Multicolor Monitoring of the Proteasome’s Catalytic Signature
| Autor: | Melanie A. Priestman, Finith E. Jernigan, Qunzhao Wang, Marion Schmidt, David S. Lawrence, Ruma Chowdhury |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Proteasome Endopeptidase Complex
Protein Folding Proteolysis Antigen presentation Saccharomyces cerevisiae Biochemistry Cell Line Small Molecule Libraries 03 medical and health sciences 0302 clinical medicine medicine Animals Humans 030304 developmental biology Fluorescent Dyes 0303 health sciences Chymotrypsin biology medicine.diagnostic_test Molecular Structure Active site General Medicine Articles biology.organism_classification Trypsin Proteasome Cell culture 030220 oncology & carcinogenesis biology.protein Molecular Medicine Rabbits medicine.drug |
| Zdroj: | ACS Chemical Biology |
| ISSN: | 1554-8937 1554-8929 |
| Popis: | The proteasome, a validated anticancer target, participates in an array of biochemical activities, which range from the proteolysis of defective proteins to antigen presentation. We report the preparation of biochemically and photophysically distinct green, red, and far-red real-time sensors designed to simultaneously monitor the proteasome’s chymotrypsin-, trypsin-, and caspase-like activities, respectively. These sensors were employed to assess the effect of simultaneous multiple active site catalysis on the kinetic properties of the individual subunits. Furthermore, we have found that the catalytic signature of the proteasome varies depending on the source, cell type, and disease state. Trypsin-like activity is more pronounced in yeast than in mammals, whereas chymotrypsin-like activity is the only activity detectable in B-cells (unlike other mammalian cells). Furthermore, chymotrypsin-like activity is more prominent in transformed B cells relative to their counterparts from healthy donors. |
| Databáze: | OpenAIRE |
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