Immunoaffinity Profiling of Tyrosine Phosphorylation in Cancer Cells  

Oleh:

Rush, John ; Moritz, Albrecht ; Lee, Kimberly A. ; Guo, Ailan ; Goss, Valerie L. ; Spek, Erik J. ; Hui, Zhang ; Xiang-Ming, Zha ; Polakiewicz, Roberto D. ; Comb, Michael J.

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 23 no. 1 (Jan. 2005), page 94-101.
Topik: cells; immunoaffinity; tyrosine phosphorylation; cancer cells

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.2 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

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Isi artikel

Tyrosine kinases play a prominent role in human cancer, yet the oncogenic signaling pathways driwing cell proliferation and surviva have been difficult to identify in part because of low cellular levels of tyrosine phosphorylation. In general, global phosphoproteomic approaches reveal small numbers of peptides containing phosphotyrosine. We have developed a strategy that emphasizes the phosphotyrosine component of the phosphoproteome and identifies large numbers of tyorisune phosphorylation sites. Peptides containing phosphotyrosine are isolated directly from protease digested cellular protein extracts with a phosphotyrosine specific antibody and are identified by tandem mass spectometry. Applying this approach to several cell systems, including cancer cell lines, their phosphorylated substrates without prior knowledge of the signaling networks that are activated, a first step in profiling normal and oncogenic signaling networks.

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