Cloning and characterization of a cDNA for murine macrophage inflammatory protein (MIP), a novel monokine with inflammatory and chemokinetic properties

In the course of studies on cachectin/TNF being conducted in our laboratory, a novel macrophage product has been detected and characterized. Termed macrophage inflammatory protein or MIP, this protein appears to be an endogenous mediator of the inflammatory events induced by endotoxin. A cDNA cloned...

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Bibliographic Details
Published inThe Journal of experimental medicine Vol. 167; no. 6; pp. 1939 - 1944
Main Authors DAVATELIS, G, TEKAMP-OLSON, P, WOLPE, S. D, HERMSEN, K, LUEDKE, C, GALLEGOS, C, COIT, D, MERRYWEATHER, J, CERAMI, A
Format Journal Article
LanguageEnglish
Published New York, NY Rockefeller University Press 01.06.1988
The Rockefeller University Press
Subjects
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Biological Products - genetics
Cell Line
Chemotactic Factors - genetics
Cloning, Molecular
DNA - genetics
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Immunobiology
Interleukin-8
Lipopolysaccharides - pharmacology
Lymphocyte Activation
Mice
Molecular Sequence Data
Monokines
Myeloid cells: ontogeny, maturation, markers, receptors
RNA, Messenger - genetics
Proteins
Complementary DNA
Nucleotide sequence
Production
Monokine
Chemical mediator
Inflammation
Molecular cloning
Endotoxin
Aminoacid sequence
Macrophage
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Summary:In the course of studies on cachectin/TNF being conducted in our laboratory, a novel macrophage product has been detected and characterized. Termed macrophage inflammatory protein or MIP, this protein appears to be an endogenous mediator of the inflammatory events induced by endotoxin. A cDNA cloned probe for this protein has been isolated from a lambda gt10 phage library prepared from poly(A)+ RNA obtained of endotoxin-induced RAW264.7 cells. The sequence codes for a 92 amino acid-long polypeptide, of which 69 amino acids correspond to the mature product. The sequence predicts a molecular weight of 7,889 and structural analysis of the protein indicates a characteristic signal sequence alpha-helix and a hydrophobic core. Sequence data also confirm no sequence similarity to any other protein listed in the Dayhoff data base.
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ISSN:0022-1007
1540-9538
DOI:10.1084/jem.167.6.1939