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Tyrosine phosphorylation of an interleukin 2 receptor-like protein in cells transformed by human T cell leukemia virus type I

Three interleukin 2 (IL-2)-independent human T cell lines transformed with human T cell leukemia virus type I were analyzed for o- phosphotyrosine-containing proteins (Ptyr proteins). Membrane and intracellular immunofluorescence was positive with antibody to Ptyr (Ptyr antibody). 10 size classes of...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188586/
https://www.ncbi.nlm.nih.gov/pubmed/2435836
Descripción
Sumario:Three interleukin 2 (IL-2)-independent human T cell lines transformed with human T cell leukemia virus type I were analyzed for o- phosphotyrosine-containing proteins (Ptyr proteins). Membrane and intracellular immunofluorescence was positive with antibody to Ptyr (Ptyr antibody). 10 size classes of Ptyr proteins with molecular masses of 81-28 kD were isolated with Ptyr antibodies. Among these, proteins of 64 kD (pI 4.5 and 4.8-5.3) and 45 kD (pI 4.3) were found on the outer cell surface. The Ptyr protein of 64 kD (pI 4.5) had the characteristics of the IL-2 receptor (IL-2-R) in that it was recognized by two monoclonal antibodies directed against different epitopes on the IL-2-R.