Activation of transforming potential of the human insulin receptor gene

Wang, L H; Lin, B; Jong, S M.J.; Dixon, D; Ellis, L; Roth, R A; Rutter, W J

doi:10.1073/pnas.84.16.5725

Title: Activation of transforming potential of the human insulin receptor gene

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Abstract

A retrovirus containing part of the human insulin receptor (hIR) gene was constructed by replacing ros sequences in the avian sarcoma virus UR2 with hIR cDNA sequences coding for 46 amino acids of the extracellular domain and the entire transmembrane and cytoplasmic domains of the ..beta.. subunit of hIR. The resulting virus, named UIR, contains the hIR sequence fused to the 5' portion of the UR2 gag gene coding for p19. UIR is capable of transforming chicken embryo fibroblasts and promoting formation of colonies in soft agar; however, it does not form tumors in vivo. A variant that arose from the parental UIR is capable of efficiently inducing sarcomas in vivo. UIR-transformed cells exhibit higher rates of glucose uptake and growth than normal cells. The 4-kilobase UIR genome codes for a membrane-associated, glycosylated gag-hIR fusion protein of 75 kDa designated P75/sup gag-hir/. P75/sup gag-hir/ contains a protein tyrosine kinase activity that is capable of undergoing autophosphorylation and of phosphorylating foreign substrates in vitro; it is phosphorylated at both serine and tyrosine residues in vivo

Authors:: Wang, L H; Lin, B; Jong, S M.J.; Dixon, D; Ellis, L; Roth, R A; Rutter, W J

Publication Date:: Sat Aug 01 00:00:00 EDT 1987

Research Org.:: Rockefeller Univ., New York, NY (USA)

OSTI Identifier:: 5209520

Resource Type:: Journal Article

Journal Name:: Proc. Natl. Acad. Sci. U.S.A.; (United States)

Additional Journal Information:: Journal Volume: 84:16

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; ONCOGENIC TRANSFORMATIONS; GENE REGULATION; SERINE; PHOSPHORYLATION; TYROSINE; ENZYME ACTIVITY; FIBROBLASTS; GENES; LEUCINE; ONCOGENIC VIRUSES; PHOSPHORUS 32; PHOSPHOTRANSFERASES; RECEPTORS; RECOMBINANT DNA; TRITIUM COMPOUNDS; AMINO ACIDS; ANIMAL CELLS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CARBOXYLIC ACIDS; CELL TRANSFORMATIONS; CHEMICAL REACTIONS; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; DNA; ENZYMES; HYDROXY ACIDS; ISOTOPES; LABELLED COMPOUNDS; LIGHT NUCLEI; MEMBRANE PROTEINS; MICROORGANISMS; NUCLEI; NUCLEIC ACIDS; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; PARASITES; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; PROTEINS; RADIOISOTOPES; SOMATIC CELLS; TRANSFERASES; VIRUSES; 550201* - Biochemistry- Tracer Techniques

Citation Formats


                    Wang, L H, Lin, B, Jong, S M.J., Dixon, D, Ellis, L, Roth, R A, and Rutter, W J. Activation of transforming potential of the human insulin receptor gene.  United States: N. p., 1987. 
        Web.  doi:10.1073/pnas.84.16.5725.

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                    Wang, L H, Lin, B, Jong, S M.J., Dixon, D, Ellis, L, Roth, R A, & Rutter, W J. Activation of transforming potential of the human insulin receptor gene.  United States.  https://doi.org/10.1073/pnas.84.16.5725

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                    Wang, L H, Lin, B, Jong, S M.J., Dixon, D, Ellis, L, Roth, R A, and Rutter, W J. 1987.  
        "Activation of transforming potential of the human insulin receptor gene".  United States.  https://doi.org/10.1073/pnas.84.16.5725.

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@article{osti_5209520,

  title        = {Activation of transforming potential of the human insulin receptor gene},

  author       = {Wang, L H and Lin, B and Jong, S M.J. and Dixon, D and Ellis, L and Roth, R A and Rutter, W J},

  abstractNote = {A retrovirus containing part of the human insulin receptor (hIR) gene was constructed by replacing ros sequences in the avian sarcoma virus UR2 with hIR cDNA sequences coding for 46 amino acids of the extracellular domain and the entire transmembrane and cytoplasmic domains of the ..beta.. subunit of hIR. The resulting virus, named UIR, contains the hIR sequence fused to the 5' portion of the UR2 gag gene coding for p19. UIR is capable of transforming chicken embryo fibroblasts and promoting formation of colonies in soft agar; however, it does not form tumors in vivo. A variant that arose from the parental UIR is capable of efficiently inducing sarcomas in vivo. UIR-transformed cells exhibit higher rates of glucose uptake and growth than normal cells. The 4-kilobase UIR genome codes for a membrane-associated, glycosylated gag-hIR fusion protein of 75 kDa designated P75/sup gag-hir/. P75/sup gag-hir/ contains a protein tyrosine kinase activity that is capable of undergoing autophosphorylation and of phosphorylating foreign substrates in vitro; it is phosphorylated at both serine and tyrosine residues in vivo},

  doi          = {10.1073/pnas.84.16.5725},

  url          = {https://www.osti.gov/biblio/5209520},
  journal      = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number       = ,

  volume       = 84:16,

  place        = {United States},

  year         = {Sat Aug 01 00:00:00 EDT 1987},

  month        = {Sat Aug 01 00:00:00 EDT 1987}

}

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