Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs

  title={Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs},
  author={Carl J. March and Bruce Mosley and Alf D. Larsen and Douglas Pat Cerretti and Gary Braedt and Virginia L. Price and Steven Gillis and Christopher S. Henney and Shirley R. Kronheim and Kenneth H. Grabstein and Paul J. Conlon and Thomas P Hopp and David J. Cosman},
Two distinct but distantly related complementary DNAs encoding proteins sharing human interleukin-1 (IL-1) activity (termed IL-lα and IL-1β), were isolated from a macrophage cDNA library. The primary translation products of the genes are 271 and 269 amino acids long, although expression in Escherichia coli of the carboxy-terminal 159 and 153 amino acids produces IL-1 biological activity. 
Primary structure and functional expression from complementary DNA of a human interleukin-1 receptor antagonist
Human monocytes induced with adherent IgG secrete an interleukin-1 receptor antagonist which could be important for the in vivo regulation of IL-1 activity and analysis of monocyte RNA indicates that the gene is transcriptionally regulated.
cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.
A direct expression strategy was used to clone the receptor for IL-1 from mouse T cells and the product of the cloned complementary DNA binds bothIL-1 alpha and IL-2 beta in a manner indistinguishable from that of the native T cell IL- 1 receptor.
Molecular cloning of the interleukin-1 beta converting enzyme.
Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA
Molecular cloning of a complementary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1).
The CSF-1 appears to be encoded by a single-copy gene, but its expression results in the synthesis of several messenger RNA species, ranging in size from about 1.5 to 4.5 kilobases.
Cloning and Characterization of an Alternatively Processed Human Type II Interleukin-1 Receptor mRNA*
The purification and characterization of a soluble IL- 1 receptor expressed by COS1 cells and the cloning of an alternatively processed type II IL-1 receptor mRNA from both human and COS 1 cells are reported.
A chicken homolog of mammalian interleukin-1 beta: cDNA cloning and purification of active recombinant protein.
Sequence homology and structural features indicate that this protein is the chicken homolog of mammalian interleukin-1beta (ChIL-1 beta), and northern blot analysis showed that ChIL- 1 beta RNA is quickly induced in blood monocyte-derived macrophages reaching maximal levels within one hour after onset of LPS treatment.


Structure and expression of a cloned cDNA for human interleukin-2
A cDNA coding for human interleukin-2 (IL-2) has been cloned from a cDNA library prepared from partially purified IL-2 mRNA, which consists of 153 amino acids including a putative signal sequence.
Nucleotide sequence of human monocyte interleukin 1 precursor cDNA.
The cDNA nucleotide sequence suggests that IL-1 is initially translated as a precursor molecule that is subsequently processed into the 15,000-20,000 Mr protein usually associated with IL- 1 activity.
Molecular cloning of cDNA for murine interleukin-3
The predicted amino acid sequence indicates that formation of mature interleukin-3 involves proteolytic removal of not only the signal peptide but additional ammo-terminal amino acids.
Expression of human immune interferon cDNA in E. coli and monkey cells
The polypeptide produced through expression of this DNA sequence in Escherichia coli or cultured monkey cells had properties characteristic of authentic human IFN-γ.
Cloning and expression of murine interleukin-1 cDNA in Escherichia coli
The cloning, sequence analysis and expression of murine IL-1 cDNA in Escherichia coli reveals a polypeptide precursor of 270 amino acids that may play a major role in the initiation and amplification of immune and inflammatory responses through its action on these diverse cell populations.
Cloning, sequence and expression of human interleukin-2 receptor
Synthetic oligonucleotides are used to probe a complementary DNA library, prepared from HUT-102 messenger RNA, for the presence of cDNA clones that might code for the IL-2 receptor.
Molecular cloning of cDNA encoding a murine haematopoietic growth regulator, granulocyte—macrophage colony stimulating factor
cDNA clones specifying the murine granulocyte–macrophage colony stimulating factor have been isolated and it bears no structural similarity to the functionally related factor, interleukin-3, described recently.
Human interleukin 1. Purification to homogeneity
Human IL-1, secreted by human peripheral blood macrophages that have been stimulated with Staphylococcus aureus, was purified by ion exchange chromatography and affinity chromatography on Procion Red agarose by a simplified procedure that results in excellent yields of pure material that retains a high level of biological activity.
Purification and partial biochemical characterization of normal human interleukin 1
  • J. Schmidt
  • Biology
    The Journal of experimental medicine
  • 1984
Amounts of IL-1 sufficient for receptor studies and detailed biochemical analysis can now be produced on a regular basis.
Studies on the synthesis and secretion of interleukin 1. I. A 33,000 molecular weight precursor for interleukin 1.
The results indicate that IL 1 is synthesized as a 33,000 m.w. precursor that is converted to the low m.W. form that is found in the culture fluid of stimulated murine macrophages.