Immunoglobulins are complex proteins that recognize foreign antigens in the body. They bind to these antigens, neutralize them and allow their destruction. Some immunoglobulins are integrated into the cell membrane where others, known as antibodies, are secreted there. The antibodies consist of two heavy chains (encoded by the IGH locus on chromosome 14) and two light chains encoded by either the IGL locus or the IGK locus on chromosome 2. All three loci share an unusual feature in which the gene region is responsible for the antigen binding ability of the chains divided into numerous alternative segments. These segments are combined at random, at the DNA level during B-lymphocyte maturation, so that each B-cell clone represents a different antibody with unique antigenic specificity. The IGL locus has 52 variable (V) segments, seven binding (J) segments, and seven alternative constant (C) regions. Further diversity can be achieved by varying the recombination site, the addition or deletion of nucleotides at the compounds, and by introducing random mutations into the entire sequence of the antigen binding domain.
One of the significant diseases related to the IGL locus and its chromosomal translocation is leukemia. This reflects the fact that the IGL gene is expressed at a very high level due to its strong promoter trait. Translocations that place oncogenes (genes that promote cell division) under the control of this regulatory system result in high levels of gene expression, which promotes cell proliferation.
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