A unique set of polypeptides is induced by γ interferon in addition to those induced in common with α and β interferons
Autor: | Lois B. Epstein, Jon Weil, J. James Sedmak, Sidney E. Grossberg, Jan L. Sabran, Charles J. Epstein |
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Rok vydání: | 1983 |
Předmět: |
Peptide Biosynthesis
chemistry.chemical_classification Gel electrophoresis Cell type Multidisciplinary Biological activity Fibroblasts Biology Cell Line Amino acid Molecular Weight Interferon-gamma medicine.anatomical_structure chemistry Biochemistry Interferon Type I medicine Protein biosynthesis Humans Down Syndrome Fibroblast Intracellular Function (biology) |
Zdroj: | Nature. 301:437-439 |
ISSN: | 1476-4687 0028-0836 |
DOI: | 10.1038/301437a0 |
Popis: | Human immune interferon (IFN-gamma) differs from leukocyte interferon (IFN-alpha) and fibroblast interferon (IFN-beta) in cell origin, inducing agents, physical and biological properties and amino acid sequence. These differences have led to interest in possible differences in the biological properties of IFN-gamma compared with IFN-alpha and IFN-beta. IFN-gamma has the same broad range of biochemical and biological actions as do IFN-alpha and IFN-beta, although relative potencies vary depending on the cell type and function investigated. There has so far been no direct evidence that IFN-gamma alters normal cell functions differently from other interferons. We report here striking qualitative and quantitative differences in the intracellular response of human fibroblasts to IFN-gamma compared with IFN-alpha and IFN-beta. Two-dimensional gel electrophoresis demonstrates, in addition to the induction of a common group of polypeptides, the existence of a set of polypeptides whose synthesis is uniquely induced by IFN-gamma. |
Databáze: | OpenAIRE |
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