Human Major Histocompatibility Complex Contains Genes for the Major Heat Shock Protein HSP70

• Published in: Proceedings of the National Academy of Sciences - PNAS 1989-03, Vol.86 (6), p.1968-1972
• Main Authors: Sargent, Carole A., Dunham, Ian, Trowsdale, John, Campbell, R. Duncan
• Format: Article
• Language: English
• Subjects: 550201 - Biochemistry- Tracer Techniques; Amino Acid Sequence; ANIMALS; ANTIGENS; Base Sequence; BASIC BIOLOGICAL SCIENCES; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; Biological and medical sciences; BIOLOGICAL EVOLUTION; BIOLOGICAL STRESS; Chromosome Mapping; Chromosomes, Human, Pair 6; Cloning, Molecular; Complement System Proteins - genetics; Cosmids; DAYS LIVING RADIOISOTOPES; DISEASES; DNA; DNA HYBRIDIZATION; DNA probes; DNA Restriction Enzymes; ETIOLOGY; Fundamental and applied biological sciences. Psychology; Gels; GENES; Genes. Genome; Genetic hybridization; Genetic loci; Genomics; Heat-Shock Proteins - genetics; HISTOCOMPATIBILITY COMPLEX; HUMAN POPULATIONS; Humans; HYBRIDIZATION; IMMUNE SYSTEM DISEASES; ISOTOPES; LIGHT NUCLEI; Major Histocompatibility Complex; MAMMALS; MAN; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; NUCLEI; Nucleic Acid Hybridization; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; PHOSPHORUS 32; PHOSPHORUS ISOTOPES; POPULATIONS; PRIMATES; PROTEINS; RADIOISOTOPES; RFLPS; Sequence Homology, Nucleic Acid; T lymphocytes; T-Lymphocytes - immunology; Tumor Necrosis Factor-alpha - genetics; VERTEBRATES
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.6.1968

Little is known as to why a large number of human diseases are influenced by the major histocompatibility complex. In some cases, a direct involvement of the products of the polymorphic class I and class II, as well as the less variable products of the class III, genes has been proposed. During characterization of the class III region for the presence of additional loci, we have located a duplicated locus encoding the major heat shock protein HSP70 between the complement and tumor necrosis factor genes. The HSP70 loci are 12 kilobases apart and lie 92 kilobases telomeric of the C2 gene. As HSP70 proteins have been linked with a protective role during and after cellular stress, and HSP70 analogues are often presented as antigens in bacterial and protozoal infections, this finding may have major implications with regard to the major histocompatibility complex and associated diseases.