations, vol.