The Full Wiki

More info on Immunoglobulin light chain

Immunoglobulin light chain: Wikis

Advertisements
  

Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.

Encyclopedia

From Wikipedia, the free encyclopedia

Schematic diagram of an typical antibody showing two Ig heavy chains (blue) linked by disulfide bonds to two Ig light chains (green). The constant (C) and variable (V) domains are shown.
An antibody molecule. The two heavy chains are colored red and blue and the two light chains green and yellow. See also:[1]

A light chain is the small polypeptide subunit of an antibody (or immunoglobulin). A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains.

Contents

In humans

There are two types of light chain in mammals,

  • lambda (λ) chain
  • kappa (κ) chain

Antibodies are produced by B lymphocytes which each express only one class of light chain. Once set, light chain class remains fixed for the life of the B lymphocyte. In a healthy individual, the total kappa to lambda ratio is roughly 65 to 35, with a highly divergent ratio indicative of neoplasm.

In other animals

The immunoglobulin light chain genes in tetrapods can be classified into three distinct groups: kappa (κ), lambda (λ), and sigma (σ). The divergence of the κ, λ, and σ isotypes preceded the radiation of tetrapods. The σ isotype was lost after the evolution of the amphibian lineage and before the emergence of the reptilian lineage.[1]

Other types of light chains can be found in lower vertebrates, such as the Ig-Light-Iota chain of Chondrichthyes and Teleostei.[2][3]

Camelids are unique among mammals as they have fully functional antibodies which have two heavy chains, but lack the light chains usually paired with each heavy chain.[4] The functional role of this separate repertoire is unknown as yet.

Structure

Only one type of light chain is present in a typical antibody, thus the two light chains of an individual antibody are identical.

Each light chain is composed of two tandem immunoglobulin domains:

  • one constant (IgC) domain
  • one variable domain (IgV) that is important for binding antigen

The approximate length of a light chain protein is from 211 to 217 amino acids.[2]

In pathology

Ig light chains produced in neoplastic plasma cells, e.g. in multiple myeloma, are called Bence Jones proteins.

References

  1. ^ Das S, Nikolaidis N, Klein J, Nei M (2008). "Evolutionary redefinition of immunoglobulin light chain isotypes in tetrapods using molecular markers". Proc Natl Acad Sci U S A. 105 (43): 16647–52. doi:10.1073/pnas.0808800105. PMID 18940927.  
  2. ^ a b Janeway CA, Jr. et al. (2001). Immunobiology. (5th ed.). Garland Publishing. (electronic full text via NCBI Bookshelf) ISBN 0-8153-3642-X.  
  3. ^ IMGT Index Antibodies (or Immunoglobulins).
  4. ^ Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa E, Bendahman N, Hamers R (1993). "Naturally occurring antibodies devoid of light chains". Nature 363 (6428): 446–8. doi:10.1038/363446a0. PMID 8502296.  

External links

Advertisements

Advertisements






Got something to say? Make a comment.
Your name
Your email address
Message