Functional proteomics of the active cysteine protease content in Drosophila S2 cells.

Journal article

The fruit fly genome is characterized by an evolutionary expansion of proteases and immunity-related genes. In order to characterize the proteases that are active in a phagocytic Drosophila model cell line (S2 cells), we have applied a functional proteomics approach that allows simultaneous detection and identification of multiple protease species. DCG-04, a biotinylated, mechanism-based probe that covalently targets mammalian cysteine proteases of the papain family was found to detect Drosop...

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Authors: Kocks, C; Maehr, R; Overkleeft, H; Wang, E; Iyer, L

• Publication status: Published
• Journal: Molecular and cellular proteomics : MCP
• Volume: 2
• Issue: 11
• Pages: 1188-1197
• Publication date: 2003-11-01
• DOI: 10.1074/mcp.M300067-MCP200
• EISSN: 1535-9484
• ISSN: 1535-9476
• Language: English
• Keywords: Amino Acid Sequence; Biotin; Phagocytes; Spectrometry, Mass, Electrospray Ionization; Drosophila; Molecular Probes; Cysteine Endopeptidases; Animals; Cell Line; Electrophoresis, Polyacrylamide Gel; Cathepsins; Leucine; Mice; Lysosomes; Molecular Sequence Data; Drosophila Proteins