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Interleukin 1 (IL-1) is a protein with several biological activities regulating host defense and immune responses. We report here the isolation of human IL-1 cDNA. It encodes a precursor polypeptide of 269 amino acids (30,747 Mr). mRNA isolated by hybridization to this cDNA was translated in a reticulocyte cell-free system, yielding immunoprecipitable IL-1. Furthermore, this hybrid-selected mRNA was injected into Xenopus laevis oocytes, which subsequently secreted biologically active IL-1. 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.
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A C Webb, and
L J Rosenwasser, and
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C A Dinarello
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Proceedings of the National Academy of Sciences of the United States of America,
P E Auron, and
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January 1991,
DNA sequence : the journal of DNA sequencing and mapping,
P E Auron, and
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January 1992,
DNA sequence : the journal of DNA sequencing and mapping,
P E Auron, and
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Nucleic acids research,
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September 1988,
Nucleic acids research,
P E Auron, and
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A Rich, and
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C A Dinarello
April 1988,
Nucleic acids research,
P E Auron, and
A C Webb, and
L J Rosenwasser, and
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A Rich, and
S M Wolff, and
C A Dinarello
September 1987,
Nucleic acids research,
P E Auron, and
A C Webb, and
L J Rosenwasser, and
S F Mucci, and
A Rich, and
S M Wolff, and
C A Dinarello
August 1988,
Nucleic acids research,
P E Auron, and
A C Webb, and
L J Rosenwasser, and
S F Mucci, and
A Rich, and
S M Wolff, and
C A Dinarello
August 1991,
Nucleic acids research,
P E Auron, and
A C Webb, and
L J Rosenwasser, and
S F Mucci, and
A Rich, and
S M Wolff, and
C A Dinarello
July 1990,
Nucleic acids research,
