Isotype

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Isotype refers to the genetic variations or differences in the constant region of the immunoglobulin (Ig) molecules. These variations are consistent across all individuals of a species and are used to classify immunoglobulins into different classes and subclasses. Isotypes are crucial for the immune system's ability to respond to a wide range of pathogens.

Structure and Function[edit | edit source]

Immunoglobulins, also known as antibodies, are glycoproteins produced by B cells that play a key role in the immune response. Each immunoglobulin molecule consists of two heavy chains and two light chains. The heavy chains determine the isotype of the antibody.

There are five main isotypes of immunoglobulins in humans:

  • IgA: Found in mucous membranes, saliva, tears, and breast milk. It plays a critical role in mucosal immunity.
  • IgD: Functions mainly as a receptor on B cells that have not been exposed to antigens.
  • IgE: Involved in allergic reactions and protection against parasitic infections.
  • IgG: The most abundant isotype in the blood, providing the majority of antibody-based immunity against pathogens.
  • IgM: The first antibody produced in response to an infection, it is effective in forming complexes with antigens.

Genetic Basis[edit | edit source]

The isotype of an immunoglobulin is determined by the constant region of the heavy chain gene. Each isotype is encoded by a different constant region gene segment located in the immunoglobulin heavy chain locus on chromosome 14 in humans.

Clinical Significance[edit | edit source]

Understanding isotypes is important in clinical settings for diagnosing and monitoring various diseases. For example, elevated levels of IgE are associated with allergic conditions, while IgG levels can indicate past exposure to pathogens or vaccination status.

Research and Applications[edit | edit source]

Isotypes are used in various research and diagnostic applications, including:

Also see[edit | edit source]



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