Expression Cloning of an Interferon-inducible 17-kDa Membrane Protein Implicated in the Control of Cell Growth (∗)

Interferon-inducible membrane proteins of approximately 17 kDa have been suggested to play a role in the antiproliferative activity of interferons based on (1) their pattern of induction in interferon-sensitive and -resistant cell lines and (2) the ability of a membrane fraction enriched in 17-kDa p...

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Published in:	The Journal of biological chemistry Vol. 270; no. 40; pp. 23860 - 23866
Main Authors:	Deblandre, Gisèle A., Marinx, Olivier P., Evans, Sharon S., Majjaj, Samira, Leo, Oberdan, Caput, Daniel, Huez, Georges A., Wathelet, Marc G.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 06-10-1995 American Society for Biochemistry and Molecular Biology
Subjects:	Animals Antibodies, Monoclonal Base Sequence Cell Division - drug effects Cell Division - genetics Cell Division - physiology Cell Line Cloning, Molecular DNA Primers - genetics DNA, Complementary - genetics Growth Inhibitors - biosynthesis Growth Inhibitors - chemistry Growth Inhibitors - genetics Humans Interferon Type I - pharmacology Interferon-gamma - pharmacology Membrane Proteins - biosynthesis Membrane Proteins - chemistry Membrane Proteins - genetics Mice Molecular Sequence Data Molecular Weight Recombinant Proteins Transfection
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Summary:	Interferon-inducible membrane proteins of approximately 17 kDa have been suggested to play a role in the antiproliferative activity of interferons based on (1) their pattern of induction in interferon-sensitive and -resistant cell lines and (2) the ability of a membrane fraction enriched in 17-kDa proteins to inhibit cell growth. To gain insight into the nature of the proteins that mediate the antiproliferative activity of interferons, a monoclonal antibody, 13A5, was generated that reacted specifically with a 17-kDa interferon-inducible cell surface protein. The expression pattern of this 17-kDa protein by human cell lines correlated with sensitivity to the antiproliferative activity of interferons. To obtain information regarding the structure of this protein, the 13A5 antibody was used to screen COS cells transfected with a human cDNA expression library. Sequence analysis of a full-length cDNA clone revealed identity with the 9-27 cDNA, previously isolated on the basis of its interferon inducibility by differential screening. In addition, the 17-kDa protein encoded by the 9-27 gene was shown to be identical to the Leu-13 antigen. Leu-13 was previously identified as a 16-kDa interferon-inducible protein in leukocytes and endothelial cells and is a component of a multimeric complex involved in the transduction of antiproliferative and homotypic adhesion signals. These results suggest a novel level of cellular regulation by interferons involving a membrane protein, encoded by the interferon-inducible 9-27 gene, which associates with other proteins at the cell surface, forming a complex relaying growth inhibitory and aggregation signals.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0021-9258 1083-351X
DOI:	10.1074/jbc.270.40.23860