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Table 16.5 Carcinogenic Substances in
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Carcinogen Aromatic amines Arsenic Asbestos Benzine Chromium Cigarettes Coal products Dusts Ionizing radiation Iron oxide Isopropyl oil Mustard gas Nickel Petroleum Ultraviolet irradiation Vinyl chloride Wood and leather dust Cancer Site(s) Bladder Liver, lung, skin Lung Bone marrow Lung, nose, nasopharynx sinuses Lung Bladder, lung Lung Bone, bone marrow, lung Lung Nasopharynx sinuses, nose Lung Lung, nasopharynx sinuses, nose Lung Skin Liver Nasopharynx sinuses, nose
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Tamarin: Principles of Genetics, Seventh Edition
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III. Molecular Genetics
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16. Gene Expression: Control in Eukaryotes
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Immunogenetics
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Antigenbinding region NH2 NH2 VL Light CL
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S S S S S S
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S S S
S S S S S
Heavy
S S
COOH VH
S S
S
S S S S
Hinge
S S S S
COOH Figure 16.31
When a mammal (e.g., mouse) is infected by a virus, part of the viral coat is recognized as an antigen, triggering an immune response. B cells produce antibodies that speci cally attach to the viral antigen (humoral immunity). Infected cells present the antigenic part of the viral coat to the outside at the major histocompatibility complex protein on the cell surface. T-cell receptors recognize this MHC-antigen complex and then trigger the destruction of the infected cell (cellular immunity).
Schematic view of an immunoglobulin protein (IgG). V variable region; C constant region; L light chain; H heavy chain. The S-S bonds are sulfhydryl bridges across two cysteines. The NH2 ends of the molecule form the antigen-recognition parts. The internal sulfhydryl bonds roughly mark areas called domains, two each on the light chains and four each on the heavy chains. The heavy chain also has a hinge domain. Similar domains are found in the T-cell receptors and the MHC proteins. These domains indicate the evolutionary relatedness of these three types of molecules.
The dual attack by B and T cells has three main components of genetic interest: antibodies (immunoglobulins), T-cell receptors, and products of the major histocompatibility complex. These three protein families are evolutionarily related to each other, and each provides a diversity of protein products.
Immunoglobulins
Immunoglobulins, produced by the B cells, are large protein molecules composed of two identical light polypeptide chains (about 214 amino acids) and two identical heavy chains (about 440 amino acids), held together by sulfhydryl bonds ( g. 16.32). Each polypeptide chain has a variable and a constant region of amino acid sequences. The variable regions recognize the antigens and thereby give speci city to the immunoglobulins ( g. 16.33). There are ve major types of heavy chains ( , , , , and ), giving rise to ve types of immunoglobulins: IgG, IgA, IgM, IgD, and IgE. Each has slightly different properties;
for example, only IgG can cross the placenta, giving immunity to the fetus. In addition, every immunoglobulin has one of two types of light chains, or (kappa or lambda). Mutations of the constant region of the chains, called allotypes, follow the rules of Mendelian inheritance. In the variable region, however, called the idiotypic variation, diversity is much greater than two alleles per individual. The average individual has the potential to express between 106 and 109 different immunoglobulins, each with a different amino acid sequence. The lower limit, 106, is arrived at through the study of persons with multiple myeloma, a malignancy in which one lymphatic cell divides over and over until it makes up a substantial portion of that person s lymphocytes. From these persons, we can isolate a relatively puri ed immunoglobulin that is the product of a single clone of cells and is referred to as a monoclonal antibody. A very low proportion of a normal person s lymphocytes produces any one speci c immunoglobulin.
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
16. Gene Expression: Control in Eukaryotes
The McGraw Hill Companies, 2001
Sixteen
Gene Expression: Control in Eukaryotes
Multiple myeloma cells can be fused to spleen cells. The resulting cells, called hybridomas, which produce monoclonal antibodies, can be perpetuated in tissue culture inde nitely, thus providing a ready supply of speci c monoclonal antibodies. Recent work with hybridomas has allowed us to locate, isolate, and sequence immunoglobulin genes. How can one genome produce 109 different antibody molecules
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