Cloning, sequence and expression of bovine interleukin 1α and interleukin 1β complementary DNAs
| Autor: | Paul E. Baker, Brian S. Davis, Charles R. Maliszewski, Douglas P. Cerretti, Steven Gillis, Michael A. Schoenborn, David Cosman |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Molecular Sequence Data
Immunology Molecular cloning Biology law.invention law Complementary DNA Animals Amino Acid Sequence RNA Messenger Cloning Molecular Molecular Biology Gene chemistry.chemical_classification Base Sequence Nucleic acid sequence Interleukin DNA Molecular biology Recombinant Proteins Amino acid Open reading frame chemistry Recombinant DNA Cattle Interleukin-1 |
| Zdroj: | Molecular Immunology. 25:429-437 |
| ISSN: | 0161-5890 |
| Popis: | Interleukin 1 (IL-1) is a cytokine which mediates a variety of immunoregulatory and inflammatory activities. Using human IL-1 alpha and IL-1 beta probes, cDNAs for the corresponding bovine genes were isolated from an alveolar macrophage library. The open reading frames of the bovine IL-1 alpha and IL-1 beta cDNAs encode proteins of 268 and 266 amino acids, respectively, each with a predicted mol. wt of approx. 31,000. Both forms of bovine IL-1 exhibit a high degree of sequence homology with IL-1 gene products from other mammalian species. Based upon comparisons with human IL-1 amino acid sequences, the post-translationally processed, mature forms of bovine IL-1 would occur as 17-18,000 mol. wt proteins. Sequences encoding mature bovine IL-1 alpha and IL-1 beta were inserted into E. coli expression plasmids and biologically active proteins were synthesized as judged by the ability of the recombinant proteins to induce proliferation of bovine thymocytes. Both IL-1 alpha and IL-1 beta exist as single genomic copies. In addition, bovine IL-1 beta mRNA is approx. 10-fold more abundant than IL-1 alpha mRNA in stimulated alveolar macrophages. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|