Immunoglobulins are complexes of proteins that recognize foreign antigens in the body. They bind to these antigens, neutralize them and contribute to their destruction. Some immunoglobulins are integrated into the leukocyte cell membrane as other immunoglobulins, known as antibodies, are excreted into the bloodstream. The antibodies are constructed of two heavy chains (encoded by the IGH gene on chromosome 14) and two light chains encoded by either the IGK gene or the IGL gene on chromosome 22. All three loci share the unusual properties of the region where the genes whose products correspond to the antigen-binding the antibody region is divided into a number of alternative segments. These segments were combined at random, at the DNA level, during B-lymphocyte maturation, so that each B-cell clone represented a different antibody with different antigenic properties. The IGK locus has 76 variable gene segments (V) and five binding segments (J) that can be combined in different ways and be fused to a single constant (C) region of the antibody. Further diversity can be achieved by varying the recombination site, adding and removing nucleotides at the compounds, and introducing random mutations into the entire sequence of the antigen binding domain.
The most well-known aspect of the IGK locus associated with a disease is the chromosomal translocations that precede and cause a large number of leukemias. This is because the IGK gene is expressed at a very high (frequent) level. Translocations that bring oncogenes (genes that are important for cell division) under the control of the IGK promoter result in frequent expression of the oncogenes and thus uncontrolled cell proliferation.
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