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M J Commoy-Chevalier

Publications and source records attributed to M J Commoy-Chevalier.

5 recordsLinked to original sources
PubMed1985

Phosphorylation of recombinant interferon-gamma by kinases released from various cells.

Recombinant interferon-gamma (IFN-gamma) in contact with human embryonic fibroblasts or with a great variety of cells from different animal species was phosphorylated in the presence of [gamma-32P]ATP and magnesium ions by a protein kinase released in the culture medium. Using SDS-polyacrylamide gel electrophoresis, we found that both the monomeric (17 000 to 18 000) and dimeric (34 000 to 35 000) molecular weight forms of IFN-gamma became intensely radioactive. Serine, but not threonine or tyrosine, was phosphorylated. It is of interest that the kinase released from reputedly insensitive cells also phosphorylated IFN-gamma. The process did not noticeably degrade the antiviral functions of the molecule nor did it affect, at least in a detectable manner, its anti-proliferative effect on WISH or Daudi cells. Furthermore, the antigenic structure and its capacity to react with monoclonal antibodies were also unaltered. It is presently not known which biological function is regulated by the phosphorylating process.

Animals↗
PubMed1980

[Production of human type I interferon by lymphocytes in contact with cells infected by herpesvirus and fixed with glutaraldehyde].

Type I interferon was released from human lymphocytes cultured on cells infected with Herpesvirus and fixed with glutaraldehyde. This process of interferon induction did not involve histocompatibility antigens nor the Herpes immunity of the lymphocyte donors. Type I interferon can also be induced after interaction between lymphocytes and other intranuclear replicating virus infected cells.

Adult↗
PubMed1979

Human leukocyte interferon: relationship between molecular structure and species specificity.

Human leukocyte interferon can be separated into two classes of subspecies by polynucleotide-agarose affinity chromatography; 30-40% of the molecular species have the polynucleotide-binding property and 60-70% lack affinity for the polynucleotide ligand. When analyzed on sodium dodecyl sulfate/polyacrylamide gel electrophoresis, the former class of interferon has a slower mobility corresponding to the migration of a polypeptide of 21,000 daltons, while the latter class has a faster mobility corresponding to a polypeptide of 13,500-15,000 daltons. By analogy to the behavior of other interferons and a class of nucleotidyl transferases on the polynucleotide-agarose chromatography, we suggest that the human leukocyte interferon having the polynucleotide-binding site is in a possibly "native" conformation and the loss of affinity for polynucleotide results from a degradative alteration of the native molecules. Moreover, the alteration of interferon is accompanied by an increase in heterospecific activity on bovine cells. It is suggested that the polypeptide domain responsible for species specificity may be closely related to the polynucleotide binding area. The modified interferon molecule, however, still conserves its antiviral activity. The simplicity and the high capacity of polynucleotide-agarose chromatography make this a powerful technique for the purification of interferon. The easy separation of these two classes of human leukocyte interferon makes the purification procedures more rational and will facilitate the preparation of both subspecies to a high degree of molecular homogeneity.

Animals↗
PubMed1978

Effect of ammonium salts on the interferon-induced antiviral state in mouse L cells.

The addition of ammonium salts to cells treated with interferon prevents the development of the antiviral state and destroys it when already established. This treatment does not seem to act on the binding of interferon to the cells but blocks a further step of activation on the cell membrane. The anti-interferon effect of ammonium salts is reversible with a complete recovery of the antiviral state. It is postulated that these salts may stabilize the interferon-receptor complex and thus prevent the changes in configuration necessary for the establishment and maintenance of its biological functions.

Ammonium Chloride↗